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The role of bile acids in carcinogenesis

Tadeja Režen, Damjana Rozman, Tünde Kovács and 4 more

Cellular and Molecular Life Sciences · 2022 · Review · CC BY

Abstract

Bile acids are soluble derivatives of cholesterol produced in the liver that subsequently undergo bacterial transformation yielding a diverse array of metabolites. The bulk of bile acid synthesis takes place in the liver yielding primary bile acids; however, other tissues have also the capacity to generate bile acids (e.g. ovaries). Hepatic bile acids are then transported to bile and are subsequently released into the intestines. In the large intestine, a fraction of primary bile acids is converted to secondary bile acids by gut bacteria. The majority of the intestinal bile acids undergo reuptake and return to the liver. A small fraction of secondary and primary bile acids remains in the circulation and exert receptor-mediated and pure chemical effects (e.g. acidic bile in oesophageal cancer) on cancer cells. In this review, we assess how changes to bile acid biosynthesis, bile acid flux and local bile acid concentration modulate the behavior of different cancers. Here, we present in-depth the involvement of bile acids in oesophageal, gastric, hepatocellular, pancreatic, colorectal, breast, prostate, ovarian cancer. Previous studies often used bile acids in supraphysiological concentration, sometimes in concentrations 1000 times higher than the highest reported tissue or serum concentrations likely eliciting unspecific effects, a practice that we advocate against in this review. Furthermore, we show that, although bile acids were classically considered as pro-carcinogenic agents (e.g. oesophageal cancer), the dogma that switch, as lower concentrations of bile acids that correspond to their serum or tissue reference concentration possess anticancer activity in a subset of cancers. Differences in the response of cancers to bile acids lie in the differential expression of bile acid receptors between cancers (e.g. FXR vs. TGR5). UDCA, a bile acid that is sold as a generic medication against cholestasis or biliary surge, and its conjugates were identified with almost purely anticancer features suggesting a possibility for drug repurposing. Taken together, bile acids were considered as tumor inducers or tumor promoter molecules; nevertheless, in certain cancers, like breast cancer, bile acids in their reference concentrations may act as tumor suppressors suggesting a Janus-faced nature of bile acids in carcinogenesis.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 18, 2026. Paragraph numbers are ours, so an answer can point at one.

Background

1Bile acids (BAs) belong to cholesterol-derived sterols. Due to the side chain carboxyl group and hydroxylation of their steroid ring they are more polar than cholesterol. They have an amphipatic character for which they are known as natural detergents. Majority of cholesterol is excreted by bile acids that are prone to enterohepatic circulation between the gallbladder and the liver. Cholesterol absorption in the intestine and cholesterol secretion into the bile both require bile salts, which are, together with enterohepatic circulation of BAs, crucial for balancing the plasma cholesterol level.

2BAs are also signaling molecules. They deorphanized the farnesoid X nuclear receptor (FXR) which is now known as a ligand-inducible transcription factor responsive to BAs. It is important to note that BAs are metabolized in a similar manner as xenobiotics, contributing to the cross-talk between the endogenous and xenobiotic metabolism in the liver through nuclear receptors Pregnane X receptor (PXR), constitutive androstane receptor (CAR) and others. While their synthesis takes place exclusively in the liver, the homeostasis and excretion involve multiple organs and compartments in the body. After discovering their signaling role, BAs have been considered as pro-carcinogenic molecules. However, recent studies have provided evidence that in certain cancers, BAs can have antineoplastic features (e.g. breast cancer). This novel, context-dependent, dualistic finding prompted us to thoroughly assess the involvement of BAs in carcinogenesis and cancer progression.

Bile acid biosynthesis

3The excess of free cholesterol is toxic to cells and needs to be excreted, primarily through conversion to more polar BAs. The introduction of a hydroxyl group in cholesterol reduces the half-life and directs the oxidized molecule to excretion. BA synthesis is thus the main cholesterol detoxification pathway where multiple cytochrome P450 (CYP) enzymes are involved in the classical or alternative pathways (Fig. 1). The two major primary BAs in humans are cholic acid (CA) and chenodeoxycholic acid (CDCA). They are synthesized in the liver and secreted into the gallbladder as glycine or taurine conjugates. The BA composition in mice substantially differs from the humans which has to be taken into account when using mouse as a model for BA related diseases. The mouse Cyp2c70 metabolizes CDCA to more hydrophilic primary muricholic acids (MCAs).

4The first enzyme of the classical BA synthesis pathway is cholesterol 7α-hydroxylase (CYP7A1), leading to 7α-cholesterol in a rate-limiting reaction step, followed by several enzymatic conversions. This enzyme is prone to the negative feedback regulation by BAs and FXR. Sterol 12α-hydroxylase (CYP8B1) lies at the branching point that leads to CA. Sterol 27-hydroxylase (CYP27A1) is needed for both CA and CDCA. In the alternative pathway, cholesterol is first metabolized by CYP27A1 to form 27-hydroxycholesterol that is a substrate for 25-hydroxycholesterol 7α-hydroxylase (CYP7B1) and later other enzymes. The alternative pathway leads majorly to CDCA. The ratio of CA to CDCA is determined by the expression level of CYP8B1, which transforms a di-hydroxylated BA to tri-hydroxylated BA. The alternative pathway is estimated to account for about 10% of cholesterol conversion. Of importance, there are major differences in individual BA synthesis genes in mouse and in humans which may be due also to different biological roles of human and mouse BA species (reviewed in).

Bacterial metabolism of bile acids, production of secondary bile acids

5Hepatocytes secrete BAs to the bile canaliculi. By fusing with each other bile canaliculi form bile ducts, which eventually form the hepatic duct that runs to the gallbladder. The gallbladder empties to the duodenum upon feeding and, hence, releases BAs to the gastrointestinal tract. Primary BAs emulsify dietary fats and activate pancreatic lipases in the small bowel. BAs are then reabsorbed through the enterocytes and get to the liver for reuptake and reuse through the portal circulation. This circle is termed the enterohepatic circulation of BAs. A fraction of the reabsorbed BAs enter the systemic circulation (total BA concentration in the serum is < 5 µM in a healthy individual) and exert hormone-like effects. The reference concentrations of the serum, tissue and fecal bile acids are in Tables 1, 2, 3.

6BAs are very powerful surfactants; therefore, bacteria, mostly in the large bowel, need to protect themselves against being disintegrated by BAs. For example, lipopolysaccharides serve as membrane components in Gram-negative bacteria to passively ward off external toxins or BAs. In addition to that, bacteria have a more sophisticated enzymatic system to cope with BAs termed BA conversion.

7The hydroxyl groups and the tauryl or glycyl conjugate on BAs are crucial elements of the molecular structure of BAs for their strong surfactant properties. Therefore, the removal, modification or substitution of these molecular elements diminishes the potentially toxic features of primary BAs and renders them largely apolar. The dehydroxylated primary BAs are called secondary BAs and the main site for converting primary BAs to secondary BAs is the large bowel. Secondary BAs can be resorbed to the portal circulation and are transported to the liver, where, however, hydroxylation and conjugation needs to be restored for reuse. The main secondary BAs in humans are lithocholic acid (LCA), deoxycholic acid (DCA) and to a lesser extent, ursodeoxycholic acid (UDCA).

8Bile salt hydrolases (BSHs) are responsible for the deconjugation of BAs, namely the removal of glycine or taurine by breaking the C24 N-acyl bond. Glycine and taurine can be fed into the metabolism of bacteria to be used as an energy source. BSH activity is common among the bacteria inhabiting the small and the large intestines; both aerobic and anaerobic bacteria can deconjugate bile salts. Namely, among the Gram-positive bacteria BSH was identified in Clostridium, Enterococcus, Bifidobacterium, Lactobacillus, Streptococcus, Eubacterium and Listeria, among Gram-negative bacteria in Bacteroides, while among archea Methanobrevibacter smithii and Methanosphera stadmanae.

9The substituents on the gonane core of BAs can be also modified, the term “secondary BA” typically stands for the removal of 7α or 7β-hydroxyl groups from primary BAs. Clostridiales and Eubacteria were shown to play a major role in dehydroxylation, although other genre or species were also implicated (e.g. Bacteroidetes, Escherichia). Although BA deconjugation and dehydroxylation are different processes, they may be linked through regulatory circuits. Other reactions of BAs involve oxidation, and epimerization that can be linked to intestinal Firmicutes (Clostridium, Eubacterium, and Ruminococcus), Bacteroides and Escherichia. Bacterial enzymes involved in secondary BA production are assembled in the BA inducible (bai) operon. Collectively, BA transformation renders secondary BAs hydrophobic and BAs loose their ability to act as detergents or toxins to bacteria. Moreover, these changes are vital in fine-tuning the affinity of BAs to BA receptors.

10Interactions between BAs and gut microbiota are bidirectional. Microbiota can transform primary BAs and, hence, modulate the composition of the BA pool. Inversely, BAs can influence the composition of the microbiome as well and facilitate bacterial translocation to tissues, further underlining that notion BAs act as potent drivers of the early intestinal microbiota maturation. Oncobiosis (dysbiosis associated with cancers) can alter the secondary BA pool that may contribute to carcinogenic effects. It is of note that several other non-BA bacterial metabolites are known that play role in carcinogenesis.

Bile acid transporters

11The enterohepatic circulation of BAs depends on BA transporters in the gastrointestinal system. Almost 90% of BAs are involved in circulation due to efficient active transport. Different uptake and efflux BAs transporters are present in the hepatic and intestinal cells (Fig. 2). After BAs are synthesized in the liver they are transported into the bile mainly by the ATP-dependent cassette transporter (BSEP), but also minor transporters, the multidrug resistance-associated protein 2 (MRP2, ABCC2) and the multidrug resistance protein 1 (MDR1, ABCB1). From the intestinal lumen, BAs are uptaken into the intestinal cells by the major apical sodium-dependent bile acid transporter (SLC10A2, ASBT), which transports BAs also across the canalicular membrane in cholangiocytes and renal tubule apical membrane from glomerular filtrate. BAs are then effluxed into the portal circulation by two Solute Carrier Family members, SLC51A or OSTα and SLC51B or OSTβ. The bile acids are then taken back up into hepatocytes by the major transporter the solute carrier family 10 (SLC10A1, NTCP),.

12BAs can enter the systemic circulation via export across the hepatic sinusoidal membrane by OSTα/OSTβ, the multidrug resistance-associated protein 3 (MRP3, ABCC3) and the multidrug resistance-associated protein 4 (MRP4, ABCC4). The MRP transporters have a role in reducing hepatic BA concentration in cholestatic conditions. MRP3 and MRP4 are also present in cholangiocytes, where they efflux BAs to portal circulation and are part of the cholehepatic shunt together with ASBT. Several transporters are expressed in the kidney, where they participate in BA elimination via urine (Fig. 2). The Solute Carrier Organic Anion Transporter Family, OATP1B1 or SLCO1B1 and OATP1B3 or SLCO1B3 contribute to the systemic clearance of BAs via liver. Other cells also express BA transporters and can, therefore, uptake BAs from the systemic circulation.

Bile acids as signaling molecules

13In addition to their role in digestion, BAs act as signaling molecules. BAs can activate membrane receptors (Fig. 3), such as G protein-coupled bile acid receptor 1 (GPBAR1, also known as TGR5), sphingosine-1-phosphate receptor 2 (S1PR2), muscarinic receptors (CHRM2 and CHRM3) and nuclear receptors (NRs), such as farnesoid X receptor (FXR, NR1H4), PXR (NR1H2), vitamin D receptor (VDR, NR1H1), CAR (NR1H3) and liver X receptor (LXR, NR1H2-3). Each BA can interact with more than one receptor. Receptors are differentially activated by BAs. For example, FXR is activated by CDCA > DCA > LCA > CA, while TGR5 is activated by LCA > DCA > CDCA > CA, respectively. VDR and PXR are mainly activated by LCA. BAs mediate immune responses, gastrointestinal mucosal barrier function, gestation, carcinogenesis and metabolic diseases. The activation of BA receptors may lead to the induction of signaling pathways involved in the regulation of several physiological functions, such as glucose, lipid and energy metabolism, as well as, in cancers. Below, we review the mode of action of BA receptors and highlight those receptor-mediated functions that have a key role in regulating the behavior of cancer cells.

G protein-coupled bile acid receptor 1 (GPBAR1, TGR5)

14TGR5 is a member of the G protein-coupled receptor superfamily, highly expressed in the epithelium of the gallbladder, the intestine, the brown adipose tissue and the skeletal muscle, as well as in the brain. TGR5 is also expressed in human monocytes/macrophages. TGR5 is not expressed by hepatocytes, while Kupffer cells and liver sinusoidal cells can express the receptor.

15Secondary BAs LCA and DCA are the most potent, natural ligands for TGR5, but the receptor also responds to CDCA and CA and a set of artificial ligands (Table 4). Ligand binding to the TGR5 receptor triggers activation of adenylate cyclase leading to the production of cAMP and the downstream activation of extracellular signal-regulated kinase 1/2 (ERK1/2), protein kinase A (PKA), protein kinase B (AKT), mammalian target of rapamycin complex 1 (mTORC1) and Rho kinase. TGR5 activation leads to metabolic changes characterized by energy expenditure and β-oxidation. BA-dependent induction of TGR5 has immunomodulating effects. Most studies point to TGR5-dependent immunosuppression partly due to the suppression of the Toll-Like Receptor 4—Nuclear factor-κB (TLR4–NF‐κB) pathway. In line with that, in a murine model of breast cancer, LCA treatment induced the proportions of tumor-infiltrating lymphocytes through TGR5.

Sphingosine-1-phosphate receptor 2 (S1PR2)

16Conjugated BAs activate S1PR2 that upregulates the expression of sphingosine kinase 2 (SphK2), which in turn enhances the level of sphingosine-1-phosphate in the nucleus. Elevated nuclear sphingosine-1-phosphate inhibits the function of histone deacetylases resulting in the upregulation of genes encoding nuclear receptors and enzymes involved in lipid and glucose metabolism Similar to TGR5, ligand binding to S1PR2 can activate different downstream signaling pathways, such as ERK, AKT and/or c-Jun N-terminal kinase (JNK1/2). Glycochenodeoxycholic acid (GCDCA) can trigger apoptosis in hepatocytes through activating S1PR2. S1PR2 is highly expressed in macrophages and has widespread immunological roles.

Muscarinic receptors (CHRM2 and CHRM3)

17Taurine conjugated BAs can activate muscarinic receptors, the cholinergic receptor muscarinic 2 and 3 (CHRM2 and CHRM3). CHRMs are overexpressed in colon cancer cells and stimulate cell proliferation and invasion. Taurolithocholic acid (TLCA) induces cholangiocarcinoma cell growth via muscarinic acetylcholine receptor and EGFR (epithelial growth factor receptor)/ERK1/2 signaling.

Farnesoid X receptor (FXR, NR1H4)

18FXR is a member of the nuclear hormone receptor superfamily. There are two FXR genes, encoding FXRα and FXRβ of which only FXRα is expressed, FXRβ is present as a non-expressed pseudogene in humans. The FXR receptor heterodimerizes with retinoid X receptor (RXR) and binds to FXR response elements (FXREs) within the regulatory regions of its target genes. BAs are physiological ligands for FXR (with decreasing affinity: CDCA, DCA, LCA, CA). FXR is expressed mainly in the liver, intestine, kidney and adrenal glands.

19FXRα controls BA synthesis, transport and detoxification. The activation of FXR receptor by BAs reduces the expression of Cyp7a1 and Cyp8b1, key enzymes of BA biosynthesis pathway. In the liver, FXRα induces the transcription of its target gene encoding small heterodimer partner (SHP, NR5O2), an orphan nuclear hormone receptor (see in detail later) that lacks a DNA binding domain and acts as a transcriptional repressor. SHP inhibits the expression of Cyp7a1 through the inhibition of the interaction with liver receptor homolog-1 (LRH-1, NR5A2). In addition to LRH-1, SHP also prevents the function of hepatocyte nuclear factor-4α (HNF4α), a positive regulator of Cyp7a1 and Cyp8b1. In the intestine, FXRα induces the expression of fibroblast growth factor 19 (FGF19) in humans and its mouse homolog fibroblast growth factor 15 (FGF15). The secreted growth factor via portal blood reaches the liver where it binds to its receptor, fibroblast growth factor receptor 4 (FGFR4) and induces JNK and ERK pathways and causes repression of Cyp7a1, thus reducing BA synthesis. In addition to Cyp7a1, Cyp8b1 is also repressed by FXRα via SHP-dependent mechanism involving HNF4α.

20FXRα is also a key regulator of BA transport by influencing the expression of BA transporters. FXRα activation suppresses BA reuptake to hepatocytes through repressing the expression of NTCP via SHP dependent mechanism. At the same time, FXRα facilitates the efflux of BAs from hepatocytes into bile by enhancing the expression of BSEP and into the systemic circulation via OSTα/β transporter. FXR also upregulates MRP2, which promotes BA secretion into the gallbladder. Finally, FXRα activates the expression of intestinal BA-binding protein (I-BABP) in the ileum which promotes transport of BAs from enterocytes into portal blood whereas limits enterocyte uptake of BAs by reducing ASBT expression. FXRα increases the expression of enzymes involved in the detoxification of BAs, such as cholesterol 25-hydroxylase or cytochrome P450 family 3 subfamily A4 (CYP3A4), dehydroepiandrosterone-sulfotransferase (SULT) 2a1 and uridine 5′-diphosphate-glucuronosyltransferase 2B4 (UGT2B4). Many studies have reported the relationship between FXR and inflammation. NF-kB activation suppressed FXR-mediated gene expression, indicating that there is a negative crosstalk between the FXR and NF-kB signaling.

Pregnane X receptor (PXR, NR1I2)

21In humans, PXR is mainly expressed in the liver and intestine. Among BAs, the most potent ligand of PXR is LCA, and the oxidized, 3-keto form of LCA. PXR acts as a xenobiotic sensor and regulates the expression of genes involved in the detoxification and metabolism of BAs. Upon ligand binding, PXR binds to the promoter of its target gene as a heterodimer with RXR. Activation of PXR induces the uptake of xenobiotics, their modification by phase I enzymes (CYPs, including CYP3A, CYP2B, CYP2C), conjugation by phase II enzymes, such as glutathione S-transferases, UDP-glucuronosyl-transferases (UGTs) and sulfotransferases, and finally elimination by phase III drug transporters including MDR1, MRP2 and organic anion-transporting polypeptide (OATP2). The activation of PXR prevents cholesterol gallstone disease by regulating BA biosynthesis and transport and protects the liver against LCA-induced toxicity. PXR activation disrupts the interaction between HNF4α and peroxisome proliferator-activated receptor gamma coactivator 1 alpha (PGC-1α, PPARGC1A), which is required for the activation of CYP7A1 gene expression, thus reducing the expression of CYP7A1 and inhibiting the synthesis of BAs. PXR activation is anti-inflammatory. PXR activation facilitates lipogenesis, suppressing β-oxidation and ketogenesis and gluconeogenesis. Furthermore, PXR through HNF4 and PGC-1α modulates the expression of CYP7A1.

Constitutive androstane receptor (CAR, NR1I3)

22CAR is the closest relative to the PXR and is expressed primarily in the liver. First studies identified that CAR has constitutive transcriptional activity in the absence of its ligand. Later, it was reported that the constitutive transcriptional activity of CAR is reversed by androstane metabolites, which are inverse agonists. CAR can be activated by direct ligand binding and indirect activation. In the absence of ligand binding, CAR forms a heterodimer with RXR and transactivates its target genes. CAR recruits coactivators in the nucleus, such as steroid receptor coactivator 1 (SRC-1, NC0A1) and PGC-1. Similar to PXR, CAR controls the expression of drug-metabolizing enzymes and transporters, thereby supporting the detoxification of xenobiotics. In contrast to PXR, it remains unclear whether BAs can function as natural ligands for CAR; nevertheless, there are reports underscoring the involvement of CAR in BA signaling.

Vitamin D receptor (VDR, NR1I1)

23In humans, VDR is highly expressed in the kidney, intestine, bone as well as in hepatocytes but expressed at low levels in other tissues. LCA is a potent endogenous VDR ligand; hence, VDR can act as an intestinal BA sensor. VDR activation induces expression of CYP3A that metabolizes LCA. In addition, VDR induces the expression of SULT2A1, MRP3 and ASBT to stimulate BA sulfonation, excretion and transport. The activated VDR plays a role in the inhibition of BA synthesis via suppression of CYP7A1, thus protecting liver cells during cholestasis.

24VDR can function as a nuclear receptor and a membrane-bounded receptor. Upon ligand binding, VDR translocates into the nucleus, where it binds to DNA response elements as a heterodimer with RXR to mediate gene transcription. Plasma membrane-associated VDR receptor activates several signaling cascades to inhibit CYP7A1 transcription. It has been shown that the activation of membrane VDR signaling by LCA in the liver activates MEK1/2ERK1/2 pathway, which stimulates nuclear VDR/RXRα heterodimer recruitment of corepressors to inhibit CYP7A1 gene transcription. In biliary epithelial cells, bile salts (CDCA, UDCA) stimulate the expression of cathelicidin, an antimicrobial peptide, via VDR and FXR to control innate immunity. The possible role of VDR in regulating immunity and the role of VDR in different cancer cells and diseases is reviewed in detail elsewhere.

Liver X receptor (LXR, NR1H2-3)

25LXRs are activated by naturally occurring cholesterol metabolites such as oxysterols and bind to DNA as heterodimers with the RXR. LXRα (NR1H3) and LXRβ (NR1H2) share a high structural homology. LXRβ is ubiquitously expressed, while LXRα is primarily expressed in the liver, the adipose tissue, the intestine and macrophages. Upon ligand activation LXRs regulate gene expression via binding to LXR response elements in the promoter regions of the target genes. LXRα promotes the conversion of cholesterol into BAs through the induction of CYP7A1 expression in the liver. LXRs enhance the efflux of cholesterol from cells and have an anti-inflammatory response in the adipose tissue and macrophages. Hyodeoxycholic acid (HDCA), a naturally occurring secondary BA generated by bacterial C-6 hydroxylation of LCA, is a weak LXRα agonist.

Small heterodimer partner (SHP, NR5O2)

26SHP is a unique nuclear receptor that contains a ligand-binding domain but lacks the conserved DNA-binding domain. SHP acts as a transcriptional corepressor regulating different metabolic processes, including lipid, glucose, energy homeostasis and BA synthesis via interaction with multiple transcription factors and nuclear receptors (reviewed in). BAs or FGF19 signaling enhances posttranslational modifications of SHP, which modulates the regulatory function of SHP protein. SHP acts as an inhibitory regulator in Hedgehog/Gli signaling pathway.

Effects of bile acids in cancers

27The role of BAs was implicated in a wide variety of neoplasias (Fig. 4, Tables 5, 6, 7). When assessing the effects of BAs, one has to keep in mind that the concentrations applied in the experiments need to correspond to the reference concentrations in serum or the compartment in question (e.g. parts of the gastrointestinal tract). However, several reports are using substantially higher concentrations than the reference. These studies need to be considered as ones using “therapeutic” concentrations. In the forthcoming chapters, we will review those neoplasias where BAs were implicated in pathogenesis.

Oesophageal carcinoma

28The development of Barrett’s esophagus (BE) and its progression to oesophageal adenocarcinoma (EAC) are linked to gastroesophageal reflux disease (GERD). Conjugated BAs, mainly taurocholic acid (TCA) and glycocholic acid (GCA) are the main BA constituents in GERD refluxate. Conjugated BA levels in the refluxate from patients with advanced BE or EAC are significantly higher than from patients with benign BE. Conjugated BAs, as TCA or taurodeoxycholic acid (TDCA), promote EAC progression (Table 7). Unconjugated BAs, including DCA and CDCA, induce oxidative stress, DNA damage and inflammation contributing to EAC carcinogenesis, while UDCA protects against DCA-induced injury (Tables 5 and 7).

29Apparently, numerous BA receptors as TGR5, S1PR2, FXR and VDR are activated in EAC cells in response to BAs in the refluxate. In good agreement with that, the inhibition of the FXR receptor suppresses tumor cell viability in vitro and reduced tumor formation in nude mouse xenografts. Furthermore, TGR5 is highly expressed in the EAC and precancerous lesions and is associated with worse overall survival suggesting that these observations can be translated to the human situation.

30Acidic bile acids bring about oxidative stress, TDCA can induce NADPH Oxidase 5 (NOX5) through TGR5. Furthermore, bile acids can induce inflammation through FXR activation and the EGFR–STAT3 (signal transducer and activator of transcription 3)—Apurinic/Apyrimidinic Endodeoxyribonuclease 1 (APE1) pathway. Acidic bile salts can also induce epithelial–mesenchymal transition (EMT) through vascular endothelial growth factor (VEGF) signaling in Barrett's cells. Interestingly, the activation of the EGFR-DNA-PKs (DNA-dependent protein kinase) pathway by insulin-like growth factor binding protein 2 (IGFBP2) protects EAC cells against acidic bile salt-induced DNA damage.

Gastric cancer

31Carcinogenesis in gastric cancer is a sequential process that includes chronic superficial gastritis, intestinal metaplasia (IM), atrophic gastritis, intramucosal carcinoma, dysplasia and invasive neoplasia. IM is considered a risk factor for gastric tumorigenesis. The concentrations of BAs in gastric juice positively correlate with the degree of intestinal metaplasia and BAs serve a critical multipronged role in the induction of intestinal metaplasia. BAs can enhance caudal-related homeobox family 2 (CDX2) and mucin 2 (MUC2) expression via FXR/NF-κB signaling and cyclooxygenase-2 (COX-2) expression via induction of SHP, all promoting gastric intestinal metaplasia. Acidic bile salts can induce telomerase activity in a c-Myc-dependent fashion, while DCA can induce the metaplastic phenotype of gastric cancer cells (see Tables 6 and 7). TGR5 is a key factor in BA-induced gastric metaplasia via HNF4α, EGFR and mitogen-activated protein kinase (MAPK) activation and promotes EMT in gastric carcinoma cells. TGR5 is overexpressed in gastrointestinal adenocarcinomas, and moderate to strong TGR5 staining is associated with decreased patient survival. Nevertheless, there anticarcinogenic effects of bile acids in gastric cancer, as UDCA (Table 5) or DCA in supraphysiological concentrations or 23(S)-mCDCA.

Hepatocellular carcinoma (HCC)

32Several studies have shown that more hydrophobic BAs as LCA, DCA and CDCA, are the main promoters of liver cancer and can contribute to the development of HCC (see in Table 7). Nevertheless, CDCA (> 100 µM), UDCA and Tauroursodeoxycholic acid (TUDCA) inhibit HCC cell growth and induce apoptosis (see in Tables 5 and 6). Deregulation of BA homeostasis marked by the expression of hepatic BA transporters (BSEP, OSTα/β, MRP2, MDR2-3, NTCP) is diminished leading to increased hepatic BA sequestration and inflammation and reduced FXR signaling in liver cirrhosis and nonalcoholic steatohepatitis that are risk factors for the development of HCC. In good agreement with that, metabolomics identified long-term elevated serum BAs in HCC patients and children (< 5 years of age) with bile salt export pump deficiency developed HCC.

33FXR activity is a major inhibitor of HCC carcinogenesis. Whole-body FXR-deficient mice spontaneously develop liver tumors in which the activation of the Wnt/β-catenin signaling pathway and oxidative stress were identified as the major drivers. Nevertheless, liver-specific FXR deficiency in mice does not induce spontaneous liver tumorigenesis, but may only serve as a tumor initiator. Due to their amphipathic nature, BAs can disrupt the plasma membrane and activate protein kinase C (PKC) and phospholipase A2 (PLA2) inducing the p38-MAPK-p53-NFκB pathway. Inflammation can suppress FXR activity that contributes to bile acid accumulation and carcinogenesis.

34Interestingly, senescence-associated secretory phenotype has crucial role in promoting obesity-associated HCC development in mice. Administration of high-fat diet to mice induces alterations in the gut microbiota and increases the levels of DCA. Increased DCA level promotes SASP phenotype in hepatic stellate cells (HSCs), which in turn secretes various tumor-promoting factors in the liver, thus facilitating HCC development in mice exposed to chemical carcinogen. SHP has a pleiotropic role in HCC, regulates cell proliferation, apoptosis, epigenetic changes and inflammation, which are associated with the antitumor role of SHP in the development of liver cancer.

Pancreatic adenocarcinoma

35BAs are involved in the induction and development of pancreatic adenocarcinoma at multiple stages. Gallstone formation can block bile flow and, therefore, can induce and sustain pancreatitis, a risk factor for pancreatic adenocarcinoma. In fact, several BA species showed a drastic increase in pancreatic adenocarcinoma patients. Treatment of pre-malignant pancreas ductal cells with bile induced carcinogenic transformation. In pancreatic adenocarcinoma cells BAs decrease susceptibility to apoptosis, boost cell cycle progression, the expression of inflammatory mediators and cellular movement, and, in high concentrations, may perturb biomembranes (Table 7). UDCA, similar to its previously discussed beneficial properties, prevents EMT in pancreatic adenocarcinoma cell lines and, therefore, has antineoplastic properties (Table 5).

Colorectal carcinoma (CRC)

36The western diet has tumor promoting activity associated with elevated concentrations of colonic BA (mainly LCA and DCA) and increased fecal BA levels, as detected in samples from CRC patients. In animals, a high-fat diet stimulates bile discharge and results in elevated BA levels in the colon. Moreover, cholecystectomy, through prolonging BA exposure of the intestinal mucosa, has been suggested as a risk factor for the development of CRC.

37BAs induce genetic instability marked by genomic instability and DNA damage via oxidative stress, defects in mitotic checkpoints, cell cycle arrest, improper chromosome alignment and multipolar division. Genomic instability caused by BAs is coupled with apoptosis resistance due to the degradation of p53 and the inhibition of caspase-3 activity. Furthermore, secondary BAs perturb cell membranes and modulate signaling cascades. These all lead to colonic cell hyperproliferation, survival and invasion.

38The disruptive effect of BAs on colon epithelium evokes a compensatory cell renewal mechanism by inducing colonic epithelial cells to become cancer stem cells (CSCs) through β-catenin signaling (Table 7). In the CRC rodent model, both LCA and DCA have tumor promoter role on colonic crypt cells in the early stages of colon carcinogenesis; however, it is important to note that BAs are suggested as tumor promoters, but not as mutagenic agents, since they can not induce tumor formation without a carcinogen/mutagen or a genetic alteration. It should be noted that DCA in low concentrations (0.05–0.3 mM) inhibit colonic cell proliferation via cell cycle block and apoptosis pathways (Table 6).

39UDCA can reduce the concentration of toxic BA in stool and blood and has shown to protect against CRC by inhibiting CSC and CRC cell formation and proliferation, oncogenic signaling pathways, as well as, inducing tumor surveillance (Table 5). Moreover, UDCA can reduces CRC recurrence, as well as the risk to develop CRC in patients with pre-cancerous conditions, as colitis or primary biliary cirrhosis.

40Sustained inflammation was implicated in the pathogenesis of colorectal cancer due to barrier breach, and bacterial translocation leading to inflammation and neoplastic transformation of colonic epithelial cells. TGR5 activation by UDCA and LCA may also exert anti-inflammatory responses through TLR4 activation or by reducing pro-inflammatory cytokine production in the colon that can decrease the frequency of developing CRC. BAs can change the gut microbial community, suggesting that BAs may also interfere with bacterial translocation.

Breast cancer

41The BAs in the breast are of gut origin. Hepatic production of BA is reduced in breast cancer patients as marked by decreasing levels of serum and fecal BAs. Furthermore, bacterial conversion of BAs to secondary BAs is also suppressed, which is the most dominant in in situ and stage I patients. The serum bile acid composition of breast cancer and benign breast disease patients is different; specifically, breast cancer patients had higher serum chenodeoxycholic acid levels and lower dihydroxy tauro-conjugated BA (Tdi-1) and sulfated dihydroxy glyco-conjugated bile acids (Gdi-S-1). Total fecal bile acid levels are lower in breast cancer patients as compared to controls. LCA concentrations in the breast can be higher than the serum levels (Table 6). Reports showed increased DCA levels in the serum and the breast cyst fluid of breast cancer patients.

42LCA is an inhibitor of breast cancer cell proliferation (Table 6). However, the reports on DCA and UDCA are contradictory in physiological concentrations, LCA tunes cancer cell metabolism towards a more oxidative state (through AMP-activated protein kinase (AMPK), PGC-1β and NRF1/NFE2L1) and induces mild oxidative stress through reducing NRF2 (nuclear factor erythroid 2-related factor 2, NFE2L2) expression and inducing Inducible nitric oxide synthase (iNOS) that reverts EMT, reduces VEGF expression, induces antitumor immunity and changes to cancer metabolism that culminates in reduced metastasis formation. In supraphysiological concentrations (> 1 µM) LCA inhibits fatty acid biosynthesis and induces cell death. LCA does not exert antiproliferative effects in its tissue reference concentrations on non-transformed primary fibroblasts. LCA exerts its antineoplastic effects through the TGR5 (Table 6).

43CDCA in supraphysiological concentrations induces MDRs through FXR and modulates estrogen and progesterone receptor-mediated gene transcription. Furthermore, CDCA inhibits tamoxifen-resistant breast cancer cell proliferation through the activation of the FXR receptor (Table 6). In contrast to that, a report by Journe and colleagues showed that FXR activation has a positive correlation with estrogen receptor expression and luminal characteristics, as well as supported cancer cell proliferation.

Prostate cancer

44Among the BAs LCA, UDCA and CDCA exerted antiproliferative effects in prostate cancer. Activation of FXR by CDCA inhibits proliferation of prostate cancer cells, reduces lipid anabolism via inhibiting Sterol Regulatory Element Binding Transcription Factor 1 (SREBF1) and induces the expression of the tumor suppressor phosphatase and tensin homolog (PTEN) (Table 6). Interestingly, FXR signaling also controls androgen metabolism in prostate cancer cells, its activation reduces the expression of UDP-glucuronosyltransferase (UGT) 2B15 and UGT2B17 within cells and causes a reduction of androgen glucuronidation. Similar to CDCA, LCA has antiproliferative effects in prostate cancer and induces apoptosis, endoplasmic reticulum stress, autophagy and mitochondrial dysfunction (see Table 6). UDCA induces death receptor-mediated apoptosis in human prostate cancer cells (Table 5).

Ovarian cancer

45In the serum of ovarian cancer patients, 3b-hydroxy-5-cholenoic acid, GUDCA, DCA and TCDCA levels decreased; importantly, taurochenodeoxycholic acid levels decreased in early-stage epithelial ovarian cancer. Zhou and colleagues have shown that sulfolithocholylglycine and TCA showed changes in the serum of ovarian cancer patients. Changes to the BA pool are so characteristic that Guan and colleagues suggested a set of 12 BAs, including glycolithocholic acid, to be used as markers to separate healthy controls from ovarian cancer patients.

46The available studies assessed the effects of BAs at supraphysiological concentrations. These concentrations of BAs are cytotoxic and induce apoptosis likely due to changes to membrane damage that is unlikely at physiological concentrations of BAs. DCA can modulate the expression of breast cancer type 1 susceptibility protein (BRCA1) and the estrogen receptor and, through these, can control drug sensitivity of ovarian cancer cells (Table 6). Furthermore, cholylglycinate interferes with the transport of cisplatin and TCDC sensitizes ovarian carcinoma cells to doxorubicin and Mitomycin.

47LXR, PXR, VDR or CAR activation was shown to exert protective features against ovarian cancer, similar to BA-elicited effects suggesting that BAs may have a more profound role in protecting against ovarian cancer. These protective effects involved the suppression of proliferation, invasion, EMT, de novo fatty acid biosynthesis, the proportions of the cancer stem cell population, and the improvement of the efficacy of chemotherapy culminating in better patient survival. Conflicting with these observation on report provided evidence that under certain conditions PXR may support proliferation. BAs can influence the expression and the activity of multiple PARP enzymes; therefore, it is likely that BAs could modulate the efficacy of PARP inhibition that is a novel modality in the chemotherapy of ovarian cancer.

Conclusions

48Primary and secondary BAs are long-standing players in carcinogenesis. Although these molecules were considered as initiators of neoplasias, recent advances have shown that the pro- or anticarcinogenic activity of BAs varies among neoplasias, most probably due to differences in the expression of BA receptors, transporters and cell-specific differences in the outcome of receptor activation. Key pathways activated in neoplasias by BAs are regulated by nuclear receptors, FXR, CAR, SHP, PXR, LXR and VDR and other membrane receptors such as S1PR2, TGR5, CHRM2 and CHRM3. They activate numerous downstream signaling pathways such as EGFR, STAT3, MAPK, HNF4α, NF-κB, TLR4, SOCS3 and β-catenin just to name some. Furthermore, BAs regulate all aspects of tumor development and progression, the EMT, invasion, metabolism, apoptosis, proliferation, senescence, immune environment and response to chemotherapy.

49The effect of BAs on neoplasias also depends on the concentrations used in the studies. While in certain models BAs in low concentration have anti-cancer effects, in superphysiological concentrations BAs have pro-cancer effects. This phenomenon is related to their amphipathic structure and the activation of additional off-target pathways not tiggered at physiological concentration. At high concentrations, BAs may perturb membranes and activate signaling pathways that sense disturbance of membranes, such as PLA2 and PKC. At high concentrations, they are also toxic and activate the detoxifying pathways, which regulate the activity of transporters of steroid hormones and chemotherapeutics. Therefore, we would urge the community to carry out studies where the concentrations of BAs correspond to the reference concentrations established for the tissue or, as a proxy, to the serum reference concentrations. As a continuation of that, in the case of UDCA the therapeutic serum concentrations can also be used as a guide. These data are summarized in Table 1. Such studies would be invaluable to understand the (patho)physiological roles of BAs and would give a good frame for the therapeutic applicability.

50Along the same lines, it is apparent that BAs can be considered as possible treatment options in certain cancers. Foremost, UDCA, that is a therapeutically available drug, has beneficial effects in multiple neoplasias (e.g., Table 5) pointing towards the possibility for repurposing UDCA. The picture for other BAs is hazier due to frequent contradictions making it hard to outline applicability. However, before the application of BAs in neoplasias we would need to decipher the cross-talk between BAs and drug metabolism, the effect on drug efficacy and drug availability, and discover the possible adverse effects of BAs, that is currently largely missing. Moreover, it is tempting to consider the manipulation of the intestinal microbiome to affect the levels of selected secondary bile acids in humans. Finally, the modulators of BA receptors should be considered as therapeutic options as well. Given the emerging evidence on the potential anti-cancer effects of BAs, further studies are vital in order to develop novel therapeutic strategies using BAs.

Search strategy and selection criteria

51References to this review were identified through the prior knowledge of the authors that was complemented by systematic search of PubMed by using the combinations “Prostate cancer AND (bile acid)”, “Gastric cancer AND (bile acid)”, “Hepatocellular carcinoma AND (bile acid)”, “Oesophageal cancer AND (bile acid)”, “(bile acid) receptors AND cancer”, “(bile acid) receptors AND prostate cancer”, “(bile acid) receptors AND gastric cancer”, “(bile acid) receptors AND hepatocellular carcinoma”, “(bile acid) receptors AND oesophageal cancer”, "(bile acid) AND ABC AND transporter", "(bile acid) AND SLC AND transporter", "(bile acid) AND SLCO AND transporter", "(bile acid) AND transport AND review", “Farnesoid X receptor (FXR) AND the cancer types assessed in the study”, “Pregnane X receptor (PXR) AND the cancer types assessed in the study”, “Constitutive androstane receptor (CAR) AND the cancer types assessed in the study”, “Vitamin D receptor (VDR) AND the cancer types assessed in the study” “Liver X receptor (LXR) AND the cancer types assessed in the study”, “Small heterodimer partner (SHP) AND the cancer types assessed in the study”. Articles published in English were included with no restriction on publication date. All references were checked at Pub Peer, two papers were flagged ( and), but when reviewing the reports we decided that the issues raised do not impact on the main message and kept the references.

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Pellicciari R, Gioiello A, Macchiarulo A, Thomas C, Rosatelli E, Natalini B, Sardella R, Pruzanski M, Roda A, Pastorini E, Schoonjans K, Auwerx J. Discovery of 6alpha-ethyl-23(S)-methylcholic acid (S-EMCA, INT-777) as a potent and selective agonist for the TGR5 receptor, a novel target for diabesity. J Med Chem. 2009;52:7958-7961.
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82.
Rizzo G, Passeri D, De Franco F, Ciaccioli G, Donadio L, Rizzo G, Orlandi S, Sadeghpour B, Wang XX, Jiang T, Levi M, Pruzanski M, Adorini L. Functional characterization of the semisynthetic bile acid derivative INT-767, a dual farnesoid X receptor and TGR5 agonist. Mol Pharmacol. 2010;78:617-630.
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83.
Genet C, Strehle A, Schmidt C, Boudjelal G, Lobstein A, Schoonjans K, Souchet M, Auwerx J, Saladin R, Wagner A. Structure-activity relationship study of betulinic acid, a novel and selective TGR5 agonist, and its synthetic derivatives: potential impact in diabetes. J Med Chem. 2010;53:178-190.
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84.
Zheng C, Zhou W, Wang T, You P, Zhao Y, Yang Y, Wang X, Luo J, Chen Y, Liu M, Chen H. A novel TGR5 activator WB403 promotes GLP-1 secretion and preserves pancreatic β- Cells in type 2 diabetic mice. PLoS ONE. 2015;10:1-16.
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85.
Pols TWH, Noriega LG, Nomura M, Auwerx J, Schoonjans K. The bile acid membrane receptor TGR5 as an emerging target in metabolism and inflammation. J Hepatol. 2011;54:1263-1272.
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Reich M, Deutschmann K, Sommerfeld A, Klindt C, Kluge S, Kubitz R, Ullmer C, Knoefel WT, Herebian D, Mayatepek E, Häussinger D, Keitel V. TGR5 is essential for bile acid-dependent cholangiocyte proliferation in vivo and in vitro. Gut. 2016;65:487-501.
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Masyuk AI, Huang BQ, Radtke BN, Gajdos GB, Splinter PL, Masyuk TV, Gradilone SA, LaRusso NF. Ciliary subcellular localization of TGR5 determines the cholangiocyte functional response to bile acid signaling. Am J Physiol Gastrointest Liver Physiol. 2013;304:2.
Not in our library10.1152/ajpgi.00383.2012
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Perino A, Pols TWH, Nomura M, Stein S, Pellicciari R, Schoonjans K. TGR5 reduces macrophage migration through mTOR-induced C/EBPβ differential translation. J Clin Investig. 2014;124:5424-5436.
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89.
Rajagopal S, Kumar DP, Mahavadi S, Bhattacharya S, Zhou R, Corvera CU, Bunnett NW, Grider JR, Murthy KS. Activation of G protein-coupled bile acid receptor, TGR5, induces smooth muscle relaxation via both Epac- and PKA-mediated inhibition of RhoA/Rho kinase pathway. Am J Physiol Gastrointest Liver Physiol. 2013;304:G527-535.
Not in our library10.1152/ajpgi.00388.2012
90.
Maruyama T, Tanaka K, Suzuki J, Miyoshi H, Harada N, Nakamura T, Miyamoto Y, Kanatani A, Tamai Y. Targeted disruption of G protein-coupled bile acid receptor 1 (Gpbar1/M-Bar) in mice. J Endocrinol. 2006;191:197-205.
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Guo C, Su J, Li Z, Xiao R, Wen J, Li Y, Zhang M, Zhang X, Yu D, Huang W, Chen WD, Wang YD. The G-protein-coupled bile acid receptor Gpbar1 (TGR5) suppresses gastric cancer cell proliferation and migration through antagonizing STAT3 signaling pathway. Oncotarget. 2015;6:34402-34413.
Not in our library10.18632/oncotarget.5353
92.
Wang YD, Chen WD, Yu D, Forman BM, Huang W. The G-Protein-coupled bile acid receptor, Gpbar1 (TGR5), negatively regulates hepatic inflammatory response through antagonizing nuclear factor kappa light-chain enhancer of activated B cells (NF-κB) in mice. Hepatology. 2011;54:1421-1432.
Not in our library10.1002/hep.24525
93.
TGR5, Not Only a Metabolic Regulator · 2016
No notice
94.
Pols TWH, Nomura M, Harach T, Lo Sasso G, Oosterveer MH, Thomas C, Rizzo G, Gioiello A, Adorini L, Pellicciari R, Auwerx J, Schoonjans K. TGR5 activation inhibits atherosclerosis by reducing macrophage inflammation and lipid loading. Cell Metab. 2011;14:747-757.
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95.
Liu R, Zhao R, Zhou X, Liang X, Campbell DJW, Zhang X, Zhang L, Shi R, Wang G, Pandak WM, Sirica AE, Hylemon PB, Zhou H. Conjugated bile acids promote cholangiocarcinoma cell invasive growth through activation of sphingosine 1-phosphate receptor 2. Hepatology. 2014;60:908-918.
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96.
Liu R, Li X, Qiang X, Luo L, Hylemon PB, Jiang Z, Zhang L, Zhou H. Taurocholate induces cyclooxygenase-2 expression via the sphingosine 1-phosphate receptor 2 in a human cholangiocarcinoma cell line. J Biol Chem. 2015;290:30988-31002.
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97.
Studer E, Zhou X, Zhao R, Wang Y, Takabe K, Nagahashi M, Pandak WM, Dent P, Spiegel S, Shi R, Xu W, Liu X, Bohdan P, Zhang L, Zhou H, Hylemon PB. Conjugated bile acids activate the sphingosine-1-phosphate receptor 2 in primary rodent hepatocytes. Hepatology. 2012;55:267-276.
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Nagahashi M, Takabe K, Liu R, Peng K, Wang X, Wang Y, Hait NC, Wang X, Allegood JC, Yamada A, Aoyagi T, Liang J, Pandak WM, Spiegel S, Hylemon PB, Zhou H. Conjugated bile acid-activated S1P receptor 2 is a key regulator of sphingosine kinase 2 and hepatic gene expression. Hepatology. 2015;61:1216-1226.
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Nagahashi M, Yuza K, Hirose Y, Nakajima M, Ramanathan R, Hait NC, Hylemon PB, Zhou H, Takabe K, Wakai T. The roles of bile acids and sphingosine-1-phosphate signaling in the hepatobiliary diseases. J Lipid Res. 2016;57:1636-1643.
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Yang J, Yang L, Tian L, Ji X, Yang L, Li L. Sphingosine 1-phosphate (S1P)/S1P receptor 2/3 axis promotes inflammatory M1 polarization of bone marrow-derived monocyte/macrophage via G(α) i/o /PI3K/JNK pathway. Cell Physiol Biochem. 2018;49:1677-1693.
Not in our library10.1159/000493611
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Karimian G, Buist-Homan M, Schmidt M, Tietge UJF, de Boer JF, Klappe K, Kok JW, Combettes L, Tordjmann T, Faber KN, Moshage H. Sphingosine kinase-1 inhibition protects primary rat hepatocytes against bile salt-induced apoptosis. Biochim Biophys Acta Mol Basis Dis. 1832;2013:1922-1929.
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Hughes JE, Srinivasan S, Lynch KR, Proia RL, Ferdek P, Hedrick CC. Sphingosine-1-phosphate induces an antiinflammatory phenotype in macrophages. Circ Res. 2008;102:950-958.
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104.
von Rosenvinge EC, Raufman JP. Muscarinic receptor signaling in colon cancer. Cancers. 2011;3:971-981.
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107.
Forman BM, Goode E, Chen J, Oro AE, Bradley DJ, Perlmann T, Noonan DJ, Burka LT, McMorris T, Lamph WW, Evans RM, Weinberger C. Identification of a nuclear receptor that is activated by farnesol metabolites. Cell. 1995;81:687-693.
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109.
Goodwin B, Jones SA, Price RR, Watson MA, McKee DD, Moore LB, Galardi C, Wilson JG, Lewis MC, Roth ME, Maloney PR, Willson TM, Kliewer SA. A regulatory cascade of the nuclear receptors FXR, SHP-1, and LRH-1 represses bile acid biosynthesis. Mol Cell. 2000;6:517-526.
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Zhang M, Chiang JYL. Transcriptional regulation of the human sterol 12α-hydroxylase gene (CYP8B1): roles of hepatocyte nuclear factor 4α in mediating bile acid repression. J Biol Chem. 2001;276:41690-41699.
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111.
Kong B, Wang L, Chiang JYL, Zhang Y, Klaassen CD, Guo GL. Mechanism of tissue-specific farnesoid X receptor in suppressing the expression of genes in bile-acid synthesis in mice. Hepatology. 2012;56:1034-1043.
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Denson LA, Sturm E, Echevarria W, Zimmerman TL, Makishima M, Mangelsdorf DJ, Karpen SJ. The orphan nuclear receptor, shp, mediates bile acid-induced inhibition of the rat bile acid transporter, ntcp. Gastroenterology. 2001;121:140-147.
Not in our library10.1053/gast.2001.25503
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Ananthanarayanan M, Balasubramanian N, Makishima M, Mangelsdorf DJ, Suchy FJ. Human bile salt export pump promoter is transactivated by the Farnesoid X receptor/bile acid receptor. J Biol Chem. 2001;276:28857-28865.
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Grobert J, Zaghini I, Fujii H, Jones SA, Kliewer SA, Willson TM, Ono T, Besnard P. Identification of a bile acid-responsive element in the human ileal bile acid-binding protein gene. Involvement of the farnesoid X receptor/9-cis- retinoic acid receptor heterodimer. J Biol Chem. 1999;274:29749-29754.
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Gnerre C, Blättler S, Kaufmann MR, Looser R, Meyer UA. Regulation of CYP3A4 by the bile acid receptor FXR: evidence for functional binding sites in the CYP3A4 gene. Pharmacogenetics. 2004;14:635-645.
Not in our library10.1097/00008571-200410000-00001
116.
Song CS, Echchgadda I, Baek BS, Ahn SC, Oh T, Roy AK, Chatterjee B. Dehydroepiandrosterone sulfotransferase gene induction by bile acid activated farnesoid X receptor. J Biol Chem. 2001;276:42549-42556.
Not in our library10.1074/jbc.m107557200
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Barbier O, Torra IP, Sirvent A, Claudel T, Blanquart C, Duran-Sandoval D, Kuipers F, Kosykh V, Fruchart JC, Staels B. FXR induces the UGT2B4 enzyme in hepatocytes: a potential mechanism of negative feedback control of FXR activity. Gastroenterology. 2003;124:1926-1940.
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118.
Wang YD, Chen WD, Wang M, Yu D, Forman BM, Huang W. Farnesoid X receptor antagonizes nuclear factor κB in hepatic inflammatory response. Hepatology. 2008;48:1632-1643.
Not in our library10.1002/hep.22519
119.
Lamba V, Yasuda K, Lamba JK, Assem M, Davila J, Strom S, Schuetz EG. PXR (NR1I2): splice variants in human tissues, including brain, and identification of neurosteroids and nicotine as PXR activators. Toxicol Appl Pharmacol. 2004;199:251-265.
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120.
Wang YM, Ong SS, Chai SC, Chen T. Role of CAR and PXR in xenobiotic sensing and metabolism. Expert Opin Drug Metab Toxicol. 2012;8:803-817.
Not in our library10.1517/17425255.2012.685237
121.
He J, Nishida S, Xu M, Makishima M, Xie W. PXR prevents cholesterol gallstone disease by regulating biosynthesis and transport of bile salts. Gastroenterology. 2011;140:2095-2106.
Not in our library10.1053/j.gastro.2011.02.055
122.
Staudinger JL, Goodwin B, Jones SA, Hawkins-Brown D, MacKenzie KI, LaTour A, Liu Y, Klaassen CD, Brown KK, Reinhard J, Willson TM, Koller BH, Kliewer SA. The nuclear receptor PXR is a lithocholic acid sensor that protects against liver toxicity. Proc Natl Acad Sci USA. 2001;98:3369-3374.
Not in our library10.1073/pnas.051551698
123.
Wistuba W, Gnewuch C, Liebisch G, Schmitz G, Langmann T. Lithocholic acid induction of the FGF19 promoter in intestinal cells is mediated by PXR. World J Gastroenterol. 2007;13:4230-4235.
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Xie W, Radominska-Pandya A, Shi Y, Simon CM, Nelson MC, Ong ES, Waxman DJ, Evans RM. An essential role for nuclear receptors SXR/PXR in detoxification of cholestatic bile acids. Proc Natl Acad Sci USA. 2001;98:3375-3380.
Not in our library10.1073/pnas.051014398
125.
Jonker JW, Liddle C, Downes M. FXR and PXR: potential therapeutic targets in cholestasis. J Steroid Biochem Mol Biol. 2012;130:147-158.
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Li T, Chiang JYL. Mechanism of rifampicin and pregnane X receptor inhibition of human cholesterol 7α-hydroxylase gene transcription. Am J Physiol Gastrointest Liver Physiol. 2005;288:74-84.
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127.
Wallace K, Cowie DE, Konstantinou DK, Hill SJ, Tjelle TE, Axon A, Koruth M, White SA, Carlsen H, Mann DA, Wright MC. The PXR is a drug target for chronic inflammatory liver disease. J Steroid Biochem Mol Biol. 2010;120:137-148.
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128.
Kakizaki S, Yamazaki Y, Takizawa D, Negishi M. New insights on the xenobiotic-sensing nuclear receptors in liver diseases–CAR and PXR. Curr Drug Metab. 2008;9:614-621.
Not in our library10.2174/138920008785821666
129.
Cheng J, Shah YM, Gonzalez FJ. Pregnane X receptor as a target for treatment of inflammatory bowel disorders. Trends Pharmacol Sci. 2012;33:323-330.
Not in our library10.1016/j.tips.2012.03.003
130.
Zhou J, Zhai Y, Mu Y, Gong H, Uppal H, Toma D, Ren S, Evans RM, Xie W. A novel pregnane X receptor-mediated and sterol regulatory element-binding protein-independent lipogenic pathway. J Biol Chem. 2006;281:15013-15020.
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131.
Nakamura K, Moore R, Negishi M, Sueyoshi T. Nuclear pregnane X receptor cross-talk with FoxA2 to mediate drug-induced regulation of lipid metabolism in fasting mouse liver. J Biol Chem. 2007;282:9768-9776.
Not in our library10.1074/jbc.m610072200
132.
Kodama S, Moore R, Yamamoto Y, Negishi M. Human nuclear pregnane X receptor cross-talk with CREB to repress cAMP activation of the glucose-6-phosphatase gene. Biochemical Journal. 2007;407:373-381.
Not in our library10.1042/bj20070481
133.
Bhalla S, Ozalp C, Fang S, Xiang L, Kemper JK. Ligand-activated pregnane X receptor interferes with HNF-4 signaling by targeting a common coactivator PGC-1α. Functional implications in hepatic cholesterol and glucose metabolism. J Biol Chem. 2004;279:45139-45147.
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134.
Choi HS, Chung M, Tzameli I, Simha D, Lee YK, Seol W, Moore DD. Differential transactivation by two isoforms of the orphan nuclear hormone receptor CAR. J Biol Chem. 1997;272:23565-23571.
Not in our library10.1074/jbc.272.38.23565
135.
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136.
Li H, Wang H. Activation of xenobiotic receptors: Driving into the nucleus. Expert Opin Drug Metab Toxicol. 2010;6:409-426.
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137.
Baes M, Gulick T, Choi HS, Martinoli MG, Simha D, Moore DD. A new orphan member of the nuclear hormone receptor superfamily that interacts with a subset of retinoic acid response elements. Mol Cell Biol. 1994;14:1544-1552.
Not in our library10.1128/mcb.14.3.1544-1552.1994
138.
di Masi A, De Marinis E, Ascenzi P, Marino M. Nuclear receptors CAR and PXR: molecular, functional, and biomedical aspects. Mol Aspects Med. 2009;30:297-343.
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139.
Wagner M, Halilbasic E, Marschall HU, Zollner G, Fickert P, Langner C, Zatloukal K, Denk H, Trauner M. CAR and PXR agonists stimulate hepatic bile acid and bilirubin detoxification and elimination pathways in mice. Hepatology. 2005;42:420-430.
Not in our library10.1002/hep.20784
140.
Han S, Chiang JY. Mechanism of vitamin D receptor inhibition of cholesterol 7alpha-hydroxylase gene transcription in human hepatocytes. Drug Metab Dispos. 2009;37:469-478.
Not in our library10.1124/dmd.108.025155
141.
Li Z, Kar Kruijt J, van der Sluis RJ, Van Berkel TJC, Hoekstra M. Nuclear receptor atlas of female mouse liver parenchymal, endothelial, and Kupffer cells. Physiol Genom. 2013;45:268-275.
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142.
Norman AW. Minireview: vitamin D receptor: new assignments for an already busy receptor. Endocrinology. 2006;147:5542-5548.
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143.
Makishima M, Lu TT, Xie W, Whitfield GK, Domoto H, Evans RM, Haussler MR, Mangelsdorf DJ. Vitamin D receptor as an intestinal bile acid sensor. Science. 2002;296:1313-1316.
Not in our library10.1126/science.1070477
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Nehring JA, Zierold C, DeLuca HF. Lithocholic acid can carry out in vivo functions of vitamin D. Proc Natl Acad Sci USA. 2007;104:10006-10009.
Not in our library10.1073/pnas.0703512104
145.
Intestinal CYP3A4 protects against lithocholic acid-induced hepatotoxicity in intestine-specific VDR-deficient mice[S] · 2014
Not checked
146.
Chatterjee B, Echchgadda I, Song CS. Vitamin D receptor regulation of the steroid/bile acid sulfotransferase SULT2A1. Methods Enzymol. 2005;400:165-191.
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147.
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148.
Chen X, Chen F, Liu S, Glaeser H, Dawson PA, Hofmann AF, Kim RB, Shneider BL, Pang KS. Transactivation of rat apical sodium-dependent bile acid transporter and increased bile acid transport by 1alpha,25-dihydroxyvitamin D3 via the vitamin D receptor. Mol Pharmacol. 2006;69:1913-1923.
Not in our library10.1124/mol.105.020792
149.
Huhtakangas JA, Olivera CJ, Bishop JE, Zanello LP, Norman AW. The vitamin D receptor is present in caveolae-enriched plasma membranes and binds 1α,25(OH)2-vitamin D3 in vivo and in vitro. Mol Endocrinol. 2004;18:2660-2671.
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150.
Han S, Li T, Ellis E, Strom S, Chiang JY. A novel bile acid-activated vitamin D receptor signaling in human hepatocytes. Mol Endocrinol. 2010;24:1151-1164.
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151.
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152.
Nagpal S, Na S, Rathnachalam R. Noncalcemic actions of vitamin D receptor ligands. Endocr Rev. 2005;26:662-687.
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153.
Janowski BA, Willy PJ, Devi TR, Falck JR, Mangelsdorf DJ. An oxysterol signalling pathway mediated by the nuclear receptor LXR alpha. Nature. 1996;383:728-731.
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Svensson S, Östberg T, Jacobsson M, Norström C, Stefansson K, Hallén D, Johansson IC, Zachrisson K, Ogg D, Jendeberg L. Crystal structure of the heterodimeric complex of LXRα and RXRβ ligand-binding domains in a fully agonistic conformation. EMBO J. 2003;22:4625-4633.
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155.
Control of cellular cholesterol efflux by the nuclear oxysterol receptor LXRα · 2000
Not checked
156.
Joseph SB, Bradley MN, Castrillo A, Bruhn KW, Mak PA, Pei L, Hogenesch J, O'Connell RM, Cheng G, Saez E, Miller JF, Tontonoz P. LXR-dependent gene expression is important for macrophage survival and the innate immune response. Cell. 2004;119:299-309.
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157.
De Marino S, Carino A, Masullo D, Finamore C, Marchianò S, Cipriani S, Di Leva FS, Catalanotti B, Novellino E, Limongelli V, Fiorucci S, Zampella A. Hyodeoxycholic acid derivatives as liver X receptor α and G-protein-coupled bile acid receptor agonists. Sci Rep. 2017;7:1-13.
Not in our library10.1038/srep43290
158.
Zhang Y, Hagedorn CH, Wang L. Role of nuclear receptor SHP in metabolism and cancer. Biochim Biophys Acta Mol Basis Dis. 1812;2011:893-908.
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161.
Kim KJ, Kim KH, Cho HK, Kim HY, Kim HH, Cheong JH. SHP (small heterodimer partner) suppresses the transcriptional activity and nuclear localization of Hedgehog signalling protein Gli1. Biochemical Journal. 2010;427:413-422.
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162.
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164.
Hong J, Behar J, Wands J, Resnick M, Wang LJ, DeLellis RA, Lambeth D, Souza RF, Spechler SJ, Cao W. Role of a novel bile acid receptor TGR5 in the development of oesophageal adenocarcinoma. Gut. 2010;59:170-180.
Not in our library10.1136/gut.2009.188375
165.
Liu R, Li X, Hylemon PB, Zhou H. Conjugated bile acids promote invasive growth of esophageal adenocarcinoma cells and cancer stem cell expansion via sphingosine 1-phosphate receptor 2-mediated yes-associated protein activation. Am J Pathol. 2018;188:2042-2058.
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166.
Zhou Z, Xia Y, Bandla S, Zakharov V, Wu S, Peters J, Godfrey TE, Sun J. Vitamin D receptor is highly expressed in precancerous lesions and esophageal adenocarcinoma with significant sex difference. Hum Pathol. 2014;45:1744-1751.
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167.
De Gottardi A, Dumonceau JM, Bruttin F, Vonlaufen A, Morard I, Spahr L, Rubbia-Brandt L, Frossard JL, Dinjens WN, Rabinovitch PS, Hadengue A. Expression of the bile acid receptor FXR in Barrett's esophagus and enhancement of apoptosis by guggulsterone in vitro. Mol Cancer. 2006;5:48.
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Guan B, Li H, Yang Z, Hoque A, Xu X. Inhibition of farnesoid X receptor controls esophageal cancer cell growth in vitro and in nude mouse xenografts. Cancer. 2013;119:1321-1329.
Not in our library10.1002/cncr.27910
169.
Pang C, LaLonde A, Godfrey TE, Que J, Sun J, Wu TT, Zhou Z. Bile salt receptor TGR5 is highly expressed in esophageal adenocarcinoma and precancerous lesions with significantly worse overall survival and gender differences. Clin Exp Gastroenterol. 2017;10:29-37.
Not in our library10.2147/ceg.s117842
170.
Capello A, Moons LM, Van de Winkel A, Siersema PD, van Dekken H, Kuipers EJ, Kusters JG. Bile acid-stimulated expression of the farnesoid X receptor enhances the immune response in Barrett esophagus. Am J Gastroenterol. 2008;103:1510-1516.
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171.
Bhat AA, Lu H, Soutto M, Capobianco A, Rai P, Zaika A, El-Rifai W. Exposure of Barrett's and esophageal adenocarcinoma cells to bile acids activates EGFR-STAT3 signaling axis via induction of APE1. Oncogene. 2018;37:6011-6024.
Not in our library10.1038/s41388-018-0388-8
172.
Zhang Q, Agoston AT, Pham TH, Zhang W, Zhang X, Huo X, Peng S, Bajpai M, Das K, Odze RD, Spechler SJ, Souza RF. Acidic bile salts induce epithelial to mesenchymal transition via VEGF signaling in non-neoplastic Barrett's cells. Gastroenterology. 2019;156:130-144.e110.
Not in our library10.1053/j.gastro.2018.09.046
173.
Activation of EGFR-DNA-PKcs pathway by IGFBP2 protects esophageal adenocarcinoma cells from acidic bile salts-induced DNA damage · 2019
Not checked
174.
Correa P, Piazuelo MB. The gastric precancerous cascade. J Dig Dis. 2012;13:2-9.
Not in our library10.1111/j.1751-2980.2011.00550.x
175.
Matsuhisa T, Arakawa T, Watanabe T, Tokutomi T, Sakurai K, Okamura S, Chono S, Kamada T, Sugiyama A, Fujimura Y, Matsuzawa K, Ito M, Yasuda M, Ota H, Haruma K. Relation between bile acid reflux into the stomach and the risk of atrophic gastritis and intestinal metaplasia: a multicenter study of 2283 cases. Dig Endosc. 2013;25:519-525.
Not in our library10.1111/den.12030
176.
Yu JH, Zheng JB, Qi J, Yang K, Wu YH, Wang K, Wang CB, Sun XJ. Bile acids promote gastric intestinal metaplasia by upregulating CDX2 and MUC2 expression via the FXR/NF-κB signalling pathway. Int J Oncol. 2019;54:879-892.
Not in our library10.3892/ijo.2019.4692
177.
Xu Y, Watanabe T, Tanigawa T, Machida H, Okazaki H, Yamagami H, Watanabe K, Tominaga K, Fujiwara Y, Oshitani N, Arakawa T. Bile acids induce cdx2 expression through the farnesoid x receptor in gastric epithelial cells. J Clin Biochem Nutr. 2010;46:81-86.
Not in our library10.3164/jcbn.09-71
178.
Park MJ, Kim KH, Kim HY, Kim K, Cheong J. Bile acid induces expression of COX-2 through the homeodomain transcription factor CDX1 and orphan nuclear receptor SHP in human gastric cancer cells. Carcinogenesis. 2008;29:2385-2393.
Not in our library10.1093/carcin/bgn207
179.
Acidified bile acids enhance tumor progression and telomerase activity of gastric cancer in mice dependent on c‐Myc expression · 2017
Not checked
180.
Wang X, Zhou P, Sun X, Zheng J, Wei G, Zhang L, Wang H, Yao J, Lu S, Jia P. Acidified bile acids increase hTERT expression via c-myc activation in human gastric cancer cells. Oncol Rep. 2015;33:3038-3044.
Not in our library10.3892/or.2015.3908
181.
Ni Z, Min Y, Han C, Yuan T, Lu W, Ashktorab H, Smoot DT, Wu Q, Wu J, Zeng W, Shi Y. TGR5-HNF4alpha axis contributes to bile acid-induced gastric intestinal metaplasia markers expression. Cell Death Discovery. 2020;6:56.
Not in our library10.1038/s41420-020-0290-3
182.
Yasuda H, Hirata S, Inoue K, Mashima H, Ohnishi H, Yoshiba M. Involvement of membrane-type bile acid receptor M-BAR/TGR5 in bile acid-induced activation of epidermal growth factor receptor and mitogen-activated protein kinases in gastric carcinoma cells. Biochem Biophys Res Commun. 2007;354:154-159.
Not in our library10.1016/j.bbrc.2006.12.168
183.
Carino A, Graziosi L, D'Amore C, Cipriani S, Marchiano S, Marino E, Zampella A, Rende M, Mosci P, Distrutti E, Donini A, Fiorucci S. The bile acid receptor GPBAR1 (TGR5) is expressed in human gastric cancers and promotes epithelial-mesenchymal transition in gastric cancer cell lines. Oncotarget. 2016;7:61021-61035.
Not in our library10.18632/oncotarget.10477
184.
Cao W, Tian W, Hong J, Li D, Tavares R, Noble L, Moss SF, Resnick MB. Expression of bile acid receptor TGR5 in gastric adenocarcinoma. Am J Physiol Gastrointest Liver Physiol. 2013;304:322-327.
Not in our library10.1152/ajpgi.00263.2012
185.
Yang HB, Song W, Cheng MD, Fan HF, Gu X, Qiao Y, Lu X, Yu RH, Chen LY. Deoxycholic acid inhibits the growth of BGC-823 gastric carcinoma cells via a p53-mediated pathway. Mol Med Rep. 2015;11:2749-2754.
Not in our library10.3892/mmr.2014.3004
186.
Song W, Yang HB, Chen P, Wang SM, Zhao LP, Xu WH, Fan HF, Gu X, Chen LY. Apoptosis of human gastric carcinoma SGC-7901 induced by deoxycholic acid via the mitochondrial-dependent pathway. Appl Biochem Biotechnol. 2013;171:1061-1071.
Not in our library10.1007/s12010-013-0417-6
187.
Guo C, Qi H, Yu Y, Zhang Q, Su J, Yu D, Huang W, Chen WD, Wang YD. The G-protein-coupled bile acid receptor Gpbar1 (TGR5) inhibits gastric inflammation through antagonizing NF-κB signaling pathway. Front Pharmacol. 2015;6:287.
Not in our library10.3389/fphar.2015.00287
188.
Fukase K, Ohtsuka H, Onogawa T, Oshio H, Ii T, Mutoh M, Katayose Y, Rikiyama T, Oikawa M, Motoi F, Egawa S, Abe T, Unno M. Bile acids repress E-cadherin through the induction of Snail and increase cancer invasiveness in human hepatobiliary carcinoma. Cancer Sci. 2008;99:1785-1792.
Not in our library10.1111/j.1349-7006.2008.00898.x
189.
Kainuma M, Takada I, Makishima M, Sano K. Farnesoid X receptor activation enhances transforming growth factor β-induced epithelial-mesenchymal transition in hepatocellular carcinoma cells. Int J Mol Sci. 2018;19:1-9.
Not in our library10.3390/ijms19071898
190.
Hu Y, Chau T, Liu HX, Liao D, Keane R, Nie Y, Yang H, Wan YJY. Bile acids regulate nuclear receptor (Nur77) expression and intracellular location to control proliferation and apoptosis. Mol Cancer Res. 2015;13:281-292.
Not in our library10.1158/1541-7786.mcr-14-0230
191.
Jang ES, Yoon JH, Lee SH, Lee SM, Lee JH, Yu SJ, Kim YJ, Lee HS, Kim CY. Sodium taurocholate cotransporting polypeptide mediates dual actions of deoxycholic acid in human hepatocellular carcinoma cells: Enhanced apoptosis versus growth stimulation. J Cancer Res Clin Oncol. 2014;140:133-144.
Not in our library10.1007/s00432-013-1554-6
192.
Nguyen PT, Kanno K, Pham QT, Kikuchi Y, Kakimoto M, Kobayashi T, Otani Y, Kishikawa N, Miyauchi M, Arihiro K, Ito M, Tazuma S. Senescent hepatic stellate cells caused by deoxycholic acid modulates malignant behavior of hepatocellular carcinoma. J Cancer Res Clin Oncol. 2020;146:3255-3268.
Not in our library10.1007/s00432-020-03374-9
193.
Xu Z, Huang G, Gong W, Zhou P, Zhao Y, Zhang Y, Zeng Y, Gao M, Pan Z, He F. FXR ligands protect against hepatocellular inflammation via SOCS3 induction. Cell Signal. 2012;24:1658-1664.
Not in our library10.1016/j.cellsig.2012.04.015
194.
Langhi C, Pedraz-Cuesta E, Donate Y, Marrero PF, Haro D, Rodríguez JC. Regulation of N-Myc downstream regulated gene 2 by bile acids. Biochem Biophys Res Commun. 2013;434:102-109.
Not in our library10.1016/j.bbrc.2013.03.058
195.
Lee S, Cho YY, Cho EJ, Yu SJ, Lee JH, Yoon JH, Kim YJ. Synergistic effect of ursodeoxycholic acid on the antitumor activity of sorafenib in hepatocellular carcinoma cells via modulation of STAT3 and ERK, Internaltion. J Mol Med. 2018;42:2551-2559.
Not in our library10.3892/ijmm.2018.3807
196.
Liu H, Qin CY, Han GQ, Xu HW, Meng M, Yang Z. Mechanism of apoptotic effects induced selectively by ursodeoxycholic acid on human hepatoma cell lines. World J Gastroenterol. 2007;13:1652-1658.
Not in our library10.3748/wjg.v13.i11.1652
197.
Zhu L, Shan LJ, Liu YJ, Chen D, Xiao XG, Li Y. Ursodeoxycholic acid induces apoptosis of hepatocellular carcinoma cells in vitro. J Dig Dis. 2014;15:684-693.
Not in our library10.1111/1751-2980.12191
198.
Chung GE, Yoon JH, Lee JH, Kim HY, Myung SJ, Yu SJ, Lee SH, Lee SM, Kim YJ, Lee HS. Ursodeoxycholic acid-induced inhibition of DLC1 protein degradation leads to suppression of hepatocellular carcinoma cell growth. Oncol Rep. 2011;25:1739-1746.
Not in our library10.3892/or.2011.1239
199.
Lim SC, Choi JE, Kang HS, Si H. Ursodeoxycholic acid switches oxaliplatin-induced necrosis to apoptosis by inhibiting reactive oxygen species production and activating p53-caspase 8 pathway in HepG2 hepatocellular carcinoma. Int J Cancer. 2010;126:1582-1595.
Not in our library10.1002/ijc.24853
200.
Yang CS, Yuk JM, Kim JJ, Hwang JH, Lee CH, Kim JM, Oh GT, Choi HS, Jo EK. Small heterodimer partner-targeting therapy inhibits systemic inflammatory responses through mitochondrial uncoupling protein 2. PLoS ONE. 2013;8:e63435.
Not in our library10.1371/journal.pone.0063435
201.
Zollner G, Wagner M, Fickert P, Silbert D, Fuchsbichler A, Zatloukal K, Denk H, Trauner M. Hepatobiliary transporter expression in human hepatocellular carcinoma. Liver Int. 2005;25:367-379.
Not in our library10.1111/j.1478-3231.2005.01033.x
202.
Bile acid transporters and regulatory nuclear receptors in the liver and beyond · 2013
No notice
203.
Bile acids and nonalcoholic fatty liver disease · 2017
No notice
204.
Zhang W, Zhou L, Yin P, Wang J, Lu X, Wang X, Chen J, Lin X, Xu G. A weighted relative difference accumulation algorithm for dynamic metabolomics data: long-term elevated bile acids are risk factors for hepatocellular carcinoma. Sci Rep. 2015;5:8984.
Not in our library10.1038/srep08984
205.
Knisely AS, Strautnieks SS, Meier Y, Stieger B, Byrne JA, Portmann BC, Bull LN, Pawlikowska L, Bilezikçi B, Ozçay F, László A, Tiszlavicz L, Moore L, Raftos J, Arnell H, Fischler B, Németh A, Papadogiannakis N, Cielecka-Kuszyk J, Jankowska I, Pawłowska J, Melín-Aldana H, Emerick KM, Whitington PF, Mieli-Vergani G, Thompson RJ. Hepatocellular carcinoma in ten children under five years of age with bile salt export pump deficiency. Hepatology. 2006;44:478-486.
Not in our library10.1002/hep.21287
206.
Yang F, Huang X, Yi T, Yen Y, Moore DD, Huang W. Spontaneous development of liver tumors in the absence of the bile acid receptor farnesoid X receptor. Can Res. 2007;67:863-867.
Not in our library10.1158/0008-5472.can-06-1078
207.
Degirolamo C, Modica S, Vacca M, Di Tullio G, Morgano A, D'Orazio A, Kannisto K, Parini P, Moschetta A. Prevention of spontaneous hepatocarcinogenesis in farnesoid X receptor-null mice by intestinal-specific farnesoid X receptor reactivation. Hepatology. 2015;61:161-170.
Not in our library10.1002/hep.27274
208.
Wolfe A, Thomas A, Edwards G, Jaseja R, Guo GL, Apte U. Increased activation of the Wnt/β-catenin pathway in spontaneous hepatocellular carcinoma observed in farnesoid X receptor knockout mice. J Pharmacol Exp Ther. 2011;338:12-21.
Not in our library10.1124/jpet.111.179390
209.
Nomoto M, Miyata M, Yin S, Kurata Y, Shimada M, Yoshinari K, Gonzalez FJ, Suzuki K, Shibasaki S, Kurosawa T, Yamazoe Y. Bile acid-induced elevated oxidative stress in the absence of farnesoid X receptor. Biol Pharm Bull. 2009;32:172-178.
Not in our library10.1248/bpb.32.172
210.
Smolková K, Mikó E, Kovács T, Leguina-Ruzzi A, Sipos A, Bai P. NRF2 in regulating cancer metabolism. Antioxid Redox Signal. 2020;33:966-997.
Not in our library10.1089/ars.2020.8024
211.
Kong B, Zhu Y, Li G, Williams JA, Buckley K, Tawfik O, Luyendyk JP, Guo GL. Mice with hepatocyte-specific FXR deficiency are resistant to spontaneous but susceptible to cholic acid-induced hepatocarcinogenesis. Am J Physiol Gastrointestinal and Liver Physiology. 2016;310:G295-302.
Not in our library10.1152/ajpgi.00134.2015
212.
Jia W, Xie G, Jia W. Bile acid-microbiota crosstalk in gastrointestinal inflammation and carcinogenesis. Nat Rev Gastroenterol Hepatol. 2018;15:111-128.
Not in our library10.1038/nrgastro.2017.119
213.
Bernstein H, Bernstein C, Payne CM, Dvorakova K, Garewal H. Bile acids as carcinogens in human gastrointestinal cancers. Mutat Res. 2005;589:47-65.
Not in our library10.1016/j.mrrev.2004.08.001
214.
Gadaleta RM, Oldenburg B, Willemsen EC, Spit M, Murzilli S, Salvatore L, Klomp LW, Siersema PD, van Erpecum KJ, van Mil SW. Activation of bile salt nuclear receptor FXR is repressed by pro-inflammatory cytokines activating NF-κB signaling in the intestine. Biochem Biophys Acta. 1812;2011:851-858.
Not in our library10.1016/j.bbadis.2011.04.005
215.
Zhang Y, Xu P, Park K, Choi Y, Moore DD, Wang L. Orphan receptor small heterodimer partner suppresses tumorigenesis by modulating cyclin D1 expression and cellular proliferation. Hepatology. 2008;48:289-298.
Not in our library10.1002/hep.22342
216.
Zhang Y, Soto J, Park K, Viswanath G, Kuwada S, Abel ED, Wang L. Nuclear receptor SHP, a death receptor that targets mitochondria, induces apoptosis and inhibits tumor growth. Mol Cell Biol. 2010;30:1341-1356.
Not in our library10.1128/mcb.01076-09
217.
He N, Park K, Zhang Y, Huang J, Lu S, Wang L. Epigenetic inhibition of nuclear receptor small heterodimer partner is associated with and regulates hepatocellular carcinoma growth. Gastroenterology. 2008;134:793-802.
Not in our library10.1053/j.gastro.2008.01.006
218.
Small heterodimer partner interacts with NLRP3 and negatively regulates activation of the NLRP3 inflammasome · 2015
No notice
219.
Gandhi D, Ojili V, Nepal P, Nagar A, Hernandez-Delima FJ, Bajaj D, Choudhary G, Gupta N, Sharma P. A pictorial review of gall stones and its associated complications. Clin Imaging. 2020;60:228-236.
Not in our library10.1016/j.clinimag.2019.11.015
220.
Feng HY, Chen YC. Role of bile acids in carcinogenesis of pancreatic cancer: An old topic with new perspective. World J Gastroenterol. 2016;22:7463-7477.
Not in our library10.3748/wjg.v22.i33.7463
221.
Fu H, Li Y, Bai G, Yin R, Yin C, Shi W, Zhang L, Li R, Zhao R. Persistent cholestasis resulting from duodenal papillary carcinoma in an adolescent male: A case report. Medicine. 2019;98:e15708.
Not in our library10.1097/md.0000000000015708
222.
Thomas RM, Jobin C. Microbiota in pancreatic health and disease: the next frontier in microbiome research, Nature Reviews. Gastroenterol Hepatol. 2020;17:53-64.
Not in our library10.1038/s41575-019-0242-7
223.
Rees DO, Crick PJ, Jenkins GJ, Wang Y, Griffiths WJ, Brown TH, Al-Sarireh B. Comparison of the composition of bile acids in bile of patients with adenocarcinoma of the pancreas and benign disease. J Steroid Biochem Mol Biol. 2017;174:290-295.
Not in our library10.1016/j.jsbmb.2017.10.011
224.
Adachi T, Tajima Y, Kuroki T, Mishima T, Kitasato A, Fukuda K, Tsutsumi R, Kanematsu T. Bile-reflux into the pancreatic ducts is associated with the development of intraductal papillary carcinoma in hamsters. J Surg Res. 2006;136:106-111.
Not in our library10.1016/j.jss.2006.04.025
225.
Tucker ON, Dannenberg AJ, Yang EY, Fahey Iii TJ. Bile acids induce cyclooxygenase-2 expression in human pancreatic cancer cell lines. Carcinogenesis. 2004;25:419-423.
Not in our library10.1093/carcin/bgh010
226.
Nagathihalli NS, Beesetty Y, Lee W, Washington MK, Chen X, Lockhart AC, Merchant NB. Novel mechanistic insights into ectodomain shedding of EGFR Ligands Amphiregulin and TGF-α: impact on gastrointestinal cancers driven by secondary bile acids. Can Res. 2014;74:2062-2072.
Not in our library10.1158/0008-5472.can-13-2329
227.
Kim YJ, Jeong SH, Kim EK, Kim EJ, Cho JH. Ursodeoxycholic acid suppresses epithelial-mesenchymal transition and cancer stem cell formation by reducing the levels of peroxiredoxin II and reactive oxygen species in pancreatic cancer cells. Oncol Rep. 2017;38:3632-3638.
Not in our library10.3892/or.2017.6045
228.
Reddy BS, Wynder EL. Metabolic epidemiology of colon cancer Fecal bile acids and neutral sterols in colon cancer patients and patients with adenomatous polyps. Cancer. 1977;39:2533-2539.
Not in our library10.1002/1097-0142(197706)39:6<2533::aid-cncr2820390634>3.0.co;2-x
229.
Murakami Y, Tanabe S, Suzuki T. High-fat diet-induced intestinal hyperpermeability is associated with increased bile acids in the large intestine of mice. J Food Sci. 2016;81:H216-222.
Not in our library10.1111/1750-3841.13166
230.
Lagergren J, Ye W, Ekbom A. Intestinal cancer after cholecystectomy: is bile involved in carcinogenesis? Gastroenterology. 2001;121:542-547.
Not in our library10.1053/gast.2001.27083
231.
Payne CM, Bernstein C, Dvorak K, Bernstein H. Hydrophobic bile acids, genomic instability, Darwinian selection, and colon carcinogenesis. Clin Exp Gastroenterol. 2008;1:19-47.
Not in our library10.2147/ceg.s4343
232.
Degirolamo C, Modica S, Palasciano G, Moschetta A. Bile acids and colon cancer: solving the puzzle with nuclear receptors. Trends Mol Med. 2011;17:564-572.
Not in our library10.1016/j.molmed.2011.05.010
233.
Turner DJ, Alaish SM, Zou T, Rao JN, Wang JY, Strauch ED. Bile salts induce resistance to apoptosis through NF-kappaB-mediated XIAP expression. Ann Surg. 2007;245:415-425.
Not in our library10.1097/01.sla.0000236631.72698.99
234.
Ridlon JM, Wolf PG, Gaskins HR. Taurocholic acid metabolism by gut microbes and colon cancer. Gut Microbes. 2016;7:201-215.
Not in our library10.1080/19490976.2016.1150414
235.
Huang XP, Fan XT, Desjeux JF, Castagna M. Bile acids, non-phorbol-ester-type tumor promoters, stimulate the phosphorylation of protein kinase C substrates in human platelets and colon cell line HT29. Int J Cancer. 1992;52:444-450.
Not in our library10.1002/ijc.2910520319
236.
Moschetta A, Portincasa P, van Erpecum KJ, Debellis L, Vanberge-Henegouwen GP, Palasciano G. Sphingomyelin protects against apoptosis and hyperproliferation induced by deoxycholate: potential implications for colon cancer. Dig Dis Sci. 2003;48:1094-1101.
Not in our library10.1023/a:1023712712025
237.
Zimber A, Gespach C. Bile acids and derivatives, their nuclear receptors FXR, PXR and ligands: role in health and disease and their therapeutic potential. Anticancer Agents Med Chem. 2008;8:540-563.
Not in our library10.2174/187152008784533008
238.
Bile acid: a potential inducer of colon cancer stem cells · 2016
No notice
239.
Hori T, Matsumoto K, Sakaitani Y, Sato M, Morotomi M. Effect of dietary deoxycholic acid and cholesterol on fecal steroid concentration and its impact on the colonic crypt cell proliferation in azoxymethane-treated rats. Cancer Lett. 1998;124:79-84.
Not in our library10.1016/s0304-3835(97)00452-7
240.
Di Ciaula A, Garruti G, Lunardi Baccetto R, Molina-Molina E, Bonfrate L, Wang DQ, Portincasa P. Bile acid physiology. Ann Hepatol. 2017;16:s4-s14.
Not in our library10.5604/5601.3001.0010.5493
241.
Bile Acids and Cancer: Direct and Environmental-Dependent Effects · 2017
Not checked
242.
Zeng H, Claycombe KJ, Reindl KM. Butyrate and deoxycholic acid play common and distinct roles in HCT116 human colon cell proliferation. J Nutr Biochem. 2015;26:1022-1028.
Not in our library10.1016/j.jnutbio.2015.04.007
243.
Hess LM, Krutzsch MF, Guillen J, Chow HH, Einspahr J, Batta AK, Salen G, Reid ME, Earnest DL, Alberts DS. Results of a phase I multiple-dose clinical study of ursodeoxycholic acid. Cancer Epidemiol Biomark Prev. 2004;13:861-867.
Not in our library10.1158/1055-9965.861.13.5
244.
Kim EK, Cho JH, Kim EJ, Kim YJ. Ursodeoxycholic acid inhibits the proliferation of colon cancer cells by regulating oxidative stress and cancer stem-like cell growth. PLoS ONE. 2017;12:1-11.
Not in our library10.1371/journal.pone.0181183
245.
Ochsenkuhn T, Marsteller I, Hay U, Diebold J, Paumgartner G, Goke B, Sackmann M. Does ursodeoxycholic acid change the proliferation of the colorectal mucosa? A randomized, placebo-controlled study. Digestion. 2003;68:209-216.
Not in our library10.1159/000075927
246.
Im E, Martinez JD. Diet induced changes in the colonic environment and colorectal cancer ursodeoxycholic acid (UDCA) can inhibit deoxycholic acid (DCA)-induced apoptosis via modulation of EGFR/ Raf-1/ERK signaling in human colon cancer cells. J Nutr. 2004;2:483-486.
Not in our library10.1093/jn/134.2.483
247.
Rigas B, Tsioulias GJ, Allan C, Wali RK, Brasitus TA. The effect of bile acids and piroxicam on MHC antigen expression in rat colonocytes during colon cancer development. Immunology. 1994;83:319-323.
Not in our library
248.
Alberts DS, Martinez ME, Hess LM, Einspahr JG, Green SB, Bhattacharyya AK, Guillen J, Krutzsch M, Batta AK, Salen G, Fales L, Koonce K, Parish D, Clouser M, Roe D, Lance P. Gastroenterologist, Phase III trial of ursodeoxycholic acid to prevent colorectal adenoma recurrence. J Natl Cancer Inst. 2005;97:846-853.
Not in our library10.1093/jnci/dji144
249.
Tung BY, Emond MJ, Haggitt RC, Bronner MP, Kimmey MB, Kowdley KV, Brentnall TA. Ursodiol use is associated with lower prevalence of colonic neoplasia in patients with ulcerative colitis and primary sclerosing cholangitis. Ann Intern Med. 2001;134:89-95.
Not in our library10.7326/0003-4819-134-2-200101160-00008
250.
Serfaty L, De Leusse A, Rosmorduc O, Desaint B, Flejou JF, Chazouilleres O, Poupon RE, Poupon R. Ursodeoxycholic acid therapy and the risk of colorectal adenoma in patients with primary biliary cirrhosis: an observational study. Hepatology. 2003;38:203-209.
Not in our library10.1053/jhep.2003.50311
251.
Garrett WS. Cancer and the microbiota. Science. 2015;348:80-86.
Not in our library10.1126/science.aaa4972
252.
Tjalsma H, Boleij A, Marchesi JR, Dutilh BE. A bacterial driver-passenger model for colorectal cancer: beyond the usual suspects. Nat Rev Microbiol. 2012;10:575-582.
Not in our library10.1038/nrmicro2819
253.
Raskov H, Burcharth J, Pommergaard HC. Linking gut microbiota to colorectal cancer. J Cancer. 2017;8:3378-3395.
Not in our library10.7150/jca.20497
254.
Ward JBJ, Lajczak NK, Kelly OB, O'Dwyer AM, Giddam AK, Ni Gabhann J, Franco P, Tambuwala MM, Jefferies CA, Keely S, Roda A, Keely SJ. Ursodeoxycholic acid and lithocholic acid exert anti-inflammatory actions in the colon. Am J Physiol Gastrointest Liver Physiol. 2017;312:G550-G558.
Not in our library10.1152/ajpgi.00256.2016
255.
Islam KB, Fukiya S, Hagio M, Fujii N, Ishizuka S, Ooka T, Ogura Y, Hayashi T, Yokota A. Bile acid is a host factor that regulates the composition of the cecal microbiota in rats. Gastroenterology. 2011;141:1773-1781.
Not in our library10.1053/j.gastro.2011.07.046
256.
Devkota S, Wang Y, Musch MW, Leone V, Fehlner-Peach H, Nadimpalli A, Antonopoulos DA, Jabri B, Chang EB. Dietary-fat-induced taurocholic acid promotes pathobiont expansion and colitis in Il10-/- mice. Nature. 2012;487:104-108.
Not in our library10.1038/nature11225
257.
Javitt NB, Budai K, Miller DG, Cahan AC, Raju U, Levitz M. Breast-gut connection: origin of chenodeoxycholic acid in breast cyst fluid. Lancet. 1994;343:633-635.
Not in our library10.1016/s0140-6736(94)92635-2
258.
Tang W, Putluri V, Ambati CR, Dorsey TH, Putluri N, Ambs S. Liver- and microbiome-derived bile acids accumulate in human breast tumors and inhibit growth and improve patient survival. Clin Cancer Res. 2019;11:1078-1432.
Not in our library10.1158/1078-0432.ccr-19-0094
259.
Murray WR, Blackwood A, Calman KC, MacKay C. Faecal bile acids and clostridia in patients with breast cancer. Br J Cancer. 1980;42:856-860.
Not in our library10.1038/bjc.1980.333
260.
Luo C, Zhang X, He Y, Chen H, Liu M, Wang H, Tang L, Tu G, Ding M. A pseudo-targeted metabolomics study based on serum bile acids profiling for the differential diagnosis of benign and malignant breast lesions. Steroids. 2021;175:108914.
Not in our library10.1016/j.steroids.2021.108914
261.
Raju U, Levitz M, Javitt NB. Bile acids in human breast cyst fluid: the identification of lithocholic acid. J Clin Endocrinol Metab. 1990;70:1030-1034.
Not in our library10.1210/jcem-70-4-1030
262.
Costarelli V, Sanders TA. Plasma bile acids and risk of breast cancer. IARC Sci Publ. 2002;156:305-306.
Not in our library
263.
Costarelli V, Sanders TA. Plasma deoxycholic acid concentration is elevated in postmenopausal women with newly diagnosed breast cancer. Eur J Clin Nutr. 2002;56:925-927.
Not in our library10.1038/sj.ejcn.1601396
264.
A joint analysis of metabolomics and genetics of breast cancer · 2014
No notice
265.
Swales KE, Korbonits M, Carpenter R, Walsh DT, Warner TD, Bishop-Bailey D. The farnesoid X receptor is expressed in breast cancer and regulates apoptosis and aromatase expression. Can Res. 2006;66:10120-10126.
Not in our library10.1158/0008-5472.can-06-2399
266.
Kovács T, Mikó E, Ujlaki G, Yousef H, Csontos V, Uray K, Bai P. The involvement of oncobiosis and bacterial metabolite signaling in metastasis formation in breast cancer. Cancer Metastasis Rev. 2022;40:1223-1249.
Not in our library10.1007/s10555-021-10013-3
267.
Baker PR, Wilton JC, Jones CE, Stenzel DJ, Watson N, Smith GJ. Bile acids influence the growth, oestrogen receptor and oestrogen-regulated proteins of MCF-7 human breast cancer cells. Br J Cancer. 1992;65:566-572.
Not in our library10.1038/bjc.1992.115
268.
Giordano C, Catalano S, Panza S, Vizza D, Barone I, Bonofiglio D, Gelsomino L, Rizza P, Fuqua SAW, Andò S. Farnesoid X receptor inhibits tamoxifen-resistant MCF-7 breast cancer cell growth through downregulation of HER2 expression. Oncogene. 2011;30:4129-4140.
Not in our library10.1038/onc.2011.124
269.
Journe F, Durbecq V, Chaboteaux C, Rouas G, Laurent G, Nonclercq D, Sotiriou C, Body JJ, Larsimont D. Association between farnesoid X receptor expression and cell proliferation in estrogen receptor-positive luminal-like breast cancer from postmenopausal patients. Breast Cancer Res Treat. 2009;115:523-535.
Not in our library10.1007/s10549-008-0094-2
270.
Liu N, Zhao J, Wang J, Teng H, Fu Y, Yuan H. Farnesoid X receptor ligand CDCA suppresses human prostate cancer cells growth by inhibiting lipid metabolism via targeting sterol response element binding protein, American Journal of. Transl Res. 2016;8:5118-5124.
Not in our library
271.
Liu J, Tong SJ, Wang X, Qu LX. Farnesoid X receptor inhibits LNcaP cell proliferation via the upregulation of PTEN. Exp Ther Med. 2014;8:1209-1212.
Not in our library10.3892/etm.2014.1894
272.
Kaeding J, Bouchaert E, Bélanger J, Caron P, Chouinard S, Verreault M, Larouche O, Pelletier G, Staels B, Bélanger A, Barbier O. Activators of the farnesoid X receptor negatively regulate androgen glucuronidation in human prostate cancer LNCAP cells. Biochem J. 2008;410:245-253.
Not in our library10.1042/bj20071136
273.
Goldberg AA, Titorenko VI, Beach A, Sanderson JT. Bile acids induce apoptosis selectively in androgen-dependent and -independent prostate cancer cells. PeerJ. 2013;1:e122.
Not in our library10.7717/peerj.122
274.
Lee WS, Jung JH, Panchanathan R, Yun JW, Kim DH, Kim HJ, Kim GS, Ryu CH, Shin SC, Hong SC, Choi YH, Jung J-M. Ursodeoxycholic acid induces death receptor-mediated apoptosis in prostate cancer cells. j Cancer Prev. 2017;22:16-21.
Not in our library10.15430/jcp.2017.22.1.16
275.
Ke C, Hou Y, Zhang H, Fan L, Ge T, Guo B, Zhang F, Yang K, Wang J, Lou G, Li K. Large-scale profiling of metabolic dysregulation in ovarian cancer. Int J Cancer. 2015;136:516-526.
Not in our library10.1002/ijc.29010
276.
Fan L, Yin M, Ke C, Ge T, Zhang G, Zhang W, Zhou X, Lou G, Li K. Use of plasma metabolomics to identify diagnostic biomarkers for early stage epithelial ovarian cancer. J Cancer. 2016;7:1265-1272.
Not in our library10.7150/jca.15074
277.
Zhou M, Guan W, Walker LD, Mezencev R, Benigno BB, Gray A, Fernández FM, McDonald JF. Rapid mass spectrometric metabolic profiling of blood sera detects ovarian cancer with high accuracy. Cancer Epidemiol Biomark Prev. 2010;19:2262-2271.
Not in our library10.1158/1055-9965.epi-10-0126
278.
Guan W, Zhou M, Hampton CY, Benigno BB, Walker LD, Gray A, McDonald JF, Fernández FM. Ovarian cancer detection from metabolomic liquid chromatography/mass spectrometry data by support vector machines. BMC Bioinformatics. 2009;10:259.
Not in our library10.1186/1471-2105-10-259
279.
Horowitz NS, Hua J, Powell MA, Gibb RK, Mutch DG, Herzog TJ. Novel cytotoxic agents from an unexpected source: bile acids and ovarian tumor apoptosis. Gynecol Oncol. 2007;107:344-349.
Not in our library10.1016/j.ygyno.2007.07.072
280.
Schuldes H, Dolderer JH, Zimmer G, Knobloch J, Bickeböller R, Jonas D, Woodcock BG. Reversal of multidrug resistance and increase in plasma membrane fluidity in CHO cells with R-verapamil and bile salts. Eur J Cancer. 2001;37:660-667.
Not in our library10.1016/s0959-8049(00)00450-0
281.
Jin Q, Noel O, Nguyen M, Sam L, Gerhard GS. Bile acids upregulate BRCA1 and downregulate estrogen receptor 1 gene expression in ovarian cancer cells. Eur J Cancer Prev. 2018;27:553-556.
Not in our library10.1097/cej.0000000000000398
282.
Pascual MJ, Macias RI, Garcia-Del-Pozo J, Serrano MA, Marin JJ. Enhanced efficiency of the placental barrier to cisplatin through binding to glycocholic acid. Anticancer Res. 2001;21:2703-2707.
Not in our library
283.
Rough JJ, Monroy MA, Yerrum S, Daly JM. Anti-proliferative effect of LXR agonist T0901317 in ovarian carcinoma cells. J Ovar Res. 2010;3:13.
Not in our library10.1186/1757-2215-3-13
284.
Scoles DR, Xu X, Wang H, Tran H, Taylor-Harding B, Li A, Karlan BY. Liver X receptor agonist inhibits proliferation of ovarian carcinoma cells stimulated by oxidized low density lipoprotein. Gynecol Oncol. 2010;116:109-116.
Not in our library10.1016/j.ygyno.2009.09.034
285.
Curtarello M, Tognon M, Venturoli C, Silic-Benussi M, Grassi A, Verza M, Minuzzo S, Pinazza M, Brillo V, Tosi G, Ferrazza R, Guella G, Iorio E, Godfroid A, Sounni NE, Amadori A, Indraccolo S. Rewiring of lipid metabolism and storage in ovarian cancer cells after anti-VEGF therapy. Cells. 2019;8:E1601.
Not in our library10.3390/cells8121601
286.
Masuyama H, Nakamura K, Nobumoto E, Hiramatsu Y. Inhibition of pregnane X receptor pathway contributes to the cell growth inhibition and apoptosis of anticancer agents in ovarian cancer cells. Int J Oncol. 2016;49:1211-1220.
Not in our library10.3892/ijo.2016.3611
287.
Bandera Merchan B, Morcillo S, Martin-Nuñez G, Tinahones FJ, Macías-González M. The role of vitamin D and VDR in carcinogenesis: Through epidemiology and basic sciences. J Steroid Biochem Mol Biol. 2017;167:203-218.
Not in our library10.1016/j.jsbmb.2016.11.020
288.
Hou YF, Gao SH, Wang P, Zhang HM, Liu LZ, Ye MX, Zhou GM, Zhang ZL, Li BY. 1α,25(OH)2D3 suppresses the migration of ovarian cancer SKOV-3 cells through the inhibition of epithelial–mesenchymal transition. Int J Mol Sci. 2016;17:E1285.
Not in our library10.3390/ijms17081285
289.
Ji M, Liu L, Hou Y, Li B. 1α,25-Dihydroxyvitamin D3 restrains stem cell-like properties of ovarian cancer cells by enhancing vitamin D receptor and suppressing CD44. Oncol Rep. 2019;41:3393-3403.
Not in our library10.3892/or.2019.7116
290.
Li J, Li B, Jiang Q, Zhang Y, Liu A, Wang H, Zhang J, Qin Q, Hong Z, Li BA. Do genetic polymorphisms of the vitamin D receptor contribute to breast/ovarian cancer? A systematic review and network meta-analysis. Gene. 2018;677:211-227.
Not in our library10.1016/j.gene.2018.07.070
291.
Lungchukiet P, Sun Y, Kasiappan R, Quarni W, Nicosia SV, Zhang X, Bai W. Suppression of epithelial ovarian cancer invasion into the omentum by 1α,25-dihydroxyvitamin D3 and its receptor. J Steroid Biochem Mol Biol. 2015;148:138-147.
Not in our library10.1016/j.jsbmb.2014.11.005
292.
Silvagno F, Poma CB, Realmuto C, Ravarino N, Ramella A, Santoro N, D'Amelio P, Fuso L, Pescarmona G, Zola P. Analysis of vitamin D receptor expression and clinical correlations in patients with ovarian cancer. Gynecol Oncol. 2010;119:121-124.
Not in our library10.1016/j.ygyno.2010.06.008
293.
Tamez S, Norizoe C, Ochiai K, Takahashi D, Shimojima A, Tsutsumi Y, Yanaihara N, Tanaka T, Okamoto A, Urashima M. Vitamin D receptor polymorphisms and prognosis of patients with epithelial ovarian cancer. Br J Cancer. 2009;101:1957-1960.
Not in our library10.1038/sj.bjc.6605414
294.
Cordes T, Hoellen F, Dittmer C, Salehin D, Kümmel S, Friedrich M, Köster F, Becker S, Diedrich K, Thill M. Correlation of prostaglandin metabolizing enzymes and serum PGE2 levels with vitamin D receptor and serum 25(OH)2D3 levels in breast and ovarian cancer. Anticancer Res. 2012;32:351-357.
Not in our library
295.
Efficacy of a non-hypercalcemic vitamin-D2 derived anti-cancer agent (MT19c) and inhibition of fatty acid synthesis in an ovarian cancer xenograft model. · 2012
Not checked
296.
Czogalla B, Deuster E, Liao Y, Mayr D, Schmoeckel E, Sattler C, Kolben T, Hester A, Furst S, Burges A, Mahner S, Jeschke U, Trillsch F. Cytoplasmic VDR expression as an independent risk factor for ovarian cancer. Histochem Cell Biol. 2020;154:421-429.
Not in our library10.1007/s00418-020-01894-6
297.
Chen Y, Tang Y, Guo C, Wang J, Boral D, Nie D. Nuclear receptors in the multidrug resistance through the regulation of drug-metabolizing enzymes and drug transporters. Biochem Pharmacol. 2012;83:1112-1126.
Not in our library10.1016/j.bcp.2012.01.030
298.
Wang Y, Masuyama H, Nobumoto E, Zhang G, Hiramatsu Y. The inhibition of constitutive androstane receptor-mediated pathway enhances the effects of anticancer agents in ovarian cancer cells. Biochem Pharmacol. 2014;90:356-366.
Not in our library10.1016/j.bcp.2014.06.003
299.
Gupta D, Venkatesh M, Wang H, Kim S, Sinz M, Goldberg GL, Whitney K, Longley C, Mani S. Expanding the roles for pregnane X receptor in cancer: proliferation and drug resistance in ovarian cancer. Clin Cancer Res. 2008;14:5332-5340.
Not in our library10.1158/1078-0432.ccr-08-1033
300.
Szanto M, Gupte R, Kraus WL, Pacher P, Bai P. PARPs in lipid metabolism and related diseases. Progr Lipid Res. 2021;84:101117.
Not in our library10.1016/j.plipres.2021.101117
301.
Phelan JP, Reen FJ, Caparros-Martin JA, O'Connor R, O'Gara F. Rethinking the bile acid/gut microbiome axis in cancer. Oncotarget. 2017;8:115736-115747.
Not in our library10.18632/oncotarget.22803
302.
Amaral JD, Viana RJS, Ramalho RM, Steer CJ, Rodrigues CMP. Bile acids: Regulation of apoptosis by ursodeoxycholic acid. J Lipid Res. 2009;50:1721-1734.
Not in our library10.1194/jlr.r900011-jlr200
303.
Trottier J, Białek A, Caron P, Straka RJ, Milkiewicz P, Barbier O. Profiling circulating and urinary bile acids in patients with biliary obstruction before and after biliary stenting. PLoS ONE. 2011;6:e22094.
Not in our library10.1371/journal.pone.0022094
304.
García-Cañaveras JC, Donato MT, Castell JV, Lahoz A. Targeted profiling of circulating and hepatic bile acids in human, mouse, and rat using a UPLC-MRM-MS-validated method. J Lipid Res. 2012;53:2231-2241.
Not in our library10.1194/jlr.d028803
305.
Ma Z, Wang X, Yin P, Wu R, Zhou L, Xu G, Niu J. Serum metabolome and targeted bile acid profiling reveals potential novel biomarkers for drug-induced liver injury. Medicine (Baltimore). 2019;98:e16717.
Not in our library10.1097/md.0000000000016717
306.
Sun Z, Huang C, Shi Y, Wang R, Fan J, Yu Y, Zhang Z, Zhu K, Li M, Ni Q, Chen Z, Zheng M, Yang Z. Distinct bile acid profiles in patients with chronic hepatitis b virus infection reveal metabolic interplay between host, virus and gut microbiome. Front Med. 2021;8:708495.
Not in our library10.3389/fmed.2021.708495
307.
James SC, Fraser K, Young W, Heenan PE, Gearry RB, Keenan JI, Talley NJ, Joyce SA, McNabb WC, Roy NC. Concentrations of fecal bile acids in participants with functional gut disorders and healthy controls. Metabolites. 2021;11:2.
Not in our library10.3390/metabo11090612
308.
Wei W, Wang HF, Zhang Y, Zhang YL, Niu BY, Yao SK. Altered metabolism of bile acids correlates with clinical parameters and the gut microbiota in patients with diarrhea-predominant irritable bowel syndrome. World J Gastroenterol. 2020;26:7153-7172.
Not in our library10.3748/wjg.v26.i45.7153
309.
Sergeev I, Keren N, Naftali T, Konikoff FM. Cholecystectomy and biliary sphincterotomy increase fecal bile loss and improve lipid profile in dyslipidemia. Dig Dis Sci. 2020;65:1223-1230.
Not in our library10.1007/s10620-019-05823-z
310.
Zhao A, Wang S, Chen W, Zheng X, Huang F, Han X, Ge K, Rajani C, Huang Y, Yu H, Zhu J, Jia W. Increased levels of conjugated bile acids are associated with human bile reflux gastritis. Sci Rep. 2020;10:11601.
Not in our library10.1038/s41598-020-68393-5
311.
Jäntti SE, Kivilompolo M, Ohrnberg L, Pietiläinen KH, Nygren H, Orešič M, Hyötyläinen T. Quantitative profiling of bile acids in blood, adipose tissue, intestine, and gall bladder samples using ultra high performance liquid chromatography-tandem mass spectrometry. Anal Bioanal Chem. 2014;406:7799-7815.
Not in our library10.1007/s00216-014-8230-9
312.
Setchell KD, Rodrigues CM, Clerici C, Solinas A, Morelli A, Gartung C, Boyer J. Bile acid concentrations in human and rat liver tissue and in hepatocyte nuclei. Gastroenterology. 1997;112:226-235.
Not in our library10.1016/s0016-5085(97)70239-7
313.
Honda A, Yoshida T, Tanaka N, Matsuzaki Y, He B, Shoda J, Osuga T. Increased bile acid concentration in liver tissue with cholesterol gallstone disease. J Gastroenterol Hepatol. 1995;30:61-66.
Not in our library10.1007/bf01211376
314.
Yao Z, Zhang X, Zhao F, Wang S, Chen A, Huang B, Wang J, Li X. Ursodeoxycholic acid inhibits glioblastoma progression via endoplasmic reticulum stress related apoptosis and synergizes with the proteasome inhibitor bortezomib. ACS Chem Neurosci. 2020;11:1337-1346.
Not in our library10.1021/acschemneuro.0c00095
315.
Fonseca I, Gordino G, Moreira S, Nunes MJ, Azevedo C, Gama MJ, Rodrigues E, Rodrigues CMP, Castro-Caldas M. Tauroursodeoxycholic acid protects against mitochondrial dysfunction and cell death via mitophagy in human neuroblastoma cells. Mol Neurobiol. 2017;54:6107-6119.
Not in our library10.1007/s12035-016-0145-3
316.
Yu H, Fu QR, Huang ZJ, Lin JY, Chen QX, Wang Q, Shen DY. Apoptosis induced by ursodeoxycholic acid in human melanoma cells through the mitochondrial pathway. Oncol Rep. 2019;41:213-223.
Not in our library10.3892/or.2018.6828
317.
Liu H, Xu HW, Zhang YZ, Huang Y, Han GQ, Liang TJ, Wei LL, Qin CY, Qin CK. Ursodeoxycholic acid induces apoptosis in hepatocellular carcinoma xenografts in mice. World J Gastroenterol. 2015;21:10367-10374.
Not in our library10.3748/wjg.v21.i36.10367
318.
Pang L, Zhao X, Liu W, Deng J, Tan X, Qiu L. Anticancer effect of ursodeoxycholic acid in human oral squamous carcinoma HSC-3 cells through the caspases. Nutrients. 2015;7:3200-3218.
Not in our library10.3390/nu7053200
319.
Fimognari C, Lenzi M, Cantelli-Forti G, Hrelia P. Apoptosis and modulation of cell cycle control by bile acids in human leukemia T cells. Ann N Y Acad Sci. 2009;1171:264-269.
Not in our library10.1111/j.1749-6632.2009.04710.x
320.
The role of bile acids in cellular invasiveness of gastric cancer · 2018
Not checked
321.
Lim SC, Duong HQ, Choi JE, Lee TB, Kang JH, Oh SH, Han SI. Lipid raft-dependent death receptor 5 (DR5) expression and activation are critical for ursodeoxycholic acid-induced apoptosis in gastric cancer cells. Carcinogenesis. 2011;32:723-731.
Not in our library10.1093/carcin/bgr038
322.
Lim SC, Duong HQ, Parajuli KR, Han SI. Pro-apoptotic role of the MEK/ERK pathway in ursodeoxycholic acid-induced apoptosis in SNU601 gastric cancer cells. Oncol Rep. 2012;28:1429-1434.
Not in our library10.3892/or.2012.1918
323.
Lim SC, Han SI. Ursodeoxycholic acid effectively kills drug-resistant gastric cancer cells through induction of autophagic death. Oncol Rep. 2015;34:1261-1268.
Not in our library10.3892/or.2015.4076
324.
Peng S, Huo X, Rezaei D, Zhang Q, Zhang X, Yu C, Asanuma K, Cheng E, Pham TH, Wang DH, Chen M, Souza RF, Spechler SJ. In Barrett's esophagus patients and Barrett's cell lines, ursodeoxycholic acid increases antioxidant expression and prevents DNA damage by bile acids. Am J Physiol Gastrointest Liver Physiol. 2014;307:129-139.
Not in our library10.1152/ajpgi.00085.2014
325.
Abdel-Latif MM, Inoue H, Reynolds JV. Opposing effects of bile acids deoxycholic acid and ursodeoxycholic acid on signal transduction pathways in oesophageal cancer cells. Eur J Cancer Prev. 2016;25:368-379.
Not in our library10.1097/cej.0000000000000198
326.
Goldman A, Condon A, Adler E, Minnella M, Bernstein C, Bernstein H, Dvorak K. Protective effects of glycoursodeoxycholic acid in Barrett's esophagus cells. Dis Esophagus. 2010;23:83-93.
Not in our library10.1111/j.1442-2050.2009.00993.x
327.
Im E, Akare S, Powell A, Martinez JD. Ursodeoxycholic acid can suppress deoxycholic acid-induced apoptosis by stimulating Akt/PKB-dependent survival signaling. Nutr Cancer. 2005;51:110-116.
Not in our library10.1207/s15327914nc5101_15
328.
Saeki T, Yui S, Hirai T, Fujii T, Okada S, Kanamoto R. Ursodeoxycholic acid protects colon cancer HCT116 cells from deoxycholic acid-induced apoptosis by inhibiting apoptosome formation. Nutr Cancer. 2012;64:617-626.
Not in our library10.1080/01635581.2012.669876
329.
Peiró-Jordán R, Krishna-Subramanian S, Hanski ML, Lüscher-Firzlaff J, Zeitz M, Hanski C. The chemopreventive agent ursodeoxycholic acid inhibits proliferation of colon carcinoma cells by suppressing c-Myc expression. Eur J Cancer Prev. 2012;21:413-422.
Not in our library10.1097/cej.0b013e32834ef16f
330.
Shah SA, Volkov Y, Arfin Q, Abdel-Latif MM, Kelleher D. Ursodeoxycholic acid inhibits interleukin beta 1 and deoxycholic acid-induced activation of NF-κB and AP-1 in human colon cancer cells. Int J Cancer. 2006;118:532-539.
Not in our library10.1002/ijc.21365
331.
Feldman R, Martinez JD. Growth suppression by ursodeoxycholic acid involves caveolin-1 enhanced degradation of EGFR. Biochem Biophys Acta. 2009;1793:1387-1394.
Not in our library10.1016/j.bbamcr.2009.05.003
332.
Kim YH, Kim JH, Kim BG, Lee KL, Kim JW, Koh S-J. Tauroursodeoxycholic acid attenuates colitis-associated colon cancer by inhibiting nuclear factor kappaB signaling. J Gastroenterol Hepatol. 2019;34:544-551.
Not in our library10.1111/jgh.14526
333.
Alpini G, Kanno N, Phinizy JL, Glaser S, Francis H, Taffetani S, LeSage G. Tauroursodeoxycholate inhibits human cholangiocarcinoma growth via Ca 2+-, PKC-, and MAPK-dependent pathways. Am J Physiol Gastrointest Liver Physiol. 2004;286:973-982.
Not in our library10.1152/ajpgi.00270.2003
334.
Alasmael N, Mohan R, Meira LB, Swales KE, Plant NJ. Activation of the Farnesoid X-receptor in breast cancer cell lines results in cytotoxicity but not increased migration potential. Cancer Lett. 2016;370:250-259.
Not in our library10.1016/j.canlet.2015.10.031
335.
Sun J, Mustafi R, Cerda S, Chumsangsri A, Xia YR, Li YC, Bissonnette M. Lithocholic acid down-regulation of NF-kappaB activity through vitamin D receptor in colonic cancer cells. J Steroid Biochem Mol Biol. 2008;111:37-40.
Not in our library10.1016/j.jsbmb.2008.01.003
336.
Vogel SM, Bauer MR, Joerger AC, Wilcken R, Brandt T, Veprintsev DB, Rutherford TJ, Fersht AR, Boeckler FM. Lithocholic acid is an endogenous inhibitor of MDM4 and MDM2. Proc Natl Acad Sci USA. 2012;109:16906-16910.
Not in our library10.1073/pnas.1215060109
337.
Powell AA, LaRue JM, Batta AK, Martinez JD. Bile acid hydrophobicity is correlated with induction of apoptosis and/or growth arrest in HCT116 cells. Biochem J. 2001;356:481-486.
Not in our library10.1042/bj3560481
338.
Qiao D, Im E, Qi W, Martinez JD. Activator protein-1 and CCAAT/enhancer-binding protein mediated GADD153 expression is involved in deoxycholic acid-induced apoptosis. Biochem Biophys Acta. 2002;1583:108-116.
Not in our library10.1016/s1388-1981(02)00190-7
339.
Lin R, Zhan M, Yang L, Wang H, Shen H, Huang S, Huang X, Xu S, Zhang Z, Li W, Liu Q, Shi Y, Chen W, Yu J, Wang J. Deoxycholic acid modulates the progression of gallbladder cancer through N(6)-methyladenosine-dependent microRNA maturation. Oncogene. 2020;39:4983-5000.
Not in our library10.1038/s41388-020-1349-6
340.
Pyo JS, Ko YS, Kang G, Kim DH, Kim WH, Lee BL, Sohn JH. Bile acid induces MUC2 expression and inhibits tumor invasion in gastric carcinomas. J Cancer Res Clin Oncol. 2015;141:1181-1188.
Not in our library10.1007/s00432-014-1890-1
341.
Krishnamurthy K, Wang G, Rokhfeld D, Bieberich E. Deoxycholate promotes survival of breast cancer cells by reducing the level of pro-apoptotic ceramide. Breast Cancer Res. 2008;10:1-16.
Not in our library10.1186/bcr2211
342.
Yoon JH, Higuchi H, Werneburg NW, Kaufmann SH, Gores GJ. Bile acids induce cyclooxygenase-2 expression via the epidermal growth factor receptor in a human cholangiocarcinoma cell line. Gastroenterology. 2002;122:985-993.
Not in our library10.1053/gast.2002.32410
343.
Baek MK, Park JS, Park JH, Kim MH, Kim HD, Bae WK, Chung IJ, Shin BA, Jung YD. Lithocholic acid upregulates uPAR and cell invasiveness via MAPK and AP-1 signaling in colon cancer cells. Cancer Lett. 2010;290:123-128.
Not in our library10.1016/j.canlet.2009.08.030
344.
Debruyne PR, Bruyneel EA, Karaguni IM, Li X, Flatau G, Muller O, Zimber A, Gespach C, Mareel MM. Bile acids stimulate invasion and haptotaxis in human colorectal cancer cells through activation of multiple oncogenic signaling pathways. Oncogene. 2002;21:6740-6750.
Not in our library10.1038/sj.onc.1205729
345.
Halvorsen B, Staff AC, Ligaarden S, Prydz K, Kolset SO. Lithocholic acid and sulphated lithocholic acid differ in the ability to promote matrix metalloproteinase secretion in the human colon cancer cell line CaCo-2. Biochem J. 2000;349:189-193.
Not in our library10.1042/bj3490189
346.
Nguyen TT, Lian S, Ung TT, Xia Y, Han JY, Jung YD. Lithocholic acid stimulates IL-8 expression in human colorectal cancer cells via activation of Erk1/2 MAPK and suppression of STAT3 activity. J Cell Biochem. 2017;118:2958-2967.
Not in our library10.1002/jcb.25955
347.
Nguyen TT, Ung TT, Li S, Lian S, Xia Y, Park SY, Do Jung Y. Metformin inhibits lithocholic acid-induced interleukin 8 upregulation in colorectal cancer cells by suppressing ROS production and NF-kB activity. Sci Rep. 2019;9:1-13.
Not in our library10.1038/s41598-019-38778-2
348.
Cheng K, Raufman J-P. Bile acid-induced proliferation of a human colon cancer cell line is mediated by transactivation of epidermal growth factor receptors. Biochem Pharmacol. 2005;70:1035-1047.
Not in our library10.1016/j.bcp.2005.07.023
349.
Payne CM, Weber C, Crowley-Skillicorn C, Dvorak K, Bernstein H, Bernstein C, Holubec H, Dvorakova B, Garewal H. Deoxycholate induces mitochondrial oxidative stress and activates NF-κB through multiple mechanisms in HCT-116 colon epithelial cells. Carcinogenesis. 2007;28:215-222.
Not in our library10.1093/carcin/bgl139
350.
Centuori SM, Gomes CJ, Trujillo J, Borg J, Brownlee J, Putnam CW, Martinez JD. Deoxycholic acid mediates non-canonical EGFR-MAPK activation through the induction of calcium signaling in colon cancer cells. Biochem Biophys Acta. 1861;2016:663-670.
Not in our library10.1016/j.bbalip.2016.04.006
351.
Zhu Y, Zhu M, Lance P. Stromal COX-2 signaling activated by deoxycholic acid mediates proliferation and invasiveness of colorectal epithelial cancer cells. Biochem Biophys Res Commun. 2012;425:607-612.
Not in our library10.1016/j.bbrc.2012.07.137
352.
Pai R, Tarnawski AS, Tran T. Deoxycholic acid activates beta-catenin signaling pathway and increases colon cell cancer growth and invasiveness. Mol Biol Cell. 2004;15:2156-2163.
Not in our library10.1091/mbc.e03-12-0894
353.
Li Z, Tanaka M, Kataoka H, Nakamura R, Sanjar R, Shinmura K, Sugimura H. EphA2 Up-regulation induced by deoxycholic acid in human colon carcinoma cells, an involvement of extracellular signal-regulated kinase and p53-independence. J Cancer Res Clin Oncol. 2003;129:703-708.
Not in our library10.1007/s00432-003-0493-z
354.
Milovic V, Teller IC, Murphy GM, Caspary WF, Stein J. Deoxycholic acid stimulates migration in colon cancer cells. Eur J Gastroenterol Hepatol. 2001;13:945-949.
Not in our library10.1097/00042737-200108000-00012
355.
Milovic V, Teller IC, Faust D, Caspary WF, Stein J. Effects of deoxycholate on human colon cancer cells: apoptosis or proliferation. Eur J Clin Invest. 2002;32:29-34.
Not in our library10.1046/j.0014-2972.2001.00938.x
356.
Qiao D, Stratagouleas ED, Martinez JD. Activation and role of mitogen-activated protein kinases in deoxycholic acid-induced apoptosis. Carcinogenesis. 2001;22:35-41.
Not in our library10.1093/carcin/22.1.35
357.
Qiao D, Gaitonde SV, Qi W, Martinez JD. Deoxycholic acid suppresses p53 by stimulating proteasome-mediated p53 protein degradation. Carcinogenesis. 2001;22:957-964.
Not in our library10.1093/carcin/22.6.957
358.
Lee HY, Crawley S, Hokari R, Kwon S, Kim YS. Bile acid regulates MUC2 transcription in colon cancer cells via positive EGFR/PKC/Ras/ERK/CREB, PI3K/Akt/IkappaB/NF-kappaB and p38/MSK1/CREB pathways and negative JNK/c-Jun/AP-1 pathway. Int J Oncol. 2010;36:941-953.
Not in our library10.3892/ijo_00000573
359.
Lechner S, Müller-Ladner U, Schlottmann K, Jung B, McClelland M, Rüschoff J, Welsh J, Schölmerich J, Kullmann F. Bile acids mimic oxidative stress induced upregulation of thioredoxin reductase in colon cancer cell lines. Carcinogenesis. 2002;23:1281-1288.
Not in our library10.1093/carcin/23.8.1281
360.
Lee DK, Park SY, Baik SK, Kwon SO, Chung JM, Oh E-S, Kim HS. Deoxycholic acid-induced signal transduction in HT-29 cells: role of NF-kappa B and interleukin-8. Korean J Gastroenterol. 2004;43:176-185.
Not in our library
361.
Fu T, Coulter S, Yoshihara E, Oh TG, Fang S, Cayabyab F, Zhu Q, Zhang T, Leblanc M, Liu S, He M, Waizenegger W, Gasser E, Schnabl B, Atkins AR, Yu RT, Knight R, Liddle C, Downes M, Evans RM. FXR regulates intestinal cancer stem cell proliferation. Cell. 2019;176:1098-1112.e1018.
Not in our library10.1016/j.cell.2019.01.036
362.
Casaburi I, Avena P, Lanzino M, Sisci D, Giordano F, Maris P, Catalano S, Morelli C, Andò S. Chenodeoxycholic acid through a TGR5-dependent CREB signaling activation enhances cyclin D1 expression and promotes human endometrial cancer cell proliferation. Cell Cycle. 2012;11:2699-2710.
Not in our library10.4161/cc.21029
363.
Gao L, Lv G, Li R, Liu WT, Zong C, Ye F, Li XY, Yang X, Jiang JH, Hou XJ, Jing YY, Han ZP, Wei LX. Glycochenodeoxycholate promotes hepatocellular carcinoma invasion and migration by AMPK/mTOR dependent autophagy activation. Cancer Lett. 2019;454:215-223.
Not in our library10.1016/j.canlet.2019.04.009
364.
Role of bile salt in regulating Mcl-1 phosphorylation and chemoresistance in hepatocellular carcinoma cells · 2011
Not checked
365.
Zhou M, Qi Z, Zhao J, Liao M, Wen S, Manyi Y. Phosphorylation of Bcl-2 plays an important role in glycochenodeoxycholate-induced survival and chemoresistance in HCC. Oncol Rep. 2017;38:1742-1750.
Not in our library10.3892/or.2017.5830
366.
Xie G, Wang X, Huang F, Zhao A, Chen W, Yan J, Zhang Y, Lei S, Ge K, Zheng X, Liu J, Su M, Liu P, Jia W. Dysregulated hepatic bile acids collaboratively promote liver carcinogenesis. Int J Cancer. 2016;139:1764-1775.
Not in our library10.1002/ijc.30219
367.
Shellman Z, Aldhahrani A, Verdon B, Mather M, Paleri V, Wilson J, Pearson J, Ward C, Powell J. Bile acids: a potential role in the pathogenesis of pharyngeal malignancy. Clin Otolaryngol. 2016;30:12822.
Not in our library10.1111/coa.12822
368.
Liu X, Chen B, You W, Xue S, Qin H, Jiang H. The membrane bile acid receptor TGR5 drives cell growth and migration via activation of the JAK2/STAT3 signaling pathway in non-small cell lung cancer. Cancer Lett. 2018;412:194-207.
Not in our library10.1016/j.canlet.2017.10.017
369.
Sharma R, Quilty F, Gilmer JF, Long A, Byrne AM. Unconjugated secondary bile acids activate the unfolded protein response and induce golgi fragmentation via a src-kinasedependant mechanism. Oncotarget. 2017;8:967-978.
Not in our library10.18632/oncotarget.13514
370.
Yen CJ, Izzo JG, Lee DF, Guha S, Wei Y, Wu TT, Chen CT, Kuo HP, Hsu JM, Sun HL, Chou CK, Buttar NS, Wang KK, Huang P, Ajani J, Hung MC. Bile acid exposure up-regulates tuberous sclerosis complex 1/mammalian target of rapamycin pathway in Barrett's-associated esophageal adenocarcinoma. Can Res. 2008;68:2632-2640.
Not in our library10.1158/0008-5472.can-07-5460
371.
Soma T, Kaganoi J, Kawabe A, Kondo K, Tsunoda S, Imamura M, Shimada Y. Chenodeoxycholic acid stimulates the progression of human esophageal cancer cells: a possible mechanism of angiogenesis in patients with esophageal cancer. Int J Cancer. 2006;119:771-782.
Not in our library10.1002/ijc.21917
372.
Prichard DO, Byrne AM, Murphy JO, Reynolds JV, O'Sullivan J, Feighery R, Doyle B, Eldin OS, Finn SP, Maguire A, Duff D, Kelleher DP, Long A. Deoxycholic acid promotes development of gastroesophageal reflux disease and Barrett's oesophagus by modulating integrin-αv trafficking. J Cell Mol Med. 2017;21:3612-3625.
Not in our library10.1111/jcmm.13271
373.
Morrow DJ, Avissar NE, Toia L, Redmond EM, Watson TJ, Jones C, Raymond DP, Litle V, Peters JH. Pathogenesis of Barrett's esophagus: bile acids inhibit the Notch signaling pathway with induction of CDX2 gene expression in human esophageal cells. Surgery. 2009;146:712-714.
Not in our library10.1016/j.surg.2009.06.050
374.
Burnat G, Majka J, Konturek PC. Bile acids are multifunctional modulators of the Barrett's carcinogenesis. J Physiol Pharmacol. 2010;61:185-192.
Not in our library
375.
Zhang R, Yin X, Shi H, Wu J, Shakya P, Liu D, Zhang J. Adiponectin modulates DCA-induced inflammation via the ROS/NF-kappa B signaling pathway in esophageal adenocarcinoma cells. Dig Dis Sci. 2014;59:89-97.
Not in our library10.1007/s10620-013-2877-5
376.
Roesly HB, Khan MR, Chen HDR, Hill KA, Narendran N, Watts GS, Chen X, Dvorak K. The decreased expression of Beclin-1 correlates with progression to esophageal adenocarcinoma: The role of deoxycholic acid. Am J Physiol Gastrointest Liver Physiol. 2012;302:864-872.
Not in our library10.1152/ajpgi.00340.2011
377.
Huo X, Juergens S, Zhang X, Rezaei D, Yu C, Strauch ED, Wang JY, Cheng E, Meyer F, Wang DH, Zhang Q, Spechler SJ, Souza RF. Deoxycholic acid causes DNA damage while inducing apoptotic resistance through NF-κ{green}b activation in benign barrett's epithelial cells. Am J Physiol Gastrointest Liver Physiol. 2011;301:278-286.
Not in our library10.1152/ajpgi.00092.2011
378.
Jenkins GJS, D'Souza FR, Suzen SH, Eltahir ZS, James SA, Parry JM, Griffiths PA, Baxter JN. Deoxycholic acid at neutral and acid pH, is genotoxic to oesophageal cells through the induction of ROS: The potential role of anti-oxidants in Barrett's oesophagus. Carcinogenesis. 2007;28:136-142.
Not in our library10.1093/carcin/bgl147
379.
Jenkins GJS, Cronin J, Alhamdani A, Rawat N, D'Souza F, Thomas T, Eltahir Z, Griffiths AP, Baxter JN. The bile acid deoxycholic acid has a non-linear dose response for DNA damage and possibly NF-κB activation in oesophageal cells, with a mechanism of action involving ROS. Mutagenesis. 2008;23:399-405.
Not in our library10.1093/mutage/gen029
380.
Song S, Guha S, Liu K, Buttar NS, Bresalier RS. COX-2 induction by unconjugated bile acids involves reactive oxygen species-mediated signalling pathways in Barrett's oesophagus and oesophageal adenocarcinoma. Gut. 2007;56:1512-1521.
Not in our library10.1136/gut.2007.121244
381.
Hu Y, Jones C, Gellersen O, Williams VA, Watson TJ, Peters JH. Pathogenesis of Barrett esophagus: deoxycholic acid up-regulates goblet-specific gene MUC2 in concert with CDX2 in human esophageal cells. Arch Surg. 1960;142(2007):540-545.
Not in our library10.1001/archsurg.142.6.540
382.
Wu JT, Gong J, Geng J, Song YX. Deoxycholic acid induces the overexpression of intestinal mucin, MUC2, via NF-kB signaling pathway in human esophageal adenocarcinoma cells. BMC Cancer. 2008;8:1-10.
Not in our library10.1186/1471-2407-8-333
383.
Looby E, Abdel-Latif MMM, Athié-Morales V, Duggan S, Long A, Kelleher D. Deoxycholate induces COX-2 expression via Erk1/2-, p38-MAPK and AP-1-dependent mechanisms in esophageal cancer cells. BMC Cancer. 2009;9:1-15.
Not in our library10.1186/1471-2407-9-190
384.
Chen M, Ye A, Wei J, Wang R, Poon K. Deoxycholic acid upregulates the reprogramming factors KFL4 and OCT4 through the IL-6/STAT3 pathway in esophageal adenocarcinoma cells. Technol Cancer Res Treat. 2020;19:1533033820945302.
Not in our library10.1177/1533033820945302
385.
Xu Y, Feingold PL, Surman DR, Brown K, Xi S, Davis JL, Hernandez J, Schrump DS, Ripley RT. Bile acid and cigarette smoke enhance the aggressive phenotype of esophageal adenocarcinoma cells by downregulation of the mitochondrial uncoupling protein-2. Oncotarget. 2017;8:101057-101071.
Not in our library10.18632/oncotarget.22380
386.
Joshi S, Cruz E, Rachagani S, Guha S, Brand RE, Ponnusamy MP, Kumar S, Batra SK. Bile acids-mediated overexpression of MUC4 via FAK-dependent c-Jun activation in pancreatic cancer. Mol Oncol. 2016;10:1063-1077.
Not in our library10.1016/j.molonc.2016.04.007

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Gut microbiota derived bile acid metabolites maintain the homeostasis of gut and systemic immunity · 2023
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