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A Summary of New Findings on the Biological Effects of Selenium in Selected Animal Species—A Critical Review

Bozena Hosnedlova, Marta Kepinska, Sylvie Skalickova and 8 more

International Journal of Molecular Sciences · 2017 · Review · CC BY

doi:10.3390/ijms18102209

Abstract

Selenium is an essential trace element important for many physiological processes, especially for the functions of immune and reproductive systems, metabolism of thyroid hormones, as well as antioxidant defense. Selenium deficiency is usually manifested by an increased incidence of retention of placenta, metritis, mastitis, aborts, lowering fertility and increased susceptibility to infections. In calves, lambs and kids, the selenium deficiency demonstrates by WMD (white muscle disease), in foals and donkey foals, it is associated with incidence of WMD and yellow fat disease, and in pigs it causes VESD (vitamin E/selenium deficiency) syndrome. The prevention of these health disorders can be achieved by an adequate selenium supplementation to the diet. The review summarizes the survey of knowledge on selenium, its biological significance in the organism, the impact of its deficiency in mammalian livestock (comparison of ruminants vs. non-ruminants, herbivore vs. omnivore) and possibilities of its peroral administration. The databases employed were as follows: Web of Science, PubMed, MEDLINE and Google Scholar.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 23, 2026. Paragraph numbers are ours, so an answer can point at one.

1. Methodology of the Review

This review is focused on the biochemical and molecular genetic nature of selenium, on its physiological effects in mammalian livestock, on the possibilities of determining its status in the organism and on the importance of its additon to animals. The methodology of the choice used scientific studies from more than 2500 viewed articles based on the search phrases, such as: physiological effects of selenium, antioxidant/antibacterial/anticancer effect of selenium, selenium and oxidative stress/Staphylococcus aureus/immunity/thyroid hormones/reproduction, fertility/milk/rumen fermentation/gastrointestinal tract, glutathione peroxidase, epigenetic effects of selenium, selenium status analysis, selenium and analytical methods, selenium and cattle/sheep/goats/pigs/horses/donkeys; and the main findings of various studies were compared.

2.1. Importance of Selenium for Animal Health

Selenium (Se) is an essential trace element that evinces antioxidant activity, anti-inflammatory, antimutagenic, anticarcinogenic or chemopreventive, antiviral, antibacterial, antifungal and antiparasitic effects. Furthermore, it is an integral component of selenoproteins participating in a whole series of physiologically important processes. The first proven selenoenzyme was glutathione peroxidase (GPx), which is an indispensable component of the antioxidant system in the organism. The selenoprotein family includes at least 25 eukaryotic proteins, whose expression is characterized by high tissue specificity, which depends on selenium availability and can be regulated by hormones. Selenoproteins contain in their active site selenium in the form of 21st amino acid selenocysteine. The incorporation of selenocysteine into selenoproteins utilizes an unique mechanism that requires decoding of the codon UGA in mRNA, normally involved in the termination of translation. The UGA recoding is strictly dependent on an RNA stem-loop structure, the selenocysteine insertion sequence (SECIS), which is found in the 3′ untranslated region (3′ UTR) of eukaryotic selenoprotein messages.

Selenium is important for the synthesis, metabolism and function of thyroid hormones, that are crucial regulators of development, growth and differentiation. In addition, they are also involved in many other physiological processes. Selenium is a component of enzymes deionidases, which are divided into three types (D1, D2 and D3) and have different tissue distribution, gene expression regulation and function. D1 is primarily expressed in liver, kidney and thyroid and is able to deiodinate thyroxine (T4). It is also essential to provide triiodothyronine (T3) for the circulation as well as serving as a scavenger enzyme for iodide in peripheral tissues. D2 is expressed in a large number of tissues, such as skeletal muscle, bone, pituitary, retina, cochlea, CNS, thyroid and brown adipose tissue and converts T4 into more active T3 by 5′-deiodination. In contrast, D3 inactivates T3 and, to a lesser extent, prevents T4 from being activated. The level of T3 in blood increases with higher selenium intake. The thyroid hormones, on the other side, affect directly the metabolism of selenium and its serum status as well as regulating the expression of some selenoproteins. The physiological significance of selenium is shown in Figure 1.

Selenium is also important for the regulation of immunity functions, plays an essential role in non-specific immune response and its low level is related to weakened immune system. In inflammatory diseases, the selenium concentration declines and the biosynthesis of selenoproteins is disturbed. The application of selenium decreases inflammatory activity. Selenium is very important for chemotactic and phagocyte activity and respiratory burst activities. Selenium deficiency leads to GPx enzyme activity decreasing and the drop in neutrophil activity as well as the cells becoming more susceptible to oxidative damage.

Selenium is involved in growth and development, as well as taking part in the regulation processes related with production, and reproduction abilities of animals.

2.2. Biochemical and Molecular Biological Activities of Selenium in Organism

Selenium is a metalloid with the atomic number 34 which belongs to the group 16 in the periodic table. It was discovered in 1817 by the Swedish chemist Jöns Jacob Berzelius. Selenium has six valence electrons, two of them being unpaired ([Ar]3d104s24p4). However, due to 4d orbitals, it is capable of formation of six covalent bonds. In oxygen-containing compounds it possesses +6, +4, and +2 oxidation states. With the majority of other elements, it forms binary compounds with an oxidation state of −2, e.g., in hydrogen selenide (H2Se) and organic selenides such as selenomethionine (SeMet).

2.2.1. Role of Selenium in Oxidative Stress

Up to now, many genes that are related to the antioxidant properties of selenium have been identified: SEPP1, SEP15, TRXNRD1–2, PRDX1–6, SELENBP1, CAT, GPx1,3,4, SOD1,2,3 (Figure 2A). The enzyme superoxide dismutase contributes to the reduction of oxidative stress by efficiently quenching the superoxide radical and converting it into less toxic hydrogen peroxide which the subsequent enzyme catalase (CAT) breaks down into water and oxygen to prevent DNA damage. In the case of reduced dietary intake of selenium and other antioxidants, its activity decreases and free radicals lead to the process of tumorigenesis. The cancer cells are shown to have increased reactive oxygen species (ROS) levels in comparison to their normal counterparts.

2.2.2. Relationship of Selenium to Cancer

Selenium exhibits toxicity against cancer cells. It was reported that selenite stimulates apoptosis in cultured cancer cells, showing greater toxicity towards malignant compared to benign cells. This also inhibits the development of mammary tumours in rat cells. The anticancer action mechanism of selenite is based on the induction cancer cell death and apoptosis by producing superoxide radicals especially in or adjacent to mitochondria. Superoxide radicals trigger the mitochondrial pathway of apoptosis. It was found that selenite-induced superoxide production, cell death, and apoptosis were inhibited by overexpression of manganese superoxide dismutase (MnSOD; SOD2). The levels of MnSOD in cancer cells may influence the efficacy of administered selenium in cancer chemoprevention. Since cancer cells usually have lower levels of MnSOD, they should be more sensitive to selenium than their normal cell counterparts. Therefore, in cancer prevention, selenium may be found to selectively induce apoptosis of cancer cells without causing significant damage to normal cells. Other researchers have also shown that selenite treatment damages mitochondria, leading to cell death.

With regards to other antioxidant enzymes, Xiang et al. found that overexpression of Cu/Zn-SOD (SOD1), CAT and GPx1, in contrast to SOD2, did not suppress apoptosis in selenite-treated prostate cancer cell, while Kim et al. reported that overexpression of SOD1 enhanced cell viability in malignant glioma cells exposed to selenite. The different effects of selenite on SOD1/2 expression, and SOD1/2 overexpression on selenite mediated cell death may be due to the multiple pathways by which selenite treatment induces ROS generation. Thus, a picture of the response of superoxide dismutases to selenite supplementation seems to be inconsistent.

The individual role of selenite, thioredoxin and the system of glutaredoxin and S-adenosylmethionine (SAM) in the redox cycle of selenium intermediate metabolites is shown in Figure 2B. The selenite is reduced to hydrogen selenide by thioredoxin, or glutaredoxin system. This reaction can also be catalysed by glutathione or cysteine to produce the same final products. Hydrogen selenide can be sequentially oxidized to a superoxide radical or undergo a redox cycle mediated by thioredoxin or the glutaredoxin system. Hydrogen selenide can spontaneously react with SAM to form methylselenol (CH3Se). Subsequently, the thioredoxin and glutaredoxin system participate in the redox cycle of methylselenol with hydrogen selenide and generate reactive oxygen species. Under reductive conditions, monomethylselenol can, thanks to its extraordinary nucleophilicity, be compared to its counterpart hydrogen selenide and act as a free radical scavenger.

2.2.3. Antioxidative Role of Selenium against the Toxic Effect of Heavy Metals

In the metabolic pathways of selenium, numerous proteins, including metallothioneins (MTs),, which play a role in heavy metal detoxification, are involved. The exposure to heavy metals, e.g., mercury (Hg) is often associated with the induction of metallothioneins. Intraperitoneal selenium administration to rats exposed to mercury resulted in a complete recovery of mercury-altered levels of oxidative stress parameters, to returning of the mercury-induced mRNA expression levels of MT-I (metallothionein-I) and MT-II (metallothionein-II) in the liver to their original state, and had also partial protective effect on the kidneys. Selenium is considered to be an antidote in the treatment of mercury intoxication, it may modulate Hg toxicity through the influence on Hg deposition in tissues, as well as Hg-induced oxidative stress, inflammation, excitotoxicity, and other pathways. Studies by Orct et al. demonstrated the protective effect of selenium on oxidative lipid damage in the brain, which is extremely sensitive to mercury during the early postnatal period. Severe selenium deficiency causes irreversible brain injury. Experimental data demonstrate that selenium treatment modifies brain mercury retention, and modulates neurotoxicity and oxidative stress in the nervous tissue of animals. Selenium counteracts the neurotoxicity of mercury presumably through the formation of nontoxic complexes. The circulating selenium transporter, selenoprotein P (SEPP), appears to have a special role in the delivery of selenium to the brain and neurons by entering via the multifunctional apolipoprotein E receptor 2 (ApoER2), a member of the lipoprotein-receptor family that is expressed in neurons in the brain.

A protective effect of selenium was also reported against toxicity of other heavy metals, such as chromium (against chromium-induced oxidative and cellular damage in thyroid gland, chromium toxicity in the brain and chromium-induced nephrotoxicity), cadmium (the protection of jejunal epithelial cells from cadmium-induced DNA damage, an antagonistic effect of selenium on cadmium-induced damage of kidney, ameliorative effect against cadmium chloride-induced neuro- and nephrotoxicity), and lead (against lead toxicity on the antioxidant system), or also overabundance of iron. Selenium reduces the adverse impacts of excess iron intake. Iron is important for many biological processes, it is distributed to the cells bound to serum protein transferrin and the iron transport into the cells takes place via the internalization of the transferrin bound to the transferrin receptor. The expression of the transferrin and ferritin genes is strictly regulated by the iron responsive element (IRE) and the iron regulatory protein (IRP). Free iron generates ROS that damage lipids, proteins and DNA. Chronic iron excess was associated with a decrease in selenium concentration and GPx activity in the heart tissue in mice, and the addition of Na2SeO3 to mice reduced the concentration of iron in the heart tissue and oxidative stress.

2.2.4. Epigenetic Effects of Selenium and Their Implications for Prevention of Carcinogenic Process

Selenium has been found to modify epigenetic marks—mitotically stable chromatin-based mechanisms that modulate gene expression without altering the genomic DNA sequence. These mechanisms include modifications to DNA and to histones (acetylation, methylation and many others), which interfere with chromosomal packaging and the binding of trans-acting factors. Changes in the epigenome are associated with a great variety of diseases, including also inflammatory disease or the onset and progression of carcinogenic process.

The role of selenium for health is based on its biological functions that are presented by the members of the selenoprotein family encoded by more than tens of genes and containing cotranslationally inserted selenocysteine. It is also a non-selenoprotein pool of low-molecular-weight selenium compounds contained in the diet or derived from selenium metabolism. The importance of selenoproteins for development and health has been clearly demonstrated in transgenic mice with single or total selenoprotein depletion.

Research studies performed on rats, mice and cell lines have shown that selenium intake affect global DNA methylation. However, the rodent studies gave inconsistent results regarding an increase or decrease of global DNA methylation in response to dietary selenium.

In mouse embryonic stem cells (ESCs), after their exposure to selenium, was found a reversible alteration of the cell heterochromatin status and also the changed DNA methylation status of genes with crucial roles in fetal development, such as Aebp2 (AE binding protein 2), Prickle2 (prickle homolog 2) and Rnd2 (Rho family GTPase 2), without compromising cellular potential for embryonic development. This implies that the genes with various functions regulated by DNA methylation are affected in ESCs as an in vitro model for early embryos.

Selenium deficiency resulted in less DNA methylation in rat liver and colon in contrast to the later study, that found significantly less global liver genomic DNA methylation in rats with supranutritional dose of selenium than those fed with selenium-deficient diet. These differences could be due to various rat inbred strains and selenium content of the basal diets as potential modifiers of selenium effects. Another possibility to influence the differences is using various techniques applied for the assessment of global DNA methylation.

Besides of global genomic DNA methylation, the regulation of site-specific DNA methylation of tumor suppressor genes is important and it has been considered as a leading mechanism by which some nutrients exert their anticancer property. Alterations in DNA methylation, which are associated with DNA methyltransferase abnormalities and result in silencing of tumor-related genes and chromosomal instability, are involved in precancerous changes in various organs. The study whether selenium affects the methylation of the p53 gene was investigated, and it was found that supranutritional dose of selenium significantly increased the exon-specific DNA methylation of the p53 gene (in exons 5–8) in liver and colon mucosa of rats compared with this in animals fed with the selenium-deficient diet.

Selenium has been shown to be associated with changes to histone marks. Interference of selenium with histone marks can principally occur through modulation of histone modifying enzyme activity/expression and via interference with substrate availability. In consideration of the large variety of marks and participating enzymes, the situation is even more complex than for DNA methylation; moreover crosstalks exist between DNA methylation and histone marks, thus a complicated network of epigenetic regulation is formed. The abnormal function and/or expression of histone deacetylases (HDACs) is linked to cancer and some neurologic and immune disorders. Numerous synthetic HDAC inhibitors have been developed and are currently tested in clinical trials. Studies have confirmed that dietary and synthetic selenocompounds inhibit HDAC activity.

Selenium also affects the microRNA (miRNA) expression. The regulation of gene expression by targeting of mRNA through non-coding RNA molecules such as miRNA is considered an additional epigenetic mechanism. Microarray analysis (comprising of 737 miRNAs in total) of the miRNA profiles of Caco-2 cells grown in selenium-deficient or selenium-supplemented medium revealed that the expression of 12 miRNAs was affected by selenium supply. Expression levels of 50 mRNAs were also selenium-responsive, and numerous of the mRNAs were predicted to be targeted by the selenium-responsive miRNAs. One of these, miRNA-185, whose expression decreased under selenium deficiency, was confirmed to regulate expression of glutathione peroxidase 2 (GPx2) and selenophosphate synthetase 2 (SPS-2) genes. As the protein product of SPS-2 is component of the selenoprotein biosynthesis process, it indicates that selenium intake affects the selenoproteome in part through epigenetic mechanisms involving miRNA-185 and possibly also other miRNAs. miRNA-185 is an especially interesting target of selenium, because it has been recently introduced as a tumor suppressor that is often downregulated in various type of cancer.

Finally, selenium has been shown to act anticarcinogenic in various epigenetic studies, but the research of the detailed role in cancerogenic process is still in its infancy, it still requires a lot of experimental studies in the future, especially it will be very interesting to reveal the role of miRNAs as mediators of selenium-dependent tumor protection against malignant transformation.

2.3.1. Described Diseases Associated with Selenium Deficiency

Many selenium deficiency diseases are often referred to the lack of another important nutrient with antioxidant function such as vitamin E. The variety of the antioxidant defense system components of the body allows it to profit from different types of antioxidants. This is especially known in these two nutrients in the etiology of certain diseases in which a nutrition deprivation of either one or the other can be asymptomatic, whereas the deficiency of both causes the disease. For example, animals fed with low-selenium diets commonly require higher amounts of vitamin E than animals sufficiently supplemented with selenium. In addition to their joint involvement in the antioxidant system, the presence of both for the proper function of the immune system and resistance against infections is just as important.

The known manifestation of selenium deficiency in calves, lambs, kids, foals and donkey foals is white muscle disease (WMD) or nutritional muscular dystrophy (NMD). The disease can be also caused by the lack of vitamin E or a combined lack of selenium and vitamin E. The clinical symptoms include stiffness, weakness and recumbency. The disease involves hyaline degeneration of muscle cells in various skeletal muscles, including the diaphragm and the heart. In ruminants, WMD is also manifested by changes in the frequency and quality of heartbeat. In lambs with WMD, the arrhythmia was diagnosed using electrocardiography (ECG). The arrhythmia is observed at early stages of cardiomyopathy. The electrocardiograms of diseased calves revealed elevated heart rate, accelerated sinus rhythm, increased P wave amplitude, shorter PR, QT and ST interval, narrower QRS complex, shorter T wave duration and insignificantly increased T wave amplitude.

The deficiency of selenium and vitamin E in horses and donkeys caused a yellow fat disease or steatitis, provoking the degeneration of the adipose tissue that is replaced by connective tissue and calcium deposits, and can be associated with dystrophic myodegeneration (white muscle disease). The symptoms are inertia, recumbency, decreased appetite, weight loss, fever, ventral oedema, stiff gait and painful neck. It is also very common to find low hematocrit, decreased selenium and vitamin E concentrations as well as elevated levels of creatine kinase and lactate dehydrogenase.

In pigs, the deficiencies of selenium and vitamin E caused the so-called VESD (vitamin E/selenium deficiency) syndrome, of which the most frequent manifestation is mulberry heart disease, which also included hepatosis dietetica and nutritional myopathy.

2.3.2. Effect of Selenium on Female Reproduction

The selenium administration in selenium-deficient cows can reduce the number of services per conception, improve the pregnancy rates at first service and result in fewer days to conception. The increase of selenium concentration prepartum in blood correlates with anoestrus/silent oestrus decreasing postpartum. The selenium deficiency caused abortions and stillborn. Giadinis et al. reported that the selenium deficiency in grazing beef cattle was the sole cause of abortion in cows. The findings of lesions on fetal heart and skeletal muscle were consistent with WMD. The most probable mechanism of the abortifacient effect of selenium deficiency is, among others, fetal heart failure. Another mechanism could be an insufficient progesterone concentration required to maintain the pregnancy in the late gestation. The administration with selenium to pregnant cows contributes to adequate progesterone secretion and also promotes its postpartum production.

The selenium and vitamin E administration reduces the incidence of retained placenta. Selenium also has an effect on the decrease in the incidence of metritis and ovarian cysts. The significant increase in the expression of the glutathione peroxidase 1 gene (GPx1) in granulosa cells of healthy follicles points to antioxidant role of GPx1 during the ovarian follicular development.

2.3.3. Effect of Selenium on Male Reproduction

Antioxidant protection plays a key role in maintaining the integrity of the sperm membrane and their fertilizing ability. Selenium involved in the antioxidant defense of the organism substantially modulates the quality of the male ejaculate. In testes, several selenoproteins such as selenophosphate synthase (SPS-2) and mitochondrial capsule selenoprotein (MCSeP) were localized. Oxidative stress (OS) is an important factor that negatively affects the fertility potential of spermatozoa by lipid peroxidation. Sperm plasma membrane is extremely susceptible to lipid peroxidation due to the presence of high concentration of polyunsaturated fatty acids (PUFAs). Those PUFAs give to the membrane a high level of fluidity and elasticity necessary for sperm motility and their fusion with oocytes. Lipid peroxidation can lead to loss of membrane fluidity and integrity, and thus to reducing of sperm-oocyte fusion ability. The number of spermatozoa and their motility are fundamental indicators of sperm functional ability.

Under physiological conditions, ROS are key for sperm function. In small amounts, they are necessary for fertilization, acrosomal reaction, hyperactivity, motility and capacitation. Under pathological conditions, however, excessive ROS levels may negatively affect their quality. Spermatozoa, as cells living in aerobic conditions, face an oxygen paradox: O2 is vital for them, but its metabolites, such as ROS, can alter sperm functions and endanger their survival. ROS cause an infertility with two key mechanisms. Besides sperm membrane damage, which results in decreased sperm motility and their ability to fuse with oocytes, they can also damage sperm DNA, leading to the transmission of defective paternal DNA to fetus. ROS may attack DNA by modification of nitrogenous bases, DNA strand breaks, DNA cross-links, and chromosomal rearrangements.

One of the markers of oxidative stress are the TBARS (thiobarbituric acid reactive substances), of which the most widely used is malondialdehyde (MDA), the product of aldehydic lipid peroxidation generated by the action of ROS on membrane lipids. MDA is one of the reactive and mutagenic aldehydic lipid peroxidation products in seminal plasma, and can be considered as a diagnostic tool in male infertility. Breininger et al. found a high negative correlation between TBARS and sperm motility in boars. An increased level of MDA in stored boar semen was associated with a rapid loss of motility and integrity of the plasma membrane of spermatozoa. The reduction of motility may be due to ROS-induced impairment of ATP (adenosine triphosphate) utilization or contractile apparatus of the sperm flagella.

Reference values for MDA and other oxidative stress parameters in mammalian livestock are shown in Appendix Table A1.

2.3.4. Effect of Selenium on Reduction of Intramammary Infection and Milk Quality

Selenium deficiency is also associated with an increased incidence of mastitis. Dietary intake of selenium and vitamin E reduces their incidence. The primary defense mechanism against mastitis is the phagocytic activity of neutrophils. In dairy cows with selenium deficiency, the phagocytic ability of the blood and neutrophils decreased. Selenium affects the innate and the adaptive immune responses of the mammary gland through humoral and cellular activities. The dietary selenium intake at the dose of ≥4 mg∙day−1 prepartum was negatively associated with the likelihood of bovine intramammary infections due to coagulase-negative staphylococci. The higher content of selenium in bulk milk tank samples was linked with the lower risk of Staphylococcus aureus-positive herd. Increasing bulk tank milk selenium by 0.2 μmol∙L−1 reduced the odds by a factor of 0.95. The effect of selenium on mammary pathogens is mediated by several mechanisms: a faster and more massive influx of polymorphonuclear leucocytes (PMN) into the udder, the more effective killing of bacteria (such as S. aureus) by PMN, high antibacterial activity of whey inhibiting growth of S. aureus and high expression of selenoproteins with antioxidant properties in the mammary gland.

The administration of selenium to heifers and cows before calving reduced the prevalence of intramammary infections and high somatic cell count (SCC) during early lactation. Injection application of Se together with Zn, Mn and Cu had a positive impact on reductions of somatic cell scores (SCSs) and mastitis incidences. In goats, that were administered with selenium and vitamin E, significantly lower somatic cell counts were observed compared to the control group.

The dietary addition of selenium increases the selenium concentration and the percentage of favourable PUFAs and cis-9, cis-12 linoleic acid in cow’s milk. In milk, most of the selenium is present in whey (47.2–73.6%) and least in the fat-phase of milk (4.8–16.2%). The dietary addition of selenium along with vitamin E increased the percentage of crude protein and lactose.

2.3.5. Effect of Selenium on Rumen Fermentation

Selenium can influence rumen microbial fermentation. Administration of SeMet increased in vitro production of short-chain fatty acids (SCFAs) by rumen microflora. On the contrary, the effects of selenite and elemental selenium on the increasing amounts of these acids were not significant. The fermentation rate was faster in the presence of SeMet when compared to elemental selenium and selenite; the plateau of fermentation of SeMet was reached within 30 h, whereas for other two mineral forms it was not reached until at least 36 h. The ratio of acetate:propionate:butyrate was differently according to the selenium source. In the presence of SeMet, the increased proportion of acetate was observed, which could be explained by the probable utilization of SeMet by rumen bacteria as an energy source. In case of limiting carbohydrate sources, proteins are degraded to NH3, amines, gas and SCFAs, and acetate predominantly produces fatty acids. In the presence of selenite, there was found contrarily the increased proportion of butyrate.

Rumen microorganisms alter the bioavailability of received selenium. Selenite or selenate delivery to ewes decreased whole blood and serum selenium concentrations compared with ewes receiving the same selenium dosage in form of SeMet as Se yeast. Incorporation of selenium into microbial biomass was ex vivo greater for SeMet (13.2-fold higher than for control group) compared with inorganic selenium addition (selenite, selenate). A large amount of amino acids, which are released by microbial proteolysis in the rumen, are re-utilized for microbial protein synthesis. SeMet is not absorbed in situ to any appreciable extent in the rumen. Bacteria reduce selenate (SeO42−) through selenite (SeO32−) to elemental Se (Se0). Selenium can also become incorporated into proteins as part of the amino acids selenocysteine (SeCys) or SeMet. This occurs as a result of the reduction of selenite with reduced glutathione to make selenodiglutathione, which is subsequently reduced to glutathioselenol (GS-SeH), which is further reduced to hydrogen selenide (H2Se) providing the necessary reactive intermediates for selenium incorporation into amino acids, or further reduction to elemental selenium. When a high selenium diet is administered to beef cattle, the number of selenium-reducing microorganisms increases.

Dietary supplement of selenized yeast at the dose of 150–300 mg∙kg−1 (which provided 0.15‒0.30 mg Se∙kg−1) of feed dry matter to cows increased the volatile fatty acid (VFA) concentration and altered the rumen fermentation towards higher propionate production compared with the control group. The dose of about 300 mg∙kg−1 of dry matter of food stimulated the digestive microorganisms and enzymes [higher digestibilities of dry matter, organic matter, crude protein, ether extract, aNDF (amylase-treated neutral detergent fiber) and ADF (acid detergent fiber) in the total tract compared to the control group.

Supplementation of selenium to sheep influences the development of some ciliates: the use of selenized yeast has a more pronounced effect on Ophryoscolex and Diploplastron populations than the equivalent amount of sodium selenite. The first-mentioned genus is the most sensitive to selenium in the diet, and in sheep with its deficient intake it is not even found. The selenium form also affects the enzymatic activity in the rumen fluid of the sheep. GGT (gamma-glutamyl transferase) and GDH (glutamate dehydrogenase) activities were significantly higher after administration of selenized yeast, AST (aspartate aminotransferase) and ALP (alkaline phosphatase) than when sodium selenite was used.

2.3.6. Effect of Selenium on Hair Production

Selenium intake is important for the bioactivity of IGF-1 (insulin-like growth factor 1), which stimulates the proliferation, migration and morphogenesis of hair follicle cells through specific cell-surface receptors (IGF-1 receptor, IGF-1R) during ontogenetic development. IGF-1 represents peptide hormone produced in the liver, which is formed as a consequence of growth hormone (GH) release from the pituitary gland, which stimulates subsequently IGF-1 production in the liver. IGF-1 is therefore a mediator for some of the GH functions, thus involved in growth and anabolism. IGF-1 mediates its effects by binding at the specific receptor.

Wu et al. reported that selenium administration to pregnant goats increases the antioxidant defense of fetal skin and improves the growth and development of fetuses and the development of their hair follicles by up-regulating IGF-1.

The growth of hair is a cyclic process in which every follicle proceeds from an active phase (anagen) through a regression phase (catagen) to a resting phase (telogen). During catagen, hair follicles undergo apoptosis and there is a decline in the level of an anti-apoptotic protein Bcl-2, and an increase in a pro-apoptotic protein Bax. The effect of IGF-1 on hair growth appears to be related to the upregulation of PDGF-A and PDGF-B and to the anti-apoptotic effect of IGF-1 (Figure 3). IGF-1 stimulates hair follicle growth, maintains the anagen stage and postpones the catagen stage by increasing the expression of the platelet-derived growth factors (PDGF-A, PDGF-B) as well as the expression ratio of Bcl-2/Bax. PDGF is a potent mitogen produced in a variety of cell types including keratinocytes and endothelial cells, and is important for cell growth.

IGF-1 activates two signaling pathways: (1) the extracellular signal related kinase/mitogen activated kinase pathway and (2) the phosphatidylinositol 3′-kinase/protein kinase B (PI3K/Akt) pathway. To exert its biological effects, IGF-1 must activate cells by binding to specific cell-surface receptors. The type I IGF receptor (IGF-1R) is the only IGF receptor to have IGF mediated signaling functions. IGF-1 is produced by mesenchymal type cells and acts in a paracrine fashion and/or an autocrine fashion by binding to the IGF-1R. This binding activates the receptor tyrosine kinase that triggers the downstream responses and finally stimulates cell division. IGF-1 may therefore be able to stimulate the proliferation of hair follicle cells through cellular signaling pathways of its receptors.

An in vitro study showed a significant difference in cumulative hair follicle elongation between the control group (0.97 ± 0.09 mm) and the 10−7 M IGF-1 treated hair follicles (1.24 ± 0.09 mm) over a period of 12 days. On the 2nd day, the IGF-1 treated group showed more prominent expression of PDGF-A, and PDGF-B also showed a significant increase in expression. Among the apoptosis related molecules, Bax and Bcl-2 showed differences in expression. On the 8th day, Bax was weakly expressed in the IGF-1 treated group. On the 2nd day, Bcl-2 was more strongly expressed in the IGF-1 treated group compared with the control group.

3.1. Selenium Status Assessment

The selenium status in the organism can be evaluated directly based on the determination of selenium content, or using the indirect method—based on the activity of selenium-dependent glutathione peroxidase. The reference values (RVs) are given in Appendix Table A1.

3.2. Total Selenium Concentration

The status of selenium can be assessed based on its content in blood, urine, tissues, excrements, and in lactating females in milk. Selenium content is usually detected by hydride generation-atomic absorption spectrometry (HG-AAS). The HG-AAS method can be used to determine the content of selenium in whole blood, blood plasma, serum and also in tissues (e.g., liver, skeletal muscle, myocardium, kidneys). For all these samples (taken from cows) after wet mineralization using HNO3 and H2O2 and subsequent reduction by HCl, the detection limit (around 0.8 μg∙L−1) and the measurement errors (4.6–15%) of this method corresponded to the requirements for use in research and clinic as well as preventive veterinary medicine.

The selenium concentration in whole blood and milk can also be determined by the ICP-MS method (inductively coupled plasma-mass spectrometry), which enables to determine the absolutely accurate concentration of the chemical element in samples compared to AAS, which is contrarily suitable for routine analysis with lower cost. The ICP-MS method is also usable for analyzing the total amount of selenium in feed samples, urine and faeces.

Selenium can be also analysed using ICP-OES (inductively coupled plasma-optical emission spectrometry), specially serum selenium as well as analysing the selenium content in diet and tissue of muscle. This method is considered to be less sensitive than ICP-MS. The fluorometric method has been succesfully employed to analyse selenium in feed, excrements, blood and tissues. The FIA-GF-AAS (flow injection analysis-graphite furnace-atomic absorption spectrometry) system coupled with a hydride generation has been utilised to detect selenium in plasma and spleen samples. VG-ICP-MS (vapor generation-inductively coupled plasma-mass spectrometry) has also been used as an analytical tool to analyse selenium content in feed, milk and whole blood.

The mere knowledge of the total concentration of the element in biological materials is not sufficient for the evaluation of its effects, it is also necessary to know the distribution between individual binding forms—species. Data on the concentration of individual selenium species are obtained in the speciation analysis process, which is usually performed by the combination of separation methods and trace element analysis methods.

Selenium species are most commonly detected by the combination of liquid chromatography (LC) and ICP-MS—LC-ICP-MS, or the HPLC-ICP-MS. HPLC (high-performance liquid chromatography) is also usable for detecting selenium species in plant feed. Speciation selenium analysis is most often performed at the level of individual seleno-amino acids and other low-molecular substances: selenite (Se+IV), selenate (Se+VI), selenomethionine (SeMet), selenocystine (SeCys2), Se-methylselenocysteine (MeSeCys) and others, which are released into the solution by enzymatic hydrolysis by non-specific proteases. Separation of these substances is performed by various LC modes, in particular ion exchange chromatography (IEC), and reversed-phase chromatography (RPC).

Serum or plasma selenium concentrations more accurately reflect the current level of supplementation and are more sensitive to short-term changes in selenium administration than its whole blood level, reflecting more of its earlier supplementation because selenium (in glutathione peroxidase) is incorporated into erythrocytes during their formation (erythropoiesis). The whole blood selenium responds slowerly to changes in supplementation (with supplementation increases more slowly, without supplementation decreases more slowly than serum or plasma selenium levels).

Although different methods are used to determine the selenium content in blood, they seem to be comparable, e.g., the detection limit in ICP methods is similar to that of fluorometric method using 2,3-aminonaphthalene, in an interlaboratory study the mean concentration of selenium in the blood in cattle using a fluorometrical analysis was similar to that of HG-AAS method. However, the concentration of selenium varies according to the sample type, there are the differences in its content in whole blood, serum and plasma.

When HG-AAG and inductively coupled argon plasma emission spectroscopy using hydride generation (ICP) are compared, a relatively similar correlation coefficient between the content of selenium in whole blood and serum in cattle was found to be: 0.79 (r2 = 0.62) for HG-AAS, and 0.88 for ICP (r2 = 0.77 (simple linear regression model), and adjusted R2 = 0.82 (expanded regression model)). However, the prediction intervals were relatively wide and the diagnostic accuracy for estimating blood selenium concentration based on its serum level is therefore very limited. For example at serum values of 0.01–0.05 μg∙mL−1, the predicted selenium concentration in blood ranged from a significant deficiency (<0.05 μg∙mL−1) to a normal value (>0.10 μg∙mL−1). Measurement of serum selenium level may not indicate whether blood selenium is within the reference range or at toxicity level. For diagnostic and clinical use, serum selenium levels must allow to distinguish normal selenium status from its deficiency. Approximately 67% of the normal distribution of the population could use the ratio blood selenium:serum selenium of 1.6–3.4:1 for data obtained from HG-AAG, and 1.1–3.4:1 for ICP. Practical use of these ratios for diagnostic purposes, whether blood selenium is in the reference range or deficiency range, is not appropriate. This fact cannot be determined based on serum selenium concentrations. The reason for the failure of this methodology is probably the variability of the hemolysis rate between the samples, and as a result of this, selenium releases from the erythrocytes into serum. Thus, a short-term change in selenium intake in the diet, reflected in blood serum but not yet in the erythrocyte selenium concentration (incorporation of selenium into erythrocytes lasts from days to weeks). In addition, genetic variability could influence selenium metabolism and the relationship between selenium in serum and blood.

The concentration of selenium in blood or serum is influenced by the selenium content in the diet and by form of received selenium. The content of selenium in blood also differs according to the breed—Jovanović et al. vs. Pavlata et al. (Appendix Table A1), sex and the age of the animal as well as geographical area, which is related to the selenium content in the soil and thus also in plants. Generally, most soils in many countries are poor in selenium, sometimes even below 0.2 mg∙kg−1. The soil selenium concentration depends on soil-climate interactions. The low-selenium soils are most likely to occur in arid regions and in areas with high pH and low clay content. Conversely, the areas with low to moderate precipitation but relatively low aridity (e.g., cool and moist climates) and high clay content are likely to have higher soil selenium concentrations. In addition to the total soil selenium content, soil physical-chemical conditions are also important, because can cause lower bioavailability of selenium and thus its lower uptake by plants, which can ultimately lead to its deficiency in animals. For example, the negative influence of sulfate (SO42−) and phosphate (PO43−) has been recently described. The selenium bioavailability in soil is influenced also by the presence of organic acids, important components founded in the rhizosphere soil.

The reference values of selenium (Appendix Table A1) in blood are different depending on the species and age of the animal, but also according to the used author’s methodology, for example Constable et al. stated a range of 0.08–0.30 μg∙mL−1 for blood serum in adult cattle, while Stowe and Herdt published a 3-fold lower upper limit (100 ng∙mL−1). However, many authors use the value of the lower limit of RV, according to different publications, ranging from 50 to 100 μg∙L−1.

3.3. Enzymatic Methods of Assessment of Selenium Status

Besides the direct detection of selenium status by determining its concentration in blood, an indirect method based on glutathione peroxidase activity assessment can be used. Approximately 11.8% of total selenium in the body is bound to this protein. GPx contains, with the exception of phospholipid-hydroperoxide GPx (PHGPx), which is monomeric, four selenium atoms and positively correlates with the amount of selenium in blood. The high correlation coefficient between selenium and GPx activity in whole blood was found to be r = 0.82, r = 0.93, r = 0.97, respectively. Despite this significant correlation between these parameters, the relationship between their values reported in various publications is often very inconsistent, e.g., Hogan et al. presented a blood selenium value in cows of 270 μg∙L−1 and a corresponding GPx activity of 80 IU∙L−1, while Ellison reported a concentration of 19.75 μg∙L−1 selenium and GPx activity of 2000 IU∙L−1 as the lower limit of the physiological range.

GPx activity depends on selenium content in the diet and is positively correlated with the selenium intake. This is due to the fact that most of the glutathione peroxidases (GPxs) (GPx1, GPx2, GPx3 and GPx4) contain selenocysteine at their catalytic site and therefore the activity of these enzymes is dependent on the accessibility of selenium. Thus, the measurement of seleno-dependent glutathione peroxidase activity (SeGPx) in blood is a widely used indicator of selenium status, antioxidative status and potential, as well as a parameter for evaluating the response to its therapeutic administration. However, GPx activity response to dietary selenium intake is very inconsistent in various studies. Although GPx activity is a useful biomarker of selenium status for a particular individual, substantial heterogeneity can be observed in various publications. Appendix Table A1 also shows a considerable variability in values. This is due to the use of various measurement units and, in particular, by a wide variety of analytical methods used. The authors do not indicate enzymatic activity in blood only in μkat∙L−1 of whole blood, but also in μmol∙g−1 of hemoglobin (Hb), U∙g−1 of hemoglobin, mmol∙L−1 of serum, IU∙L−1 serum, U∙mL−1 of serum. There is a vast variety of other reference units found in the literature such as: IU∙L−1 of whole blood, IU∙mL−1 PCV (packed cell volume), per mg of blood plasma protein, mg of hemoglobin, mL of whole blood as well as mL of blood plasma. Different units appeared even at defined reference limits in various countries, the activity value also depends on the chosen method of calculation (linear vs. polynomial regression): RV for sheep bred in Iran 191.67–196.52 U∙g−1 of Hb vs. in the Czech Republic >637 μkat∙L−1 (LR), resp. 677 μkat∙L−1 (PR) of whole blood. For this reason, literary data can usually not be compared. The individual methods of analysis differ in different reaction temperatures in vitro and in the use of various anticoagulants. The evident differences in RV determination are even reflected within the same author for one animal species in the same state (RV for GPx activity in cattle in the Czech Republic: 472.20–665.40 vs. 760.23 μkat∙L−1 of whole blood). According to Esworthy et al., a quantitative determination of protein or DNA content for the standardization of analytical data used to express GPx enzymatic activity, is necessary.

The interpretation of GPx activity values is also affected by the stage of reproductive cycle of the animal (e.g., estrous cycle phase, pregnancy) and the selected reference unit. Different SeGPx activity profiles per mg of hemoglobin vs. mL of whole blood, or per mL of blood plasma vs. mg of blood plasma protein during peri-oestrus period in sows reflect metabolic changes induced by the ovulation process and with this associated conditions for oxidative stress, which can play a role in the change of enzymatic activities. Likewise, different SeGPx profiles were obtained (mL of blood plasma vs. blood plasma protein—expressed per unit of blood plasma protein) in sows during early gestation. This is probably due to a decrease in blood plasma protein concentration during the first month of gestation, most likely due to a decrease in plasma albumin concentration.

It follows from the above that while for the lower limit of the physiological range of selenium in whole blood of cattle a more uniform standard is used (50–100 μg∙L−1), the unified reference limit for GPx activity practically does not exist. Lacking standardization in determining GPx activity and interpretation of results leads to the study of this issue. It is recommended that each laboratory establishes its own regression equation.

GPx activity in serum or whole blood shows a similar time relation, with regard to supplementation, as selenium level (in serum vs. whole blood), i.e., serum activity reflects short-term supplementation and whole blood activity of previous supplementation levels. Approximately 98% of GPx activity in peripheral blood is associated with erythrocytes and about 73% of selenium in blood is contained in the cellular component of the blood. The life span of erythrocytes in adult cattle is approximately 160 days. Bovine erythrocytes contain only selenium-dependent GPx activity, therefore selenium concentrations in blood or erythrocytes and GPx activity in blood or erythrocytes are excellent indicators of long-term selenium status in cattle.

Dalto et al. observed that SeGPx activity response in blood plasma on selenium supplementation during the peri-oestrus period was more pronounced under similar experimental conditions than in whole blood. Such influence of blood fractions cannot be seen in long-term profiles of SeGPx activity, SeGPx in blood plasma is therefore a better indicator of acute response to oxidative stress. The main metabolic changes induced by the physiological state of the animal may play an important role in the homeostasis of this enzyme.

The SeGPx activity value also depends on the estrous phase of females. In the longer term, it affects the SeGPx activity as well as the level of vitamin B6, which plays a central role in amino acid metabolism. B6-dependent enzymes catalyze most reactions of the transsulfuration pathways, ensuring the conversion of homocysteine to cysteine and further into GPx proteins. Because mammals metabolize sulfur- and seleno-amino acids similarly, vitamin B6 plays an important role in the fate of sulfur-homocysteine and its selenium counterpart between transsulfuration and one-carbon metabolism, especially in conditions of oxidative stress. This is extremely important in reproduction because ovarian metabolism can generate excessive amounts of ROS during a peri-estrus period that can disturb ovarian function and early embryo development. At a later stage of gestation, placentation increases embryo oxygen tension and may cause higher expression of ROS markers and lead to embryo death. Metabolic accumulation ROS surprisingly positively regulates the flow of one-carbon units to transsulfuration and negatively regulates remethylation. However, in the embryos, the transsulfuration pathway is not functional.

The GPx activity in samples is most often measured by the method of Paglia and Valentine—() (Appendix Table A1), which is based on the measurement of the decrease in light absorbance at 340 nm after oxidation of glutathione by cumene hydroperoxide catalyzed by glutathione peroxidase.

Besides the detection of GPx activity in various tissues and organs (whole blood, serum, liver, testes, skin), various types of this enzyme [(erythrocyte GPx, GPx1, GPx3, GPx4 (Appendix Table A1)] are also detected. The clinical relevance of determining the activity of different types of GPx in various tissues is very different. As a selenium status marker, glutathione peroxidase 3 (GPx3), a glycosylated protein secreted to extracellular compartments, is also often used as a selenium status marker. It uses a wide range of substrates—H2O2, fatty acid hydroperoxides and phospholipid hydroperoxidases, and is an effective antioxidant of blood plasma.

The activity of erythrocyte GPx in sheep is the dominating component (97.3%) of whole blood GPx activity; on the contrary, the proportion of serum GPx3 activity (2.7%) has a very low significance.

Cellular GPx (GPx1) and extracellular GPx (GPx3) are expressed in the liver, heart, placenta, gastrointestinal tract (GIT), thyroid gland, kidneys and erythrocytes in many species, including human, rat and mouse. GPx1 and GPx3 are also expressed in bovine mammary epithelial cells. In addition to GPx1 and GPx3, GPx4 mRNA was also detected in bovine mammary tissue. Enzyme GPx2 is found primarily in the GIT, on the contrary, in the mammary gland, its amount is very low.

4.1. Intake Recommendations for Selenium in Animals

An adequate dietary selenium intake helps to prevent disease caused by its deficiency, prevents the accumulation of lipid hydroperoxides in organs and tissues and thus protects them from damage by ROS. The daily recommended dose of selenium for the animals is shown in Table 1. When determining the dose, the presence of some other food components that antagonize selenium, e.g., sulfur (S), should be taken into account. Higher dietary sulfur intake reduces plasma selenium concentration and its bioavailability in the organism. Other antagonistic relationships have been described between selenium and other essential or toxic elements: As, Cu, Ni, Co, Cr, Mn, Zn, Cd, Sn, Pb, Hg, Bi, Mo, Ag, Au.

4.2. Dietary Forms of Selenium

Besides traditional forms of selenium—inorganic (selenite, selenate), organic (selenomethionine, dimethylselenide, and others), in the form of selenized yeasts or selenium bound to Chlorella algae biomass, the use of its nanoform, which substantially increases its biological utilization in the organism, has recently come to the forefront of interest.

5. Conclusions

Selenium is an important essential element that interferes through selenoproteins in many physiological processes of the organism and affects the production and reproductive properties of mammalian livestock. By adequate supply of selenium in the feed, it can effectively prevent health problems from its deficiency. Knowledge of the importance of selenium in the body is not yet sufficiently comprehensive, and even less so in animal species, and a deeper study of the effects of selenium may reveal a number of new biologically significant processes.

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    Not in our library10.1016/j.smallrumres.2009.12.042

  56. 56.

    Arthur J.R. The glutathione peroxidases. Cell Mol. Life Sci. 2000;57:1825-1835.

    Not in our library10.1007/pl00000664

  57. 57.

    Hatfield D.L., Tsuji P.A., Carlson B.A., Gladyshev V.N. Selenium and selenocysteine: Roles in cancer, health, and development. Trends Biochem. Sci. 2014;39:112-120.

    Not in our library10.1016/j.tibs.2013.12.007

  58. 58.

    Labunskyy V.M., Hatfield D.L., Gladyshev V.N. Selenoproteins: Molecular pathways and physiological roles. Physiol. Rev. 2014;94:739-777.

    Not in our library10.1152/physrev.00039.2013

  59. 59.

    Mangiapane E., Pessione A., Pessione E. Selenium and selenoproteins: An overview on different biological systems. Curr. Protein. Pept. Sci. 2014;15:598-607.

    Not in our library10.2174/1389203715666140608151134

  60. 60.

    Surai P.F. Selenium in Nutrition and Health. 2006;487-587.

    Not in our library

  61. 61.
    Selenium in the Environment, Metabolism and Involvement in Body Functions · 2013
    No notice
  62. 62.

    Shetty S.P., Shah R., Copeland P.R. Regulation of selenocysteine incorporationinto the selenium transport protein, selenoprotein P. J. Biol. Chem. 2014;289:25317-25326.

    Not in our library10.1074/jbc.m114.590430

  63. 63.

    Papp L.V., Lu J., Holmgren A., Khanna K.K. From selenium to selenoproteins: Synthesis, identity, and their role in human health. Antioxid. Redox Signal. 2007;9:775-806.

    Not in our library10.1089/ars.2007.1528

  64. 64.

    Allmang C., Krol A. Selenoprotein synthesis: UGA Does not end the story. Biochimie. 2006;88:1561-1571.

    Not in our library10.1016/j.biochi.2006.04.015

  65. 65.

    Kryukov G.V., Castellano S., Novoselov S.V., Lobanov A.V., Zehtab O., Guigó R., Gladyshev V.N. Characterization of mammalian selenoproteomes. Science. 2003;300:1439-1443.

    Not in our library10.1126/science.1083516

  66. 66.

    Squires J.E., Berry M.J. Eukaryotic selenoprotein synthesis: Mechanistic insight incorporating new factors and new functions for old factors. IUBMB Life. 2008;60:232-235.

    Not in our library10.1002/iub.38

  67. 67.

    Berry M.J., Banu L., Chen Y.Y., Mandel S.J., Kieffer J.D., Harney J.W., Larsen P.R. Recognition of UGA as a selenocysteine codon in type I deiodinase requires sequences in the 3′ untranslated region. Nature. 1991;353:273-276.

    Not in our library10.1038/353273a0

  68. 68.

    Bubenik J.L., Miniard A.C., Driscoll D.M. Characterization of the UGA-recoding and SECIS-binding activities of SECIS-binding protein 2. RNA Biol. 2014;11:1402-1413.

    Not in our library10.1080/15476286.2014.996472

  69. 69.

    Nourbakhsh M., Ahmadpour F., Chahardoli B., Malekpour-Dehkordi Z., Nourbakhsh M., Hosseini-Fard S.R., Doustimotlagh A., Golestani A., Razzaghy-Azar M. Selenium and its relationship with selenoprotein P and glutathioneperoxidase in children and adolescents with Hashimoto’s thyroiditisand hypothyroidism. J. Trace Elem. Med. Biol. 2016;34:10-14.

    Not in our library10.1016/j.jtemb.2015.10.003

  70. 70.

    Duntas L.H., Benvenga S. Selenium an element for life. Endocrine. 2015;48:756-775.

    Not in our library10.1007/s12020-014-0477-6

  71. 71.

    Lin S.L., Wang C.W., Tan S.R., Liang Y., Yao H.D., Zhang Z.W., Xu S.W. Selenium deficiency inhibits the conversion of thyroidal thyroxine (T4) to triiodothyronine (T3) in chicken thyroids. Biol. Trace Elem. Res. 2014;161:263-271.

    Not in our library10.1007/s12011-014-0083-8

  72. 72.

    Rowntree J.E., Hill G.M., Hawkins D.R., Link J.E., Rincker M.J., Bednar G.W., Kreft R.A. Effect of Se on selenoprotein activity and thyroid hormone metabolism in beef and dairy cows and calves. J. Anim. Sci. 2004;82:2995-3005.

    Not in our library10.2527/2004.82102995x

  73. 73.

    Guyot H., Rollin F. The diagnosis of selenium and iodine deficiencies in cattle. Ann. Med. Vet. 2007;151:166-191.

    Not in our library

  74. 74.

    Bianco A.C., Salvatore D., Gereben B., Berry M.J., Larsen P.R. Biochemistry, cellular and molecular biology, and physiological roles of the iodothyronine selenodeiodinases. Endocr. Rev. 2002;23:38-89.

    Not in our library10.1210/edrv.23.1.0455

  75. 75.

    Larsen P.R., Zavacki A.M. The role of the iodothyronine deiodinases in the physiology and pathophysiology of thyroid hormone action. Eur. Thyroid J. 2012;1:232-242.

    Not in our library10.1159/000343922

  76. 76.

    Dentice M., Marsili A., Zavacki A., Larsen P.R., Salvatore D. The deiodinases and the control of intracellular thyroid hormone signaling during cellular differentiation. Biochim. Biophys. Acta. 2013;1830:3937-3945.

    Not in our library10.1016/j.bbagen.2012.05.007

  77. 77.

    Burmeister L.A., Pachucki J., St Germain D.L. Thyroid hormones inhibit type 2 iodothyronine deiodinase in the rat cerebral cortex by both pre- and posttranslational mechanisms. Endocrinology. 1997;138:5231-5237.

    Not in our library10.1210/endo.138.12.5602

  78. 78.

    Bianco A.C., Kim B.W. Deiodinases: Implications of the local control of thyroid hormone action. J. Clin. Investig. 2006;116:2571-2579.

    Not in our library10.1172/jci29812

  79. 79.

    Shinde P.L., Dass R.S., Garg A.K. Effect of vitamin E and selenium supplementation on haematology, blood chemistry and thyroid hormones in male buffalo (Bubalus bubalis) calves. J. Anim. Feed Sci. 2009;18:241-256.

    Not in our library10.22358/jafs/66388/2009

  80. 80.

    Sethy K., Dass R.S., Garg A.K., Sahu S., Gogoi S. Effect of different selenium sources (Selenium yeast and Sodium selenite) on haematology, blood chemistry and thyroid hormones in male goats (Capra hircus). Indian J. Anim. Res. 2015;49:788-792.

    Not in our library10.18805/ijar.7040

  81. 81.

    Mittag J., Behrends T., Hoefig C.S., Vennström B., Schomburg L. Thyroid hormones regulate selenoprotein expression and selenium status in mice. PLoS ONE. 2010;5:e12931.

    Not in our library10.1371/journal.pone.0012931

  82. 82.

    Köhrle J., Gärtner R. Selenium and thyroid. Best Pract. Res. Clin. Endocrinol. Metab. 2009;23:815-827.

    Not in our library10.1016/j.beem.2009.08.002

  83. 83.

    Dercksen D.P., Counotte G.H., Hazebroek M.K., Arts W., van Rijn T. Selenium requirements of dairy goats [Article in Dutch]. Tijdschr Diergeneeskd. 2007;132:468-471.

    Not in our library

  84. 84.

    Effraimidis G., Wiersinga W.M. Mechanisms in endocrinology: Autoimmunethyroid disease: Old and new players. Eur. J. Endocrinol. 2014;170:R241-R252.

    Not in our library10.1530/eje-14-0047

  85. 85.

    Schomburg L. Selenium, selenoproteins and the thyroid gland: Interactions in health and disease. Nat. Rev. Endocrinol. 2012;8:160-171.

    Not in our library10.1038/nrendo.2011.174

  86. 86.

    Radostits O.M., Gay C.C., Hinchcliff K.W., Constable P.D. Veterinary Medicine: A Textbook of the Diseases of Cattle, Horses, Sheep, Pigs and Goats. 2007;552-557.

    Not in our library

  87. 87.

    Wang C., Liu Q., Yang W.Z., Dong Q., Yang X.M., He D.C., Zhang P., Dong K.H., Huang Y.X. Effects of selenium yeast on rumen fermentation, lactation performance and feed digestibilities in lactating dairy cows. Livest. Sci. 2009;126:239-244.

    Not in our library10.1016/j.livsci.2009.07.005

  88. 88.

    Aghwan Z.A., Sazili A.Q., Kadhim K.K., Alimon A.R., Goh Y.M., Adeyemi K.D. Effects of dietary supplementation of selenium and iodine on growth performance, carcass characteristics and histology of thyroid gland in goats. Anim. Sci. J. 2016;87:690-696.

    Not in our library10.1111/asj.12484

  89. 89.

    Alhidary I.A., Shini S., Al Jassim R.A., Abudabos A.M., Gaughan J.B. Effects of selenium and vitamin E on performance, physiological response, and selenium balance in heat-stressed sheep. J. Anim. Sci. 2015;93:576-588.

    Not in our library10.2527/jas.2014-8419

  90. 90.

    Alimohamady R., Aliarabi H., Bahari A., Dezfoulian A.H. Influence of different amounts and sources of selenium supplementation on performance, some blood parameters, and nutrient digestibility in lambs. Biol. Trace Elem. Res. 2013;154:45-54.

    Not in our library10.1007/s12011-013-9698-4

  91. 91.

    Calvo L., Toldrá F., Rodríguez A.I., López-Bote C., Rey A.I. Effect of dietary selenium source (organic vs. mineral) and muscle pH on meat quality characteristics of pigs. Food Sci. Nutr. 2016;5:94-102.

    Not in our library10.1002/fsn3.368

  92. 92.

    Downs K.M., Hess J.B., Bilgili S.F. Selenium source effect on broiler carcass characteristics, meat quality and drip loss. J. Appl. Anim. Res. 2000;18:61-72.

    Not in our library10.1080/09712119.2000.9706324

  93. 93.

    Habibian M., Sadeghi G., Ghazi S., Moeini M.M. Selenium as a feed supplement for heat-stressed poultry: A review. Biol. Trace Elem. Res. 2015;165:183-193.

    Not in our library10.1007/s12011-015-0275-x

  94. 94.

    Hu H., Wang M., Zhan X., Li X., Zhao R. Effect of different selenium sources on productive performance, serum and milk Se concentrations, and antioxidant status of sows. Biol. Trace Elem. Res. 2011;142:471-480.

    Not in our library10.1007/s12011-010-8803-1

  95. 95.

    James B.W., Goodband R.D., Unruh J.A., Tokach M.D., Nelssen J.L., Dritz S.S., O’Quinn P.R., Andrews B.S. Effects of creatine monohydrate on finishing pig growth performance, carcass characteristics and meat quality. Anim. Feed Sci. Technol. 2002;96:135-145.

    Not in our library10.1016/s0377-8401(01)00346-7

  96. 96.

    Lv C.H., Wang T., Regmi N., Chen X., Huang K., Liao S.F. Effects of dietary supplementation of selenium-enriched probiotics on production performance and intestinal microbiota of weanling piglets raised under high ambient temperature. J. Anim. Physiol. Anim. Nutr. (Berl.). 2015;99:1161-1171.

    Not in our library10.1111/jpn.12326

  97. 97.

    Mateo R.D., Spallholz J.E., Elder R., Yoon I., Kim S.W. Efficacy of dietary selenium sources on growth and carcass characteristics of growing-finishing pigs fed diets containing high endogenous selenium. J. Anim. Sci. 2007;85:1177-1183.

    Not in our library10.2527/jas.2006-067

  98. 98.

    Revilla-Vázquez A., Ramírez-Bribiesca E., López-Arellano R., Hernández-Calva L.M., Tórtora-Pérez J., García-García E., Cruz M.R.G. Supplement of selenium with intraruminal bolus of sodium selenite in sheep. Agrociencia. 2008;42:629-635.

    Not in our library

  99. 99.

    Song Y.X., Hou J.X., Zhang L., Wang J.G., Liu X.R., Zhou Z.Q., Cao B.Y. Effect of dietary selenomethionine supplementation on growth performance, tissue Se concentration, and blood glutathione peroxidase activity in kid boer goats. Biol. Trace Elem. Res. 2015;167:242-250.

    Not in our library10.1007/s12011-015-0316-5

  100. 100.

    Suchý P., Straková E., Herzig I. Selenium in poultry nutrition: A review. Czech J. Anim. Sci. 2014;59:495-503.

    Not in our library

  101. 101.

    Tufarelli V., Laudadio V. Dietary supplementation with selenium and vitamin E improves milk yield, composition and rheological properties of dairy Jonica goats. J. Dairy Res. 2011;78:144-148.

    Not in our library10.1017/s0022029910000907

  102. 102.

    Wu X., Yao J., Yang Z., Yue W., Ren Y., Zhang C., Liu X., Wang H., Zhao X., Yuan S., et al. Improved fetal hair follicle development by maternal supplement of selenium at nano size (Nano-Se). Livest. Sci. 2011;142:270-275.

    Not in our library10.1016/j.livsci.2011.08.005

  103. 103.

    Zhan X.A., Wang M., Zhao R.Q., Li W.F., Xu Z.R. Effects of different selenium source on selenium distribution, loin quality and antioxidant status in finishing pigs. Anim. Feed Sci. Technol. 2007;132:202-211.

    Not in our library10.1016/j.anifeedsci.2006.03.020

  104. 104.

    Kommisrud E., Osterås O., Vatn T. Blood selenium associated with health and fertility in Norwegian dairy herds. Acta Vet. Scand. 2005;46:229-240.

    Not in our library10.1186/1751-0147-46-229

  105. 105.

    Ahsan U., Kamran Z., Raza I., Ahmad S., Babar W., Riaz M.H., Iqbal Z. Role of selenium in male reproduction—A review. Anim. Reprod. Sci. 2014;146:55-62.

    Not in our library10.1016/j.anireprosci.2014.01.009

  106. 106.

    Bourne N., Wathes D.C., Lawrence K.E., McGowan M., Laven R.A. The effect of parenteral supplementation of vitamin E with selenium on the health and productivity of dairy cattle in the UK. Vet. J. 2008;177:381-387.

    Not in our library10.1016/j.tvjl.2007.06.006

  107. 107.

    Cerny K.L., Anderson L., Burris W.R., Rhoads M., Matthews J.C., Bridges P.J. Form of supplemental selenium fed to cycling cows affects systemic concentrations of progesterone but not those of estradiol. Theriogenology. 2016;85:800-806.

    Not in our library10.1016/j.theriogenology.2015.10.022

  108. 108.

    Chandra G., Aggarwal A., Singh A., Singh A.K., Kumar M., Kushwaha R., Singh Y.K. Oxidative stress in sperm biology—A review. Agric. Rev. 2012;33:54-61.

    Not in our library

  109. 109.

    El-Sharawy M., Eid E., Darwish S., Abdel-Razek I., Islam M.R., Kubota K., Yamauchi N., El-Shamaa I. Effect of organic and inorganic selenium supplementation on semen quality and blood enzymes in buffalo bulls. Anim. Sci. J. 2016;21.

    Not in our library10.1111/asj.12736

  110. 110.

    Foresta C., Flohé L., Garolla A., Roveri A., Ursini F., Maiorino M. Male fertility is linked to the selenoprotein phospholipid hydroperoxide glutathione peroxidase. Biol. Reprod. 2002;67:967-971.

    Not in our library10.1095/biolreprod.102.003822

  111. 111.

    Giadinis N.D., Loukopoulos P., Petridou E.J., Panousis N., Konstantoudaki K., Filioussis G., Tsousis G., Brozos C., Koutsoumpas A.T., Chaintoutis S.C., et al. Abortions in three beef cattle herds attributed to selenium deficiency. Pak. Vet. J. 2016;36:145-148.

    Not in our library

  112. 112.

    Grazul-Bilska A.T., Neville T.L., Borowczyk E., Sharma A., Reynolds L.P., Caton J.S., Redmer D.A., Vonnahme K.A. Ovarian and uterine characteristics and onset of puberty in adolescent offspring: Effects of maternal diet and selenium supplementation in sheep. Theriogenology. 2014;81:887-895.

    Not in our library10.1016/j.theriogenology.2013.12.024

  113. 113.

    Hemingway R.G. The influences of dietary intakes and supplementation with selenium and vitamin E on reproduction diseases and reproductive efficiency in cattle and sheep. Vet. Res. Commun. 2003;27:159-174.

    Not in our library10.1023/a:1022871406335

  114. 114.

    Mahan D.C., Peters J.C. Long-term effects of dietary organic and inorganic selenium sources and levels on reproducing sows and their progeny. J. Anim. Sci. 2004;82:1343-1358.

    Not in our library10.2527/2004.8251343x

  115. 115.

    Marin-Guzman J., Mahan D.C., Pate J.L. Effect of dietary selenium and vitamin E on spermatogenic development in boars. J. Anim. Sci. 2000;78:1537-1543.

    Not in our library10.2527/2000.7861537x

  116. 116.
    Selenium in Cattle: A Review · 2016
    No notice
  117. 117.

    Moeini M.M., Karami H., Mikaeili E. Effect of selenium and vitamin E supplementation during the late pregnancy on reproductive indices and milk production in heifers. Anim. Reprod. Sci. 2009;114:109-114.

    Not in our library10.1016/j.anireprosci.2008.09.012

  118. 118.

    Patterson H.H., Adams D.C., Klopfenstein T.J., Clark R.T., Teichert B. Supplementation to meet metabolizable protein requirements of primiparous beef heifers: II. Pregnancy and economics. J. Anim. Sci. 2003;81:563-570.

    Not in our library10.2527/2003.813563x

  119. 119.

    Shi L., Yue W., Zhang C., Ren Y., Zhu X., Wang Q., Shi L., Lei F. Effects of maternal and dietary selenium (Se-enriched yeast) on oxidative status in testis and apoptosis of germ cells during spermatogenesis of their offspring in goats. Anim. Reprod. Sci. 2010;119:212-218.

    Not in our library10.1016/j.anireprosci.2010.02.012

  120. 120.

    Shi L., Song R., Yao X., Ren Y. Effects of selenium on the proliferation, apoptosis and testosterone production of sheep Leydig cells in vitro. Theriogenology. 2017;93:24-32.

    Not in our library10.1016/j.theriogenology.2017.01.022

  121. 121.

    Spears J.W., Weiss W.P. Role of antioxidants and trace elements in health and immunity of transition dairy cows. Vet. J. 2008;176:70-76.

    Not in our library10.1016/j.tvjl.2007.12.015

  122. 122.

    Speight S.M., Estienne M.J., Harper A.F., Crawford R.J., Knight J.W., Whitaker B.D. Effects of dietary supplementation with an organic source of selenium on characteristics of semen quality and in vitro fertility in boars. J. Anim. Sci. 2012;90:761-770.

    Not in our library10.2527/jas.2011-3874

  123. 123.

    Surai P.F., Fisinin V.I. Selenium in Pig Nutrition and reproduction: Boars and semen quality—A Review. Asian-Australas. J. Anim. Sci. 2015;28:730-746.

    Not in our library10.5713/ajas.14.0593

  124. 124.

    Talukdar D.J., Talukdar P., Ahmed K. Minerals and its impact on fertility of livestock: A review. Agric. Rev. 2016;37:333-337.

    Not in our library10.18805/ag.v37i4.6464

  125. 125.

    Zubair M., Ali M., Ahmad M., Sajid S.M., Ahmad I., Gul S.T. Effect of Selenium and Vitamin E on cryopreservation of semen and reproductive performance of animals (a review). J. Entomol. Zool. Stud. 2015;3:82-86.

    Not in our library

  126. 126.

    Bao R.K., Zheng S.F., Wang X.Y. Selenium protects against cadmium-induced kidney apoptosis in chickens by activating the PI3K/AKT/Bcl-2 signaling pathway. Environ. Sci. Pollut. Res. Int. 2017;13.

    Not in our library10.1007/s11356-017-9422-6

  127. 127.

    Bjørklund G., Aaseth J., Ajsuvakova O.P., Nikonorov A.A., Skalny A.V., Skalnaya M.G., Tinkov A.A. Molecular interaction between mercury and selenium in neurotoxicity. Coord. Chem. Rev. 2017;332:30-37.

    Not in our library10.1016/j.ccr.2016.10.009

  128. 128.

    Dai X., Thongchot S., Dokduang H., Loilome W., Khuntikeo N., Titapun A., Ungarreevittaya P., Yongvanit P., Techasen A., Namwat N. Potential of selenium compounds as new anticancer agents for cholangiocarcinoma. Anticancer Res. 2016;36:5981-5988.

    Not in our library10.21873/anticanres.11186

  129. 129.

    Galadari S., Rahman A., Pallichankandy S., Thayyullathil F. Reactive oxygen species and cancer paradox: To promote or to suppress? Free Radic. Biol. Med. 2017;104:144-164.

    Not in our library10.1016/j.freeradbiomed.2017.01.004

  130. 130.

    Gao Z., Li J., Song X., Zhang J., Wang X., Jing H., Ren Z., Li S., Zhang C., Jia L. Antioxidative, anti-inflammation and lung-protective effects of mycelia selenium polysaccharides from Oudemansiella radicata. Int. J. Biol. Macromol. 2017;104:1158-1164.

    Not in our library10.1016/j.ijbiomac.2017.07.029

  131. 131.

    Gu L.X., Wen Z.S., Xiang X.W., Ma L., Wang X.B., Ma J.Y., Qu Y.L. Immunomodulatory effect of low molecular-weight seleno-aminopolysaccharides in intestinal epithelial cells. Int. J. Biol. Macromol. 2017;99:570-577.

    Not in our library10.1016/j.ijbiomac.2017.03.008

  132. 132.

    Guastamacchia E., Giagulli V.A., Licchelli B., Triggiani V. Selenium and iodine in autoimmune thyroiditis. Endocr. Metab. Immune Disord. Drug Targets. 2015;15:288-292.

    Not in our library10.2174/1871530315666150619094242

  133. 133.

    Hegedüs V., Prokisch J., Fébel H., Kleiner D., Ditrói K., Szijártó A., Blázovics A. Nanoselenium treatment in fatty liver. Z. Gastroenterol. 2012;50.

    Not in our library10.1055/s-0032-1312383

  134. 134.

    Lee J.M., Chun H.J., Choi H.S., Kim E.S., Seo Y.S., Jeen Y.T., Lee H.S., Um S.H., Kim C.H., Sul D. Selenium administration attenuates 5-flurouracil-induced intestinal mucositis. Nutr. Cancer. 2017;69:616-622.

    Not in our library10.1080/01635581.2017.1300289

  135. 135.

    Orct T., Lazarus M., Ljubojević M., Sekovanić A., Sabolić I., Blanuša M. Metallothionein, essential elements and lipid peroxidation in mercury-exposed suckling rats pretreated with selenium. Biometals. 2015;28:701-712.

    Not in our library10.1007/s10534-015-9859-3

  136. 136.

    Tran A.P., Webster T. Selenium nanoparticles inhibit Staphylococcus aureus growth. Int. J. Nanomed. 2011;6:1553-1558.

    Not in our library10.2147/ijn.s21729

  137. 137.

    Wu C., Xu Z., Huang K. Effects of Dietary Selenium on inflammation and hydrogen sulfide in the gastrointestinal tract in chickens. Biol. Trace Elem. Res. 2016;174:428-435.

    Not in our library10.1007/s12011-016-0735-y

  138. 138.

    Zhu K., Jiang L., Chu Y., Zhang Y.S. Protective effect of selenium against cisplatin-induced nasopharyngeal cancer in male albino rats. Oncol. Lett. 2016;12:5068-5074.

    Not in our library10.3892/ol.2016.5346

  139. 139.

    Chan J.M., Darke A.K., Penney K.L., Tangen C.M., Goodman P.J., Lee G.S., Sun T., Peisch S., Tinianow A.M., Rae J.M., et al. Selenium- or vitamin E-related gene variants, interaction with supplementation, and risk of high-grade prostate cancer in SELECT. Cancer Epidemiol. Biomark. Prev. 2016;25:1050-1058.

    Not in our library10.1158/1055-9965.epi-16-0104

  140. 140.

    Fernandes A.P., Wallenberg M., Gandin V., Misra S., Tisato F., Marzano C., Rigobello M.P., Kumar S., Björnstedt M. Methylselenol formed by spontaneous methylation of selenide is a superior selenium substrate to the thioredoxin and glutaredoxin systems. PLoS ONE. 2012;7:e50727.

    Not in our library10.1371/journal.pone.0050727

  141. 141.

    Weekley C.M., Jeong G., Tierney M.E., Hossain F., Maw A.M., Shanu A., Harris H.H., Witting P.K. Selenite-mediated production of superoxide radical anions in A549 cancer cells is accompanied by a selective increase in SOD1 concentration, enhanced apoptosis and Se-Cu bonding. J. Biol. Inorg. Chem. 2014;19:813-828.

    Not in our library10.1007/s00775-014-1113-x

  142. 142.

    Park S.H., Kim J.H., Chi G.Y., Kim G.Y., Chang Y.C., Moon S.K., Nam S.W., Kim W.J., Yoo Y.H., Choi Y.H. Induction of apoptosis and autophagy by sodium selenite in A549 human lung carcinoma cells through generation of reactive oxygen species. Toxicol. Lett. 2012;212:252-261.

    Not in our library10.1016/j.toxlet.2012.06.007

  143. 143.

    Shen H.M., Yang C.F., Ding W.X., Liu J., Ong C.N. Superoxide radical-initiated apoptotic signalling pathway in selenite-treated HepG(2) cells: Mitochondria serve as the main target. Free Radic. Biol. Med. 2001;30:9-21.

    Not in our library10.1016/s0891-5849(00)00421-4

  144. 144.

    Wang H.T., Yang X.L., Zhang Z.H., Lu J.L., Xu H.B. Reactive oxygen species from mitochondria mediate SW480 cells apoptosis induced by Na2SeO3. Biol. Trace Elem. Res. 2002;85:241-254.

    Not in our library10.1385/bter:85:3:241

  145. 145.

    Zhong W., Oberley T.D. Redox-mediated effects of selenium on apoptosis and cell cycle in the LNCaP human prostate cancer cell line. Cancer Res. 2001;61:7071-7078.

    Not in our library

  146. 146.

    Zhu Y., Xu H., Huang K. Mitochondrial permeability transition and cytochrome c release induced by selenite. J. Inorg. Biochem. 2002;90:43-50.

    Not in our library10.1016/s0162-0134(02)00407-5

  147. 147.

    Husbeck B., Nonn L., Peehl D.M., Knox S.J. Tumor-selective killing by selenite in patient-matched pairs of normal and malignant prostate cells. Prostate. 2006;66:218-225.

    Not in our library10.1002/pros.20337

  148. 148.

    Nilsonne G., Sun X., Nyström C., Rundlöf A.K., Potamitou Fernandes A., Björnstedt M., Dobra K. Selenite induces apoptosis in sarcomatoid malignant mesothelioma cells through oxidative stress. Free Radic. Biol. Med. 2006;41:874-885.

    Not in our library10.1016/j.freeradbiomed.2006.04.031

  149. 149.

    Ip C., Ganther H.E. Activity of methylated forms of selenium in cancer prevention. Cancer Res. 1990;50:1206-1211.

    Not in our library

  150. 150.

    Xiang N., Zhao R., Zhong W. Sodium selenite induces apoptosis by generation of superoxide via the mitochondrial-dependent pathway in human prostate cancer cells. Cancer Chemother. Pharmacol. 2009;63:351-362.

    Not in our library10.1007/s00280-008-0745-3

  151. 151.

    Li J., Zuo L., Shen T., Xu C.M., Zhang Z.N. Induction of apoptosis by sodium selenite in human acute promyelocytic leukemia NB4 cells: Involvement of oxidative stress and mitochondria. J. Trace Elem. Med. Biol. 2003;17:19-26.

    Not in our library10.1016/s0946-672x(03)80041-x

  152. 152.

    Kim E.H., Sohn S., Kwon H.J., Kim S.U., Kim M.J., Lee S.J., Choi K.S. Sodium selenite induces superoxide-mediated mitochondrial damage and subsequent autophagic cell death in malignant glioma cells. Cancer Res. 2007;67:6314-6324.

    Not in our library10.1158/0008-5472.can-06-4217

  153. 153.

    Björnstedt M., Kumar S., Holmgren A. Selenodiglutathione is a highly efficient oxidant of reduced thioredoxin and a substrate for mammalian thioredoxin reductase. J. Biol. Chem. 1992;267:8030-8034.

    Not in our library

  154. 154.

    Ganther H.E. Reduction of the selenotrisulfide derivative of glutathione to a persulfide analog by glutathione reductase. Biochemistry. 1971;10:4089-4098.

    Not in our library10.1021/bi00798a013

  155. 155.

    Horky P., Jancikova P., Sochor J., Hynek D., Chavis G.J., Ruttkay-Nedecky B., Cernei N., Zitka O., Zeman L., Adam V., et al. Effect of organic and inorganic form of selenium on antioxidant status of breeding boars ejaculate revealed by electrochemistry. Int. J. Electrochem. Sci. 2012;7:9643-9657.

    Not in our library

  156. 156.

    Kim J.H., Wang S.Y., Kim I.C., Ki J.S., Raisuddin S., Lee J.S., Han K.N. Cloning of a river pufferfish (Takifugu obscurus) metallothionein cDNA and study of its induction profile in cadmium-exposed fish. Chemosphere. 2008;71:1251-1259.

    Not in our library10.1016/j.chemosphere.2007.11.067

  157. 157.

    Agarwal R., Raisuddin S., Tewari S., Goel S.K., Raizada R.B., Behari J.R. Evaluation of comparative effect of pre- and posttreatment of selenium on mercury-induced oxidative stress, histological alterations, and metallothionein mRNA expression in rats. J. Biochem. Mol. Toxicol. 2010;24:123-135.

    Not in our library10.1002/jbt.20320

  158. 158.

    Bjørklund G. Selenium as an antidote in the treatment of mercury intoxication. Biometals. 2015;28:605-614.

    Not in our library10.1007/s10534-015-9857-5

  159. 159.

    Burk R.F., Hill K.E. Selenoprotein P-expression, functions, and roles in mammals. Biochim. Biophys. Acta. 2009;1790:1441-1447.

    Not in our library10.1016/j.bbagen.2009.03.026

  160. 160.

    El-Ansary A., Bjørklund G., Tinkov A.A., Skalny A.V., Al Dera H. Relationship between selenium, lead, and mercury in red blood cells of Saudi autistic children. Metab. Brain Dis. 2017;32:1073-1080.

    Not in our library10.1007/s11011-017-9996-1

  161. 161.

    Burk R.F., Hill K.E., Motley A.K., Winfrey V.P., Kurokawa S., Mitchell S.L., Zhang W. Selenoprotein P and apolipoprotein E receptor-2 interact at the blood-brain barrier and also within the brain to maintain an essential selenium pool that protects against neurodegeneration. FASEB J. 2014;28:3579-3588.

    Not in our library10.1096/fj.14-252874

  162. 162.

    Hassanin K.M., Abd El-Kawi S.H., Hashem K.S. The prospective protective effect of selenium nanoparticles against chromium-induced oxidative and cellular damage in rat thyroid. Int. J. Nanomed. 2013;8:1713-1720.

    Not in our library10.2147/ijn.s42736

  163. 163.

    Hao P., Zhu Y., Wang S., Wan H., Chen P., Wang Y., Cheng Z., Liu Y., Liu J. Selenium Administration Alleviates Toxicity of Chromium(VI) in the Chicken Brain. Biol. Trace Elem. Res. 2017;178:127-135.

    Not in our library10.1007/s12011-016-0915-9

  164. 164.

    Wan H., Zhu Y., Chen P., Wang Y., Hao P., Cheng Z., Liu Y., Liu J. Effect of various selenium doses on chromium(IV)-induced nephrotoxicity in a male chicken model. Chemosphere. 2017;174:306-314.

    Not in our library10.1016/j.chemosphere.2017.01.143

  165. 165.

    Lynch S.J., Horgan K.A., White B., Walls D. Selenium source impacts protection of porcine jejunal epithelial cells from cadmium-induced DNA damage, with maximum protection exhibited with yeast-derived selenium compounds. Biol. Trace Elem. Res. 2017;176:311-320.

    Not in our library10.1007/s12011-016-0828-7

  166. 166.

    Wang X., Bao R., Fu J. The antagonistic effect of selenium on cadmium-induced damage and mRNA levels of selenoprotein genes and inflammatory factors in chicken kidney Tissue. Biol. Trace Elem. Res. 2017;16.

    Not in our library10.1007/s12011-017-1041-z

  167. 167.

    Sadek K.M., Lebda M.A., Abouzed T.K., Nasr S.M., Shoukry M. Neuro- and nephrotoxicity of subchronic cadmium chloride exposure and the potential chemoprotective effects of selenium nanoparticles. Metab. Brain Dis. 2017;28.

    Not in our library10.1007/s11011-017-0053-x

  168. 168.

    Özkan-Yilmaz F., Özlüer-Hunt A., Gündüz S.G., Berköz M., Yalin S. Effects of dietary selenium of organic form against lead toxicity on the antioxidant system in Cyprinus carpio. Fish Physiol. Biochem. 2014;40:355-363.

    Not in our library10.1007/s10695-013-9848-9

  169. 169.

    Danzeisen R., Achsel T., Bederke U., Cozzolino M., Crosio C., Ferri A., Frenzel M., Gralla E.B., Huber L., Ludolph A., et al. Superoxide dismutase 1 modulates expression of transferrin receptor. J. Biol. Inorg. Chem. 2006;11:489-498.

    Not in our library10.1007/s00775-006-0099-4

  170. 170.

    Roy C.N., Enns C.A. Iron homeostasis: New tales from the crypt. Blood. 2000;96:4020-4027.

    Not in our library

  171. 171.

    Bartfay W.J. Selenium status and the pathogenesis of iron-overload cardiomyopathies: Cause or Consequence. Queen’s Health Sci. J. 2003;6:40-46.

    Not in our library

  172. 172.

    Bartfay W.J., Bartfay E. Decreasing effects of iron toxicosis on selenium and glutathione peroxidase activity. West. J. Nurs. Res. 2002;24:119-131.

    Not in our library10.1177/01939450222045789

  173. 173.

    Dawson M.A., Kouzarides T. Cancer epigenetics: From mechanism to therapy. Cell. 2012;150:12-27.

    Not in our library10.1016/j.cell.2012.06.013

  174. 174.

    Speckmann B., Grune T. Epigenetic effects of selenium and their implications for health. Epigenetics. 2015;10:179-190.

    Not in our library10.1080/15592294.2015.1013792

  175. 175.

    Dozmorov M.G., Wren J.D., Alarcón-Riquelme M.E. Epigenomic elements enriched in the promoters of autoimmunity susceptibility genes. Epigenetics. 2014;9:276-285.

    Not in our library10.4161/epi.27021

  176. 176.

    Häsler R., Feng Z., Bäckdahl L., Spehlmann M.E., Franke A., Teschendorff A., Rakyan V.K., Down T.A., Wilson G.A., Feber A., et al. A functional methylome map of ulcerative colitis. Genome Res. 2012;22:2130-2137.

    Not in our library10.1101/gr.138347.112

  177. 177.

    Nilsson E., Jansson P.A., Perfilyev A., Volkov P., Pedersen M., Svensson M.K., Poulsen P., Ribel-Madsen R., Pedersen N.L., Almgren P., et al. Altered DNA methylation and differential expression of genes influencing metabolism and inflammation in adipose tissue from subjects with type 2 diabetes. Diabetes. 2014;63:2962-2976.

    Not in our library10.2337/db13-1459

  178. 178.

    Whayne T.F. Epigenetics in the development, modification, and prevention of cardiovascular disease. Mol. Biol. Rep. 2015;42:765-776.

    Not in our library10.1007/s11033-014-3727-z

  179. 179.

    Arai E., Kanai Y. DNA methylation profiles in precancerous tissue and cancers: Carcinogenetic risk estimation and prognostication based on DNA methylation status. Epigenomics. 2010;2:467-481.

    Not in our library10.2217/epi.10.16

  180. 180.

    Timp W., Feinberg A.P. Cancer as a dysregulated epigenome allowing cellular growth advantage at the expense of the host. Nat. Rev. Cancer. 2013;13:497-510.

    Not in our library10.1038/nrc3486

  181. 181.

    Conrad M., Jakupoglu C., Moreno S.G., Lippl S., Banjac A., Schneider M., Beck H., Hatzopoulos A.K., Just U., Sinowatz F., et al. Essential role for mitochondrial thioredoxin reductase in hematopoiesis, heart development, and heart function. Mol. Cell. Biol. 2004;24:9414-9423.

    Not in our library10.1128/mcb.24.21.9414-9423.2004

  182. 182.

    Bösl M.R., Takaku K., Oshima M., Nishimura S., Taketo M.M. Early embryonic lethality caused by targeted disruption of the mouse selenocysteine tRNA gene (Trsp). Proc. Natl. Acad. Sci. USA. 1997;94:5531-5534.

    Not in our library10.1073/pnas.94.11.5531

  183. 183.

    Davis C.D., Uthus E.O., Finley J.W. Dietary selenium and arsenic affect DNA methylation in vitro in Caco-2 cells and in vivo in rat liver and colon. J. Nutr. 2000;130:2903-2909.

    Not in our library10.1093/jn/130.12.2903

  184. 184.

    Uthus E.O., Ross S.A., Davis C.D. Differential effects of dietary selenium (Se) and folate on methyl metabolism in liver and colon of rats. Biol. Trace Elem. Res. 2006;109:201-214.

    Not in our library10.1385/bter:109:3:201

  185. 185.

    Armstrong K.M., Bermingham E.N., Bassett S.A., Treloar B.P., Roy N.C., Barnett M.P. Global DNA methylation measurement by HPLC using low amounts of DNA. Biotechnol. J. 2011;6:113-117.

    Not in our library10.1002/biot.201000267

  186. 186.

    Xiang N., Zhao R., Song G., Zhong W. Selenite reactivates silenced genes by modifying DNA methylation and histones in prostate cancer cells. Carcinogenesis. 2008;29:2175-2181.

    Not in our library10.1093/carcin/bgn179

  187. 187.

    Arai Y., Ohgane J., Yagi S., Ito R., Iwasaki Y., Saito K., Akutsu K., Takatori S., Ishii R., Hayashi R., et al. Epigenetic assessment of environmental chemicals detected in maternal peripheral and cord blood samples. J. Rep. Dev. 2011;57:507-517.

    Not in our library10.1262/jrd.11-034a

  188. 188.

    Zeng H., Yan L., Cheng W.H., Uthus E.O. Dietary selenomethionine increases exon-specific DNA methylation of the p53 gene in rat liver and colon mucosa. J. Nutr. 2011;141:1464-1468.

    Not in our library10.3945/jn.111.140715

  189. 189.

    Du J., Patel D.J. Structural biology-based insights into combinatorial readout and crosstalk among epigenetic marks. Biochim. Biophys. Acta. 2014;1839:719-727.

    Not in our library10.1016/j.bbagrm.2014.04.011

  190. 190.

    Falkenberg K.J., Johnstone R.W. Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders. Nat. Rev. Drug Discov. 2014;13:673-691.

    Not in our library10.1038/nrd4360

  191. 191.

    Gowda R., Madhunapantula S.V., Desai D., Amin S., Robertson G.P. Selenium-containing histone deacetylase inhibitors for melanoma management. Cancer Biol. Ther. 2012;13:756-765.

    Not in our library10.4161/cbt.20558

  192. 192.

    Kassam S., Goenaga-Infante H., Maharaj L., Hiley C.T., Juliger S., Joel S.P. Methylseleninic acid inhibits HDAC activity in diffuse large B-cell lymphoma cell lines. Cancer Chemother. Pharmacol. 2011;68:815-821.

    Not in our library10.1007/s00280-011-1649-1

  193. 193.

    Desai D., Salli U., Vrana K.E., Amin S. SelSA, selenium analogs of SAHA as potent histone deacetylase inhibitors. Bioorg. Med. Chem. Lett. 2010;20:2044-2047.

    Not in our library10.1016/j.bmcl.2009.07.068

  194. 194.

    Maciel-Dominguez A., Swan D., Ford D., Hesketh J. Selenium alters miRNA profile in an intestinal cell line: Evidence that miR-185 regulates expression of GPX2 and SEPSH2. Mol. Nutr. Food Res. 2013;57:2195-2205.

    Not in our library10.1002/mnfr.201300168

  195. 195.

    Li Q., Wang J.X., He Y.Q., Feng C., Zhang X.J., Sheng J.Q., Li P.F. MicroRNA-185 regulates chemotherapeutic sensitivity in gastric cancer by targeting apoptosis repressor with caspase recruitment domain. Cell Death Dis. 2014;5:e1197.

    Not in our library10.1038/cddis.2014.148

  196. 196.

    Qu F., Cui X., Hong Y., Wang J., Li Y., Chen L., Liu Y., Gao Y., Xu D., Wang Q. MicroRNA-185 suppresses proliferation, invasion, migration, and tumorigenicity of human prostate cancer cells through targeting androgen receptor. Mol. Cell Biochem. 2013;377:121-130.

    Not in our library10.1007/s11010-013-1576-z

  197. 197.

    Combs G.F. The Vitamins: Fundamental Aspects in Nutrition and Health. 2008;583.

    Not in our library

  198. 198.

    Au Yeung K.J., Smith A., Zhao A., Madden K.B., Elfrey J., Sullivan C., Levander O., Urban J.F., Shea-Donohue T. Impact of vitamin E or selenium deficiency on nematode-induced alterations in murine intestinal function. Exp. Parasitol. 2005;109:201-208.

    Not in our library10.1016/j.exppara.2004.12.015

  199. 199.

    Smith A., Madden K.B., Yeung K.J., Zhao A., Elfrey J., Finkelman F., Levander O., Shea-Donohue T., Urban J.F. Deficiencies in selenium and/or vitamin E lower the resistance of mice to Heligmosomoides polygyrus infections. J. Nutr. 2005;135:830-836.

    Not in our library10.1093/jn/135.4.830

  200. 200.

    Abutarbush S.M., Radostits O.M. Congenital nutritional muscular dystrophy in a beef calf. Can. Vet. J. 2003;44:738-739.

    Not in our library

  201. 201.

    Radostits O.M., Gay C.C., Blood D.C., Hinchcliff K.W. Veterinary Medicine: A Textbook of the Diseases of Cattle, Sheep, Pigs, Goats and Horses. 2000.

    Not in our library

  202. 202.

    Streeter R.M., Divers T.J., Mittel L., Korn A.E., Wakshlag J.J. Selenium deficiency associations with gender, breed, serum vitamin E and creatine kinase, clinical signs and diagnoses in horses of different age groups: A retrospective examination 1996–2011. Equine Vet. J. Suppl. 2012;44:31-35.

    Not in our library10.1111/j.2042-3306.2012.00643.x

  203. 203.

    Cardona Á.J., Reza G.L. Esteatosis en un burro (Equus asinus). Primer reporte en Colombia (Steatosis in donkey (Equus asinus). First report in Colombia). Rev. MVZ Cordoba. 2011;16:2793-2798.

    Not in our library10.21897/rmvz.280

  204. 204.

    Sobiech P., Kuleta Z. Levels of selected biochemical indicators of serum and blood during subclinical form of nutritional muscular dystrophy in lambs. Pol. J. Vet. Sci. 1999;2:37-41.

    Not in our library

  205. 205.

    Żarczyńska K., Sobiech P., Radwińska J., Rękawek W. Effects of selenium on animal health. J. Elementol. 2013;18:329-340.

    Not in our library10.5601/jelem.2013.18.2.12

  206. 206.

    Kojouri G.A., Rezakhani A., Ahmadi H. Arrhythmias in advance stiff lamb disease. Small Rumin. Res. 2009;84:65-69.

    Not in our library10.1016/j.smallrumres.2009.06.005

  207. 207.

    Van Loon G., Lefère L., Bauwens C., Kleyn K., Broux B., De Clercq D., Deprez P. Yellow fat disease (steatitis): Description of 20 cases with emphasis on typical ultrasonographic findings. Equine Vet. J. 2015;47.

    Not in our library10.1111/evj.12486_43

  208. 208.

    Bruijn C., Veldhuis E., Sloet M. Yellow fat disease in equides. Equine Vet. Educ. 2006;18:38-44.

    Not in our library10.1111/j.2042-3292.2006.tb00413.x

  209. 209.

    Fajt Z., Svoboda M., Drábek J., Dubanský V. Selen a jeho význam pro zdravotní stav prasat—Review. Veterinarstvi. 2009;59:221-224.

    Not in our library

  210. 210.

    Kamada H., Nonaka I., Takenouchi N., Amari M. Effects of selenium supplementation on plasma progesterone concentrations in pregnant heifers. Anim. Sci. J. 2014;85:241-246.

    Not in our library10.1111/asj.12139

  211. 211.

    Uematsu M., Kitahara G., Sameshima H., Osawa T. Serum selenium and liposoluble vitamins in Japanese Black cows that had stillborn calves. J. Vet. Med. Sci. 2016;78:1501-1504.

    Not in our library10.1292/jvms.15-0268

  212. 212.

    Underwood E.J., Suttle N.F. Selenium. The Mineral Nutrition of Livestock. 2004;421-475.

    Not in our library

  213. 213.

    Kamada H. Effects of selenium-rich yeast supplementation on the plasma progesterone levels of postpartum dairy cows. Asian-Australas. J. Anim. Sci. 2017;30:347-354.

    Not in our library10.5713/ajas.16.0372

  214. 214.

    Wilde D. Influence of macro and micro minerals in the peri-parturient period on fertility in dairy cattle. Anim. Reprod. Sci. 2006;96:240-249.

    Not in our library10.1016/j.anireprosci.2006.08.004

  215. 215.

    Ceko M.J., Hummitzsch K., Hatzirodos N., Bonner W.M., Aitken J.B., Russell D.L., Lane M., Rodgers R.J., Harris H.H. X-ray fluorescence imaging and other analyses identify selenium and GPX1 as important in female reproductive function. Metallomics. 2015;7:66-77.

    Not in our library10.1039/c4mt00228h

  216. 216.

    Davis C.D., Tsuji P.A., Milner J.A. Selenoproteins and cancer prevention. Annu. Rev. Nutr. 2012;32:73-95.

    Not in our library10.1146/annurev-nutr-071811-150740

  217. 217.

    Fairweather-Tait S.J., Collings R., Hurst R. Selenium bioavailability: Current knowledge and future research requirements. Am. J. Clin. Nutr. 2010;91:1484S-1491S.

    Not in our library10.3945/ajcn.2010.28674j

  218. 218.

    Badade Z.G., More K., Narshetty J. Oxidative stress adversely affects spermatogenesis in male infertility. Biomed. Res. 2011;22:323-328.

    Not in our library

  219. 219.

    Brouwers J.F., Gadella B.M. In situ detection and localization of lipid peroxidation in individual bovine sperm cells. Free Radic. Biol. Med. 2003;35:1382-1391.

    Not in our library10.1016/j.freeradbiomed.2003.08.010

  220. 220.

    Cerolini S., Maldjian A., Surai P., Noble R. Viability, susceptibility to peroxidation and fatty acid composition of boar semen during liquid storage. Anim. Reprod. Sci. 2000;58:99-111.

    Not in our library10.1016/s0378-4320(99)00035-4

  221. 221.

    Kemal Duru N., Morshedi M., Oehninger S. Effects of hydrogen peroxide on DNA and plasma membrane integrity of human spermatozoa. Fertil. Steril. 2000;74:1200-1207.

    Not in our library10.1016/s0015-0282(00)01591-0

  222. 222.

    Kefer J.C., Agarwal A., Sabanegh E. Role of antioxidants in the treatment of male infertility. Int. J. Urol. 2009;16:449-457.

    Not in our library10.1111/j.1442-2042.2009.02280.x

  223. 223.

    Agarwal A., Nallella K.P., Allamaneni S.S., Said T.M. Role of antioxidants in treatment of male infertility: An overview of the literature. Reprod. Biomed. Online. 2004;8:616-627.

    Not in our library10.1016/s1472-6483(10)61641-0

  224. 224.

    Koracevic D., Koracevic G., Djordjevic V., Andrejevic S., Cosic V. Method for the measurement of antioxidant activity in human fluids. J. Clin. Pathol. 2001;54:356-361.

    Not in our library10.1136/jcp.54.5.356

  225. 225.
    Thiobarbituric acid reactive substance (TBARS) a marker of oxidative stress in obstructive sleep apnea · 2014
    Not checked
  226. 226.

    Bhutia R.D., Upadhyay B., Maneesh M. Association of plasma level of thiobarbituric acid reactive substances with extent of hepatocellular injury in preterm infants with cholestatic jaundice. Indian J. Clin. Biochem. 2006;21:39-41.

    Not in our library10.1007/bf02912909

  227. 227.

    Shang X.J., Li K., Ye Z.Q., Chen Y.G., Yu X., Huang Y.F. Analysis of lipid peroxidative levels in seminal plasma of infertile men by high-performance liquid chromatography. Arch. Androl. 2004;50:411-416.

    Not in our library10.1080/01485010490484138

  228. 228.

    Tavilani H., Goodarzi M.T., Vaisi-Raygani A., Salimi S., Hassanzadeh T. Activity of antioxidant enzymes in seminal plasma and their relationship with lipid peroxidation of spermatozoa. Int. Braz. J. Urol. 2008;34:485-491.

    Not in our library10.1590/s1677-55382008000400011

  229. 229.

    Breininger E., Beorlegui N.B., O’Flaherty C.M., Beconi M.T. Alpha-tocopherol improves biochemical and dynamic parameters in cryopreserved boar semen. Theriogenology. 2005;63:2126-2135.

    Not in our library10.1016/j.theriogenology.2004.08.016

  230. 230.

    Kumaresan A., Kadirvel G., Bujarbaruah K.M., Bardoloi R.K., Das A., Kumar S., Naskar S. Preservation of boar semen at 18 degrees C induces lipid peroxidation and apoptosis like changes in spermatozoa. Anim. Reprod. Sci. 2009;110:162-171.

    Not in our library10.1016/j.anireprosci.2008.01.006

  231. 231.

    Gómez-Fernández J., Gómez-Izquierdo E., Tomás C., Mocé E., de Mercado E. Is sperm freezability related to the post-thaw lipid peroxidation and the formation of reactive oxygen species in boars? Reprod. Domest. Anim. 2013;48:177-182.

    Not in our library10.1111/j.1439-0531.2012.02126.x

  232. 232.

    Giadinis N.D., Panousis N., Petridou E.J., Siarkou V.I., Lafi S.Q., Pourliotis K., Hatzopoulou E., Fthenakis G.C. Selenium, vitamin E and vitamin A blood concentrations in dairy sheep flocks with increased or low clinical mastitis incidence. Small Rumin. Res. 2011;95:193-196.

    Not in our library10.1016/j.smallrumres.2010.08.010

  233. 233.

    Meschy F. Nutrition Minérale des Ruminants. 2010;208.

    Not in our library

  234. 234.

    Sordillo L.M. Selenium-dependent regulation of oxidative stress and immunity in periparturient dairy cattle. Vet. Med. Int. 2013;2013:154045.

    Not in our library10.1155/2013/154045

  235. 235.

    Salman S., Khol-Parisini A., Schafft H., Lahrssen-Wiederholt M., Hulan H.W., Dinse D., Zentek J. The role of dietary selenium in bovine mammary gland health and immune function. Anim. Health Res. Rev. 2009;10:21-34.

    Not in our library10.1017/s1466252308001588

  236. 236.

    Passchyn P., Piepers S., De Vliegher S. Pathogen group-specific risk factors for intramammary infection in treated and untreated dairy heifers participating in a prepartum antimicrobial treatment trial. J. Dairy Sci. 2014;97:6260-6270.

    Not in our library10.3168/jds.2014-8119

  237. 237.

    Ceballos-Márquez A., Barkema H.W., Stryhn H., Dohoo I.R., Keefe G.P., Wichtel J.J. Bulk tank milk selenium and its association with milk production parameters in Canadian dairy herds. Can. Vet. J. 2012;53:51-56.

    Not in our library

  238. 238.

    Erskine R.J., Eberhart R.J., Grasso P.J., Scholz R.W. Induction of Escherichia coli mastitis in cows fed selenium-deficient or selenium-supplemented diets. Am. J. Vet. Res. 1989;50:2093-2100.

    Not in our library

  239. 239.

    Erskine R.J., Eberhart R.J., Scholz R.W. Experimentally induced Staphylococcus aureus mastitis in selenium-deficient and selenium-supplemented dairy cows. Am. J. Vet. Res. 1990;51:1107-1111.

    Not in our library

  240. 240.

    Ali-Vehmas T., Vikerpuur M., Fang W., Sandholm M. Giving selenium supplements to dairy cows strengthens the inflammatory response to intramammary infection and induces a growth-suppressing effect on mastitis pathogens in whey. Zentralbl. Veterinarmed. A. 1997;44:559-571.

    Not in our library10.1111/j.1439-0442.1997.tb01142.x

  241. 241.

    Sordillo L.M., O’Boyle N., Gandy J.C., Corl C.M., Hamilton E. Shifts in thioredoxin reductase activity and oxidant status in mononuclear cells obtained from transition dairy cattle. J. Dairy Sci. 2007;90:1186-1192.

    Not in our library10.3168/jds.s0022-0302(07)71605-3

  242. 242.

    Ceballos A., Kruze J., Barkema H.W., Dohoo I.R., Sanchez J., Uribe D., Wichtel J.J., Wittwer F. Barium selenate supplementation and its effect on intramammary infection in pasture-based dairy cows. J. Dairy Sci. 2010;93:1468-1477.

    Not in our library10.3168/jds.2009-2410

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    Ceballos-Marquez A., Barkema H.W., Stryhn H., Wichtel J.J., Neumann J., Mella A., Kruze J., Espindola M.S., Wittwer F. The effect of selenium supplementation before calving on early-lactation udder health in pastured dairy heifers. J. Dairy Sci. 2010;93:4602-4612.

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    Machado V.S., Bicalho M.L., Pereira R.V., Caixeta L.S., Knauer W.A., Oikonomou G., Gilbert R.O., Bicalho R.C. Effect of an injectable trace mineral supplement containing selenium, copper, zinc, and manganese on the health and production of lactating Holstein cows. Vet. J. 2013;197:451-456.

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    Ran L., Wu X., Shen X., Zhang K., Ren F., Huang K. Effects of selenium form on blood and milk selenium concentrations, milk component and milk fatty acid composition in dairy cows. J. Sci. Food Agric. 2010;90:2214-2219.

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    Muñiz-Naveiro O., Domínguez-González R., Bermejo-Barrera A., Cocho J.A., Fraga J.M., Bermejo-Barrera P. Determination of total selenium and selenium distribution in the milk phases in commercial cow’s milk by HG-AAS. Anal. Bioanal. Chem. 2005;381:1145-1151.

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    Eulogio G.L.J., Hugo C.V., Antonio C.N., Alejandro C.-I., Juan M.Q. Effects of the selenium and vitamin E in the production, physicochemical composition and somatic cell count in milk of Ayrshire cows. J. Anim. Vet. Adv. 2012;11:687-691.

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    Kim J., Van Soest P.J., Combs G.F. Studies on the effects of selenium on rumen microbial fermentation in vitro. Biol. Trace Elem. Res. 1997;56:203-213.

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    Van Soest P.J. Nutritional Ecology of the Ruminant. 1994;476.

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    Macfarlane G.T., Gibson G.R., Beatty E., Cummings J.H. Estimation of shortchain fatty production from protein by human intestinal bacteria on branched-chain fatty acid measurements. FEMS Microbiol. Ecol. 1992;101:81-88.

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    Galbraith M.L., Vorachek W.R., Estill C.T., Whanger P.D., Bobe G., Davis T.Z., Hall J.A. Rumen microorganisms decrease bioavailability of inorganic selenium supplements. Biol. Trace Elem. Res. 2016;171:338-343.

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    Hall J.A., Van Saun R.J., Bobe G., Stewart W.C., Vorachek W.R., Mosher W.D., Nichols T., Forsberg N.E., Pirelli G.J. Organic and inorganic selenium: I. Oral bioavailability in ewes. J. Anim. Sci. 2012;90:568-576.

    Not in our library10.2527/jas.2011-4075

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    Hidiroglou M., Jenkins K.J. Fate of Se-75-selenomethionine in gastrointestinal-tract of sheep. Can. J. Anim. Sci. 1973;53:527-536.

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    Turner R.J., Weiner J.H., Taylor D.E. Selenium metabolism in Escherichia coli. Biometals. 1998;11:223-227.

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    Eun J.S., Davis T.Z., Vera J.M., Miller D.N., Panter K.E., ZoBell D.R. Addition of high concentration of inorganic selenium in orchardgrass (Dactylis glomerata L.) hay diet does not interfere with microbial fermentation in mixed ruminal microorganisms in continuous cultures. Prof. Anim. Sci. 2013;29:39-45.

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    Mihaliková K., Grešáková Ľ., Boldižárová K., Faix Š., Leng Ľ., Kišidayová S. The effects of organic selenium supplementation on the rumen ciliate population in sheep. Folia Microbiol. 2005;50:353-356.

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    Faixová Z., Piešová E., Maková Z., Čobanová K., Faix Š. Effect of dietary supplementation with selenium-enriched yeast or sodium selenite on ruminal enzyme activities and blood chemistry in sheep. Acta Vet. Brno. 2016;85:185-194.

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    Karl J.P., Alemany J.A., Koenig C., Kraemer W.J., Frystyk J., Flyvbjerg A., Young A.J., Nindl B.C. Diet, body composition, and physical fitness influences on IGF-I bioactivity in women. Growth Horm. IGF Res. 2009;19:491-496.

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    McElwee K., Hoffmann R. Growth factors in early hair follicle morphogenesis. Eur. J. Dermatol. 2000;10:341-350.

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    Ristow M., Schmeisser S. Extending life span by increasing oxidative stress. Free Radic. Biol. Med. 2011;51:327-336.

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    Lindner G., Botchkarev V.A., Botchkareva N.V., Ling G., van der Veen C., Paus R. Analysis of apoptosis during hair follicle regression (catagen). Am. J. Pathol. 1997;151:1601-1617.

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    Ahn S.Y., Pi L.Q., Hwang S.T., Lee W.S. Effect of IGF-I on hair growth is related to the anti-apoptotic Effect of IGF-I and up-regulation of PDGF-A and PDGF-B. Ann. Dermatol. 2012;24:26-31.

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    Kamp H., Geilen C.C., Sommer C., Blume-Peytavi U. Regulation of PDGF and PDGF receptor in cultured dermal papilla cells and follicular keratinocytes of the human hair follicle. Exp. Dermatol. 2003;12:662-672.

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    Ullrich A., Schlessinger J. Signal transduction by receptors with tyrosine kinase activity. Cell. 1990;61:203-212.

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    Jones J.I., Clemmons D.R. Insulin-like growth factors and their binding proteins: Biological actions. Endocr. Rev. 1995;16:3-34.

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    Ludvíková E., Pavlata L., Vyskočil M., Jahn P. Selenium status of horses in the Czech Republic. Acta Vet. Brno. 2005;74:369-375.

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    Pavlata L., Pechová A., Illek J. Direct and indirect assessment of selenium status in cattle—A comparison. Acta Vet. Brno. 2000;69:281-287.

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    Slavík P., Illek J., Rajmon R., Zelený T., Jílek F. Selenium dynamics in the blood of beef cows and calves fed diets supplemented with organic and inorganic selenium sources and the effect on reproduction. Acta Vet. Brno. 2008;77:11-15.

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    Harapin I., Bauer M., Bedrica L., Potočnjak D. Correlation between glutathione peroxidase activity and the quantity of selenium in the whole blood of beef calves. Acta Vet. Brno. 2000;69:87-92.

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    Jovanović B.I.V.M., Veličković M., Milanović S., Valčić O., Gvozdić D., Vranješ-Đurić S. Supplemental selenium reduces the levels of biomarkers of oxidative and general stress in peripartum dairy cows. Acta Vet. Beograd. 2015;65:191-201.

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    Pavlata L., Misurova L., Pechova A., Husakova T., Dvorak R. Direct and indirect assessment of selenium status in sheep—A comparison. Vet. Med. 2012;57:219-223.

    Not in our library

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    Pechova A., Pavlata L., Illek J. Blood and tissue selenium determination by hydride generation atomic absorption spectrophotometry. Acta Vet. Brno. 2005;74:483-490.

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    Slavík P., Illek J., Zelený T. Selenium status in heifers, late pregnancy cows and their calves in the Šumava Region, Czech Republic. Acta Vet. Brno. 2007;76:519-524.

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    Chung J.Y., Kim J.H., Ko Y.H., Jang I.S. Effects of dietary supplemented inorganic and organic selenium on antioxidant defense systems in the intestine, serum, liver and muscle of Korean native goats. Asian Australas. J. Anim. 2007;20:52-59.

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    Stockdale C.R., Gill H.S. Effect of duration and level of supplementation of diets of lactating dairy cows with selenized yeast on selenium concentrations in milk and blood after the withdrawal of supplementation. J. Dairy Sci. 2011;94:2351-2359.

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    Balán J., Vosmanská M., Száková J., Mestek O. Speciační analýza selenu v odtučněném řepkovém šrotu. Chem. Listy. 2014;108:256-263.

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    Juniper D.T., Phipps R.H., Jones A.K., Bertin G. Selenium supplementation of lactating dairy cows: Effect on selenium concentration in blood, milk, urine, and feces. J. Dairy Sci. 2006;89:3544-3551.

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    Konvičná J., Vargová M., Paulíková I., Kováč G., Kostecká Z. Oxidative stress and antioxidant status in dairy cows during prepartal and postpartal periods. Acta Vet. Brno. 2015;84:133-140.

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    Kralik Z., Kralik G., Biazik E., Straková E., Suchý P. Effects of organic selenium in broiler feed on the content of selenium and fatty acid profile in lipids of thigh muscle tissue. Acta Vet. Brno. 2013;82:277-282.

    Not in our library10.2754/avb201382030277

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    Faixová Z., Faix Š., Bořutová R., Leng Ľ. Efficacy of dietary selenium to counteract toxicity of deoxynivalenol in growing broiler chickens. Acta Vet. Brno. 2007;76:349-356.

    Not in our library10.2754/avb200776030349

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    Kuricová S., Boldižárová K., Grešáková Ľ., Levkut M., Leng Ľ. Chicken selenium satus when fed a diet supplemented with Se-yeast. Acta Vet. Brno. 2003;72:339-346.

    Not in our library10.2754/avb200372030339

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    Liesegang A., Staub T., Wichert B., Wanner M., Kreuzer M. Effect of vitamin E supplementation of sheep and goats fed diets supplemented with polyunsaturated fatty acids and low in Se. J. Anim. Physiol. Anim. Nutr. (Berl.). 2008;92:292-302.

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  283. 283.

    Feldmann J., Salaün P., Lombi E. Critical review perspective: Elemental speciation analysis methods in environmental chemistry—Moving towards methodological integration. Environ. Chem. 2009;6:275-289.

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    Sanz-Medel A. Trace element analytical speciation in biological systems: Importance, challenges and trends. Spectrochim. Acta Part B Atomic Spectrosc. 1998;53:197-211.

    Not in our library10.1016/s0584-8547(97)00135-3

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    Szpunar J., McSheehy S., Połeć K., Vacchina V., Mounicou S., Rodriguez I., Łobiński R. Gas and liquid chromatography with inductively coupled plasma mass spectrometry detection for environmental speciation analysis—Advances and limitations. Spectrochim. Acta Part B Atomic Spectrosc. 2000;55:779-793.

    Not in our library10.1016/s0584-8547(00)00210-x

  286. 286.

    Michalke B. The coupling of LC to ICP-MS in element speciation—Part II: Recent trends in application. Trends Anal. Chem. 2002;21:154-165.

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    Takahashi K., Suzuki N., Ogra Y. Bioavailability Comparison of Nine Bioselenocompounds In Vitro and In Vivo. Int. J. Mol. Sci. 2017;18:506.

    Not in our library10.3390/ijms18030506

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    Kahakachchi C., Boakye H.T., Uden P.C., Tyson J.F. Chromatographic speciation of anionic and neutral selenium compounds in Se-accumulating Brassica juncea (Indian mustard) and in selenized yeast. J. Chromatogr. A. 2004;1054:303-312.

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  289. 289.

    Kotrebai M., Birringer M., Tyson J.F., Block E., Uden P.C. Selenium speciation in enriched and natural samples by HPLC-ICP-MS and HPLC-ESI-MS with perfluorinated carboxylic acid ion-pairing agents. Analyst. 2000;125:71-78.

    Not in our library10.1039/a906320j

  290. 290.

    Li H.F., Lombi E., Stroud J.L., McGrath S.P., Zhao F.J. Selenium speciation in soil and rice: Influence of water management and Se fertilization. J. Agric. Food Chem. 2010;58:11837-11843.

    Not in our library10.1021/jf1026185

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    McSheehy S., Kelly J., Tessier L., Mester Z. Identification of selenomethionine in selenized yeast using two-dimensional liquid chromatography-mass spectrometry based proteomic analysis. Analyst. 2005;130:35-37.

    Not in our library10.1039/b414246b

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    Montes-Bayón M., Molet M.J., González E.B., Sanz-Medel A. Evaluation of different sample extraction strategies for selenium determination in selenium-enriched plants (Alliumsativum and Brassicajuncea) and Se speciation by HPLC-ICP-MS. Talanta. 2006;68:1287-1293.

    Not in our library10.1016/j.talanta.2005.07.040

  293. 293.

    Slekovec M., Goessler W. Accumulation of selenium in natural plants and selenium supplemented vegetable and selenium speciation by HPLC-ICPMS. Chem. Speciat. Bioavailab. 2005;17:63-73.

    Not in our library10.3184/095422905782774919

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    Cuderman P., Kreft I., Germ M., Kovacevic M., Stibilj V. Selenium species in selenium-enriched and drought-exposed potatoes. J. Agric. Food Chem. 2008;56:9114-9120.

    Not in our library10.1021/jf8014969

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    Cuderman P., Ožbolt L., Kreft I., Stibilj V. Extraction of Se species in buckwheat sprouts grown from seeds soaked in various Se solutions. Food Chem. 2010;123:941-948.

    Not in our library10.1016/j.foodchem.2010.04.063

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    Pedrero Z., Encinar J.R., Madrid Y., Cámara C. Identification of selenium species in selenium-enriched Lens esculenta plants by using two-dimensional liquid chromatography-inductively coupled plasma mass spectrometry and [77Se]selenomethionine selenium oxide spikes. J. Chromatogr. A. 2007;1139:247-253.

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  297. 297.

    Smrkolj P., Stibilj V., Kreft I., Germ M. Selenium species in buckwheat cultivated with foliar addition of Se(VI) and various levels of UV-B radiation. Food Chem. 2006;96:675-681.

    Not in our library10.1016/j.foodchem.2005.05.002

  298. 298.

    Montes-Bayón M., LeDuc D.L., Terry N., Caruso J.A. Selenium speciation in wild-type and genetically modified Se accumulating plants with HPLC separation and ICP-MS/ES-MS detection. J. Anal. Atomic Spectrom. 2002;17:872-879.

    Not in our library10.1039/b202608m

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    Van Saun R.J. Rational approach to selenium supplementation essential. Feedstuffs. 1990;15:15-17.

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    National Research Council (NRC). Selenium in Nutrition. 1983;107-113.

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    Tracy M.L., Möller G. Continuous flow vapor generation for inductively coupled argon plasma spectrometric analysis. Part 1: Selenium. J. Assoc. Off. Anal. Chem. 1990;73:404-410.

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    Koh T.S. Interlaboratory study of blood selenium determinations. J. Assoc. Off. Anal. Chem. 1987;70:664-667.

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    Calamari L., Ferrari A., Bertin G. Effect of selenium source and dose on selenium status of mature horses. J. Anim. Sci. 2009;87:167-178.

    Not in our library10.2527/jas.2007-0746

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    Constable P.D., Hinchcliff K.W., Done S.H., Grünberg W. Veterinary Medicine: A Textbook of the Diseases of Cattle, Horses, Sheep, Pigs, and Goats. 2017;2356.

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    Kojouri G.A., Sharifi S. Preventing effects of nano-selenium particles on serum concentration of blood urea nitrogen, creatinine, and total protein during intense exercise in donkey. J. Equine Vet. Sci. 2013;33:597-600.

    Not in our library10.1016/j.jevs.2012.09.008

  306. 306.

    Montgomery J.B., Wichtel J.J., Wichtel M.G., McNiven M.A., McClure J.T., Markham F., Horohov D.W. Effects of selenium source on measures of selenium status and immune function in horses. Can. J. Vet. Res. 2012;76:281-291.

    Not in our library

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    Maas J., Galey F.D., Peauroi J.R., Case J.T., Littlefield E.S., Gay C.C., Koller L.D., Crisman R.O., Weber D.W., Warner D.W., et al. The correlation between serum selenium and blood selenium in cattle. J. Vet. Diagn. Investig. 1992;4:48-52.

    Not in our library10.1177/104063879200400111

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    Chadio S.E., Kotsampasi B.M., Menegatos J.G., Zervas G.P., Kalogiannis D.G. Effect of selenium supplementation on thyroid hormone levels and selenoenzyme activities in growing lambs. Biol. Trace Elem. Res. 2006;109:145-154.

    Not in our library10.1385/bter:109:2:145

  309. 309.

    Fortier M.E., Audet I., Giguère A., Laforest J.P., Bilodeau J.F., Quesnel H., Matte J.J. Effect of dietary organic and inorganic selenium on antioxidant status, embryo development, and reproductive performance in hyperovulatory first-parity gilts. J. Anim. Sci. 2012;90:231-240.

    Not in our library10.2527/jas.2010-3340

  310. 310.

    Kim Y.Y., Mahan D.C. Comparative effects of high dietary levels of organic and inorganic selenium on selenium toxicity of growing-finishing pigs. J. Anim. Sci. 2001;79:942-948.

    Not in our library10.2527/2001.794942x

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    Yin S.A., Sato I., Yamagushi K. Comparison of selenium level and glutathione peroxidase activity in tissues of vitamin B6 deficient rats fed sodium selenite or dl selenomethionine. J. Nutr. Biochem. 1992;3:633-639.

    Not in our library10.1016/0955-2863(92)90082-t

  312. 312.

    Kim Y.Y., Mahan D.C. Prolonged feeding of high dietary levels of organic and inorganic selenium to gilts from 25 kg body weight through one parity. J. Anim. Sci. 2001;79:956-966.

    Not in our library10.2527/2001.794956x

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    Pavlata L., Pechová A., Bečvář O., Illek J. Selenium status in cattle at slaughter: Analyses of blood, skeletal muscle, and liver. Acta Vet. Brno. 2001;70:277-284.

    Not in our library10.2754/avb200170030277

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    Stowe H.D., Herdt T.H. Clinical assessment of selenium status of livestock. J. Anim. Sci. 1992;70:3928-3933.

    Not in our library10.2527/1992.70123928x

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    Campbell J.R., Jim G.K., Booker C.W., Guichon P.T. A survey of the selenium status of beef cows in Alberta. Can. Vet. J. 1995;36:698-702.

    Not in our library

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    Gunter S.A., Beck P.A., Phillips J.K. Effects of supplementary selenium source on the performance and blood measurements in beef cows and their calves. J. Anim. Sci. 2003;81:856-864.

    Not in our library10.2527/2003.814856x

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    Premarathna H.L., McLaughlin M.J., Kirby J.K., Hettiarachchi G.M., Beak D., Stacey S., Chittleborough D.J. Potential availability of fertilizer selenium in field capacity and submerged soils. Soil. Sci. Soc. Am. J. 2010;74:1589-1596.

    Not in our library10.2136/sssaj2009.0416

  318. 318.

    Roca-Perez L., Gil C., Cervera M.L., Gonzálvez A., Ramos-Miras J., Pons V., Bech J., Boluda R. Selenium and heavy metals content in some Mediterranean soils. J. Geochem. Explor. 2010;107:110-116.

    Not in our library10.1016/j.gexplo.2010.08.004

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    Zachara B.A., Pawluk H., Bloch-Boguslawska E., Sliwka K.M., Korenkiewicz J., Skok Z., Ryć K. Tissue level, distribution, and total body selenium content in healthy and diseased humans in Poland. Arch. Environ. Health. 2001;56:461-466.

    Not in our library10.1080/00039890109604483

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    Gupta U.C., Gupta S.C. Selenium in soils and crops, its deficiencies in livestock and humans: Implications for management. Commun. Soil Sci. Plant Anal. 2000;31:1791-1807.

    Not in our library10.1080/00103620009370538

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    Delesalle C., de Bruijn M., Wilmink S., Vandendriessche H., Mol G., Boshuizen B., Plancke L., Grinwis G. White muscle disease in foals: Focus on selenium soil content. A case series. BMC Vet. Res. 2017;13.

    Not in our library10.1186/s12917-017-1040-5

  322. 322.

    Jones G.D., Droz B., Greve P., Gottschalk P., Poffet D., McGrath S.P., Seneviratne S.I., Smith P., Winkel L.H. Selenium deficiency risk predicted to increase under future climate change. Proc. Natl. Acad. Sci. USA. 2017;114:2848-2853.

    Not in our library10.1073/pnas.1611576114

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    Supriatin S., Weng L., Comans R.N. Selenium speciation and extractability in Dutch agricultural soils. Sci. Total Environ. 2015;532:368-382.

    Not in our library10.1016/j.scitotenv.2015.06.005

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    Dinh Q.T., Li Z., Tran T.A.T., Wang D., Liang D. Role of organic acids on the bioavailability of selenium in soil: A review. Chemosphere. 2017;184:618-635.

    Not in our library10.1016/j.chemosphere.2017.06.034

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    Awadeh F.T., Kincaid R.L., Johnson K.A. Effect of level and source of dietary selenium on concentrations of thyroid hormones and immunoglobulins in beef cows and calves. J. Anim. Sci. 1998;76:1204-1215.

    Not in our library10.2527/1998.7641204x

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    Ursini F., Maiorino M., Roveri A. Phospholipid hydroperoxide glutathione peroxidase (PHGPx): More than an antioxidant enzyme? Biomed. Environ. Sci. 1997;10:327-332.

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    Maas J., Peauroi J.R., Tonjes T., Karlonas J., Galey F.D., Han B. Intramuscular selenium administration in selenium-deficient cattle. J. Vet. Int. Med. 1993;7:342-348.

    Not in our library10.1111/j.1939-1676.1993.tb01029.x

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    Hogan J.S., Smith K.L., Weiss W.P., Todhunter D.A., Schockey W.L. Relationships among vitamin E, selenium, and bovine blood neutrophils. J. Dairy Sci. 1990;73:2372-2378.

    Not in our library10.3168/jds.s0022-0302(90)78920-5

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    Ellison R.S. A review of copper and selenium reference ranges in cattle and sheep. Vet. Contin. Educ. Massey Univ. 1992;145:3-27.

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    Juniper D.T., Phipps R.H., Givens D.I., Jones A.K., Green C., Bertin G. Tolerance of ruminant animals to high dose in-feed administration of a selenium-enriched yeast. J. Anim. Sci. 2008;86:197-204.

    Not in our library10.2527/jas.2006-773

  331. 331.

    Brigelius-Flohé R., Maiorino M. Glutathione peroxidases. Biochim. Biophys. Acta. 2013;1830:3289-3303.

    Not in our library10.1016/j.bbagen.2012.11.020

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    Bermingham E.N., Hesketh J.E., Sinclair B.R., Koolaard J.P., Roy N.C. Selenium-enriched foods are more effective at increasing glutathione peroxidase (GPx) activity compared with selenomethionine: A meta-analysis. Nutrients. 2014;6:4002-4031.

    Not in our library10.3390/nu6104002

  333. 333.

    Han D., Xie S., Liu M., Xiao X., Liu H., Zhu X., Yang Y. The effects of dietary selenium on growth performances, oxidative stress and tissue selenium concentration of gibel carp (Carassius auratus gibelio). Aquac. Nutr. 2011;17:e741-e749.

    Not in our library10.1111/j.1365-2095.2010.00841.x

  334. 334.

    Dalto B.D., Tsoi S., Audet I., Dyck M.K., Foxcroft G.R., Matte J.J. Gene expression of porcine blastocysts from gilts fed organic or inorganic selenium and pyridoxine. Reproduction. 2015;149:31-42.

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    Niedźwiedź A., Nicpoń J., Zawadzki M., Służewska-Niedźwiedź M., Januszewska L. The influence of road transport on the activities of glutathione reductase, glutathione peroxidase, and glutathione-S-transferase in equine erythrocytes. Vet. Clin. Pathol. 2012;41:123-126.

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    Hill G.M., Link J.E., Meyer L., Fritsche K.L. Effect of vitamin E and selenium on iron utilization in neonatal pigs. J. Anim. Sci. 1999;77:1762-1768.

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    Mahan D.C. Effect of organic and inorganic selenium sources and levels on sow colostrum and milk selenium content. J. Anim. Sci. 2000;78:100-105.

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    Knowles S.O., Grace N.D., Wurms K., Lee J. Significance of amount and form of dietary selenium on blood, milk, and casein selenium concentrations in grazing cows. J. Dairy Sci. 1999;82:429-437.

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    Svoboda M., Kotrbáček V., Ficek R., Drábek J. Effect of Organic Selenium from Se-enriched Alga (Chlorella spp.) on Selenium Transfer from Sows to Their Progeny. Acta Vet. Brno. 2009;78:373-377.

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    Trávníček J., Racek J., Trefil L., Rodinová H., Kroupová V., Illek J., Doucha J., Písek L. Activity of glutathione peroxidase (GSH-Px) in the blood of ewes and their lambs receiving the selenium-enriched unicellular alga Chlorella. Czech J. Anim. Sci. 2008;53:292-298.

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    Valčić O., Jovanović I., Milanović S., Gvozdić D. Selenium status of feedstuffs and grazing ewes in Serbia. Acta Vet. Beaograd. 2013;63:665-675.

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    Değer Y., Ertekin A., Değer S., Mert H. Lipid peroxidation and antioxidant potential of sheep liver infected naturally with distomatosis. Turk. Parazitol. Derg. 2008;32:23-26.

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    Yaralioglu-Gurgoze S., Cetin H., Cen O., Yilmaz S., Atli M.O. Changes in malondialdehyde concentrations and glutathione peroxidase activity in purebred Arabian mares with endometritis. Vet. J. 2005;170:135-137.

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    Mélo S.K., Diniz A.I., de Lira V.L., de Oliveira Muniz S.K., da Silva G.R., Manso H.E., Manso Filho H.C. Antioxidant and haematological biomarkers in different groups of horses supplemented with polyunsaturated oil and vitamin E. J. Anim. Physiol. Anim. Nutr. (Berl.). 2016;100:852-859.

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    El-Bahr S.M., El-Deeb W.M. Acute-phase proteins, oxidative stress biomarkers, proinflammatory cytokines, and cardiac troponin in Arabian mares affected with pyometra. Theriogenology. 2016;86:1132-1136.

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    Sankari S., Atroshi F. Effect of dietary selenium on erythrocyte glutathione peroxidase and blood selenium in two types of Finnisheep genetically selected for high and low glutathione peroxidase activity. Zbl. Vet. Med. A. 1983;30:452.

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    Tietze F. Enzymatic method for the quantitative determination of nanogram amounts of total and oxidized glutathione: Applications to mammalian blood and other tissues. Anal. Biochem. 1969;27:502-522.

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    Jentzsch A.M., Bachmann H., Fürst P., Biesalski H.K. Improved analysis of malondialdehyde in human body fluids. Free Radic. Biol. Med. 1996;20:251-256.

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    Gérard-Monnier D., Erdelmeier I., Régnard K., Moze-Henry N., Yadan J.C., Chaudière J. Reactions of 1-methyl-2-phenylindole with malondialdehyde and 4-hydroxyalkenals. Analytical applications to a colorimetric assay of lipid peroxidation. Chem. Res. Toxicol. 1998;11:1176-1183.

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