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Glut 1 in Cancer Cells and the Inhibitory Action of Resveratrol as A Potential Therapeutic Strategy

Angara Zambrano, Matías Molt, Elena Uribe and 1 more

International Journal of Molecular Sciences · 2019 · Review · CC BY

doi:10.3390/ijms20133374

Abstract

An important hallmark in cancer cells is the increase in glucose uptake. GLUT1 is an important target in cancer treatment because cancer cells upregulate GLUT1, a membrane protein that facilitates the basal uptake of glucose in most cell types, to ensure the flux of sugar into metabolic pathways. The dysregulation of GLUT1 is associated with numerous disorders, including cancer and metabolic diseases. There are natural products emerging as a source for inhibitors of glucose uptake, and resveratrol is a molecule of natural origin with many properties that acts as antioxidant and antiproliferative in malignant cells. In the present review, we discuss how GLUT1 is involved in the general scheme of cancer cell metabolism, the mechanism of glucose transport, and the importance of GLUT1 structure to understand the inhibition process. Then, we review the current state-of-the-art of resveratrol and other natural products as GLUT1 inhibitors, focusing on those directed at treating different types of cancer. Targeting GLUT1 activity is a promising strategy for the development of drugs aimed at treating neoplastic growth.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 22, 2026. Paragraph numbers are ours, so an answer can point at one.

1. Introduction

An important element in the glucose metabolism of cancer cells is the uptake of glucose. This process is well-regulated and involves several elements, such as the effect of signaling growth factors and the interaction with the extracellular matrix. To survive, cancer cells get oncogenic mutations to become independent of external regulation for glucose uptake.

Natural products have been an increasingly important source of drugs for cancer treatment. Resveratrol (RSV) is a natural compound present in red fruits with well-known antioxidant and antiproliferative properties. RSV also has many targets in the cell and there are a lot of studies of the signal pathway implicated in the survival process. Nevertheless, there are controversial reports of oxidant and antioxidant activities of RSV. This may be possibly explained by considering that RSV is a photosensitive molecule which must be carefully manipulated and used at the exact dose.

This review focuses on the importance of RSV and other small inhibitors having GLUT1 as the principal target in the cancer cell. In the first sections of the review, we illustrate the current vision of cancer cell metabolism and the role of GLUT1 as the limiting step in the flux of glucose. Then, we revisit different aspects of GLUT1, including kinetic, physiological, and some structural details. Finally, we summarize the numerous studies that have been focused on developing specific inhibitors of the activity of GLUT1, with special emphasis in natural compounds such as RSV.

There are many reports showing overexpression of GLUT1 in cancer cells. Clinically, there is a correlation between glucose uptake, diagnosis, and prognosis of tumors. We will also describe the mechanism involved in glucose transport, which is an important step for glucose uptake.

We also consider and define the differences in the energy metabolism of normal and cancer cells, as a biochemical basis for the identification of possible targets for metabolic therapy in the treatment of cancer. A promising strategy for antitumor therapy could be the inhibition of glucose transporters in neoplastic cells, thus generating a state of energy deprivation that may facilitate the effect of other anticancer therapies. It is interesting to investigate the possibility of using natural drugs such as RSV in combinatorial treatment in order to reduce the side effects and improve cancer treatments.

2. Glucose Uptake and Cancer Metabolism

In order to satisfy the higher demands of metabolites necessary for an increased proliferation, the cancer cell needs to improve the nutrients uptake from the medium. Glucose is the main nutrient for proliferation in eukaryotic cells. By means of glucose metabolism, the cell generates various intermediates and also generates reduced equivalents, such as NADH, FADH2, and NADPH, which are necessary for anabolic reactions in order to maintain a high growth rate (Figure 1). The first step of glycolysis is glucose phosphorylation by hexokinase (HK), and after many reactions pyruvate, NADH and ATP are finally obtained. In the presence of oxygen, normal cells convert pyruvate to Acetyl-CoA and use the Krebs cycle and oxidative phosphorylation (OXPHOS) pathways, which produce more ATP than glucose fermentation. In contrast, cancer cells are highly dependent of the glycolytic pathway to meet their energy requirements and prefer glucose fermentation over mitochondrial oxidation, even under aerobic conditions; this is called the Warburg effect (Figure 1, blue line). In many cancer cells, there is also an upregulation of the hexokinase 2 enzyme (HK2), together with an increased conversion of pyruvate to lactate (fermentation), which regenerates the NAD+ that feeds glycolysis, and also shows less OXPHOS activity, even in presence of oxygen. In this connection, Fantin et al. in 2006 observed that suppression of aerobic lactate production increases the OXPHOS activity in mammary tumor cells, clearly showing the preference of cancer cells for glycolysis. On the other hand, Shim et al. in 1998 found that apoptosis could be caused by glucose deprivation of transformed cancer cells, thus reinforcing the importance of the Warburg effect in cancer proliferation.

However, there are also tumors that use OXPHOS as a predominant ATP-generating mechanism (Figure 1, red line). In fact, it has been demonstrated that many tumor cell lines, such as U-937 and HeLa cells, used mitochondrial respiration to support their growth. The detection of higher mitochondrial membrane potential in tumors than normal cells provides an advantage for the detection of oxidative tumors. On the other hand, some malignant cells utilize a metabolic strategy involving aerobic glycolysis and increased activity of the Krebs cycle, fed by anaplerotic reactions with carbons from fatty acids, glutamate, glutamine or aspartate. In this connection, there are reports showing that inhibition of ATP synthesis by mitochondrial uncoupling agents in cancer cells, results in increased production of lactate in the presence of oxygen (Figure 1, black line). Interestingly, these cancer cells became resistant to apoptosis. With regard to mitochondrial uncoupling, there are mitochondrial carriers named uncoupling proteins (UCPs) that are able to control mitochondrial ROS generation that favors the survival of cancer cells. UCPs have been connected with proliferation and anaplerotic mitochondrial metabolism in cancer cells. In agreement with this, Esteves et al. in 2015 used microarray analysis to report the existence of 2 different types of cancer on the basis of UCP2 mRNA expression level with probably some metabolic differences, opening questions related to glycolysis, OXPHOS, and proliferation that must be elucidated.

Independently of which strategy is followed by a cancer cell, a hallmark of cancer is the increase in glucose uptake, and taking advantage of this fact, the positron emission tomography (PET) has been used for cancer diagnostic with the glucose analog 2-(18F)-fluoro-2-deoxy-D-glucose (FDG) as a tracer of glucose uptake. Nevertheless, this technique does not permit to evaluate whether glucose is utilized specifically by glycolysis or by the aerobic pathway including OXPHOS.

There are different studies that indicate that the Warburg effect and the mitochondrial function occur simultaneously. Therefore, the proliferating cells may use one or both ATP-producing pathways, and an understanding of the limiting reactions in their metabolism will be useful for improving anticancer therapies.

3.1. Glucose Transporters

Since sugar does not simply diffuse across the lipid bilayer, glucose uptake may be considered as the rate-limiting step for cancer cell metabolism and growth. Understanding the molecular mechanism of glucose transport becomes highly relevant because it is the starting point for the rational design of drugs aimed at blocking sugar uptake, which translates into stalling cell growth and eventually tumor death.

Glucose crosses the lipid bilayer through specialized membrane proteins known as sugar transporters. There are three well-known families of sugar transporters in mammals: GLUT family (glucose transporters), SGLT family (sodium-glucose linked transporters), and the recently discovered SWEET family (sugars will eventually be exported transporters). While describing SGLT and SWEET carriers is out of the scope of this review, here we briefly summarize their main features.

SGLT transporters are symporters that move glucose against a concentration gradient by coupling the cotransport of sodium down its concentration gradient. Thus, SGLT carriers are energetically linked to a secondary transport system, Na+/K+ ATPase, which maintains the Na+ gradient. This sets the main difference with GLUT transporters, which facilitate the movement of glucose down the concentration gradient without requiring primary or secondary ATP hydrolysis.

SGLT carriers are essential for glucose absorption in the small intestine and glucose reabsorption in the renal tissue (Further information about the function of SGLT transporters can be found in references). The SWEET carriers are less understood, although they may be part of a sugar export system. In plants, SWEET carriers play a role in the efflux of glucose of several physiological processes, including seed filling and nectar secretion. In mammals, SWEET transporters are localized in the Golgi and catalyze the efflux of glucose from Xenopus oocytes, suggesting its participation in glucose export.

Regarding the GLUT family, there are 14 members that differ in substrate selectivity, tissue expression and subcellular localization. These carriers can be further classified into three classes based on substrate specificity and sequence similarity: Class I, which includes GLUT1-4 and 14, they have high selectivity for glucose; class II, comprising GLUT5, 7, 9, and 11, which have selectivity for glucose and fructose; and the uncharacterized class III, which include GLUT6, 8, 10, 12, and 13 (known as HMIT). Members of class I are the best understood as they directly regulate sugar homeostasis. GLUT1 is expressed in most cell types and has a KM for glucose of about 3–7 mM. GLUT2, 3, and 4 are also well-studied proteins because of their relevance, together with GLUT1 in sugar homeostasis. GLUT2 and GLUT3 are low and high-affinity glucose carriers with KM for glucose of about 17 and 1 mM, respectively. GLUT2 is localized in the small intestine, liver, and pancreatic tissue, while GLUT3 is mainly found in the brain. GLUT4 has a KM for glucose similar to that of GLUT1 and is localized in vesicles that fuse with the plasma membrane in response to insulin signaling. Any dramatic and steady increase in glucose concentration, e.g., after a meal rich in sugars, induces translocation of GLUT4 to the plasma membrane, which lowers blood levels of glucose. Consequently, the physiological extracellular glucose levels are kept around 5 mM because of the direct action of GLUT1 and GLUT4. A detailed review of the GLUT family can be found in Reference.

3.2. GLUT1: Kinetic Properties and Mechanism of Transport

GLUTs proteins must perform repeated cycles of conformational changes to load and release substrate molecules on opposite sides of the biological membrane. The transport process of the GLUTs that involucrate multiple conformational changes is an essential first step for elucidating the transport mechanism. The resolution of structures of human GLUT 1 and 3 and rat GLUT 5, in different conformational states, have served as a framework for the understanding of their functional mechanism. The GLUT 1 transporter carries out the typical alternative access mechanism for the translocation of a substrate, which involves the state open to the outside, closed and open towards the interior. The substrate-binding site is alternatively shown on each side of the membrane and structural changes are continuous during a transport cycle. The comparison of GLUT1/3/5 structures in different conformational states indicates that the entry of the substrate causes movements of domains and local conformational adjustments. The conformational change from the outside to the inside of the transporter implies the rotation of the N and C domains at ~15 degrees. The N domain remains practically unchanged during conformational changes, suggesting a rigid rotation with respect to C domain. In contrast, in the C-terminal domain, the discontinuous TM7/10 helices and their neighboring segments suffer prominent local rearrangements. TM7b leans towards the core of the cavity, and TM10b moves away from the transport path while the substrate is released. The difference in the conformational changes of the N and C domains would be due to a different composition of amino acids and the structural properties of each domain. The internal core of N domain is mainly hydrophilic, although the surface oriented to the substrate is largely hydrophobic. Seven water molecules located within the N domain form H bonds with the polar residues of the TM1 and TM4 in the internal core of the N domain, which may maintain the rigidity of the N domain during the conformational changes. In contrast, the internal core of the C domain is highly hydrophobic and contains only one molecule of water, although the substrate-oriented region contains polar residues. Furthermore, GLUT proteins have an intracellular domain (ICH) that is formed by three or four helices located between the N and C domains and a short helix at the C-terminus. Together with the TM domains, the ICH domain also undergoes important changes during the translocation of the substrate. This generates a rearrangement of ICH interactions with the N and C domains. It is proposed that the ICH domain functions as a “door lock” that ensures the intracellular gate, also stabilizing the external conformation. In the same way, Quistgaard et al. in 2016 proposed a model for the MFS family of transporters that considers a movement from an occluded state to a rotation of N- and C-terminal domains outward facing or inward facing, or vice versa, that facilitates the movement of substrate from outside to inside of the membrane and vice versa during the transport cycle, reinforcing the alternating access mechanism of GLUTs. The structural information has been fundamental to elucidate the transport mechanism of GLUTs and supports the design of drugs to new therapies against several human diseases such as cancer.

3.3. GLUT1 Overexpression in Cancer Cells

As we mentioned before, GLUT1 expression is an important hallmark in many types of cancers, including breast cancer, gastric adenocarcinoma, and many other types of cancer (see Table 1). Interestingly, some cancers have been reported with a normal o decreased expression in GLUT1, such as Sarcomas, lymphomas, melanomas, and hepatoblastomas. It is important to mention that Oh et al. in 2017 made a downregulation of GLUT1 expression in breast cancer cell, getting a decrease in cellular apoptosis, induced by an up-regulation in Akt signaling pathway, suggesting that drugs focused only on GLUT1 as a therapeutic target must be evaluated in each cancer cell type.

Table 1 lists several pieces of evidence indicating the overexpression of GLUT1 in various cancer models and cell lines.

3.4. How Is GLUT1 Regulated?

Until now, several meta-analyses have suggested that GLUT1 could be used as an optimal biomarker in several cancer types. Indeed, the overexpression of GLUT1 is correlated with prognosis and survival in solid tumors.

In general, GLUTs are regulated by several molecular mechanisms. Specifically, the expression of GLUT1 is regulated by many transcription factors. It has been demonstrated that hypoxia-inducible factor (HIF-1alpha) promotes GLUT1 expression in hypoxic conditions, c-Myc has been shown to regulate GLUT1 expression in many tumors, and the un-controlled Ras pathway induces the up-regulation of GLUT1 expression. The anomalous expression of GLUT1 is also specifically affected by the PI3K/Akt pathway; Akt has been involved in the expression of GLUT1 and GLUT3 in cancer cells.

GLUT1 mRNA have different sequence motifs within the 3’-UTR, which are involved in the transcript stability and control of GLUT1 expression. The alteration of the stability of GLUT1 transcription is associated with a variation of glucose concentrations, and the presence of growth factors, cytokines, and some hormones. Also, it has been demonstrated that the long non-coding RNA HOX transcript antisense RNA (HOTAIR) is able to up-regulate GLUT1, and the same goes for the miRNA-150, which is able to regulate glycolysis by modifying GLUT1 expression.

The presence of growth factors is involved not only in modifying gene expression, but they also have further an important role inducing the translocation from intracellular compartments to the plasma membrane. Many of these growth factors stimulate PI3K/Akt signaling pathway, which enhances GLUT1 activity by increasing the membrane trafficking. This pathway is known as a master regulator of cell growth and proliferation and is highly mutated in human cancers.

4. Inhibition of Glucose Uptake by Resveratrol

Resveratrol (3,5,4′-trihydroxystilbene or RSV) is a polyphenolic natural product that attracted great interest mainly due to its anticarcinogenic, anti-inflammatory, and cardioprotective properties. RSV has structural similarities with tyrosine kinases that are known inhibitors of GLUT1. For this reason, we performed experiments in order to investigate the relationship between RSV and this transporter. By using kinetic assays, we observed for the first time that RSV inhibit the glucose uptake in human leukemic cell lines U-937 and HL-60, by a direct interaction with the internal face of GLUT1, in a noncompetitive mode.

With regard to RSV and glucose uptake, studies in different human ovarian cancer cells have shown that treatments with RSV were able to inhibit glucose uptake, lactate production, Akt, and mTOR signaling, and cell viability depending on the dose and time used. There are a great number of studies relating RSV and glucose uptake in cancer cells and in pathological conditions such as insulin resistance that we summarize in Table 2. Most of the experiments were done in vitro, but also in vivo using labeled glucose analogs. In cancer cells it is observed that resveratrol inhibited the uptake of glucose, favoring the anticancer action; but in pathological conditions such as insulin resistance or diabetes, resveratrol increased glucose uptake and insulin sensitivity favoring the antidiabetic effect. Other studies in neuronal cells showing that RSV had an inhibitory effect of the glucose uptake, favoring the neuronal regulation of glucose and insulin sensitivity. Among other mechanisms of action RSV also targets a great number of intracellular molecules implicated in cell cycle control and apoptosis induction. RSV is an attractive candidate for cancer therapy because of its unique capacity to affect the mTOR/AMPK pathway at different levels. By inhibiting mTOR and ribosomal protein S6 kinase, and by activating AMPK, RSV exerts a potent short-term effect on metabolism. The type of cell death observed in cancer cells treated with RSV has been reported as apoptosis or autophagy. Van Ginkel et al. concluded that elevated levels of RSV lead to tumor regression and widespread tumor cell death. The underlying mechanism involves direct activation of the intrinsic and extrinsic apoptotic pathway. Thus, in normal adipocytes, it has been observed that RSV induces apoptosis at concentrations greater than 20 µM, while in insulin-resistant adipocytes; RSV stimulates glucose transport via SIRT1-AMPK-Akt. These results suggest that RSV can behave differently according to the dose used and the cell type and the metabolic state. Recently, Dai et al. showed that RSV inhibits the growth and proliferation of MGC-803 cells of gastric cancer in a dose- and time-dependent way by downregulating the expression of genes related with Wnt pathway as β-catenin, c-myc, and cyclin D1, proteins related with GLUTs gene regulation. On the other hand, Kleszcz, et al. did not observe inhibition of c-myc gene expression by resveratrol in FaDu hypopharyngeal carcinoma cells, but the doses used were significantly lower. With respect to autophagy, a number of studies show that RSV induces autophagy and cell death in cancer cells when they are nutrient-deprived and that RSV could act by inducing a starvation-like signaling response. Indeed, activation of the JNK pathway by RSV leads to the induction of genes that participate in both the initial and late steps of autophagy in CML cells. RSV could also impact mitochondrial membrane potential, the respiration chain, and ATP synthesis.

RSV also stimulates the molecular pathway dependent on sirtuins, histone deacetylases, that regulates the activity of transcription factors in many tissues related to energy metabolism. RSV induces the expression of silent information regulator-6 (SIRT6) in hypopharyngeal carcinoma FaDu cell line. SIRT6 influences the expression of several glycolytic genes such as GLUT1, aldolase, pyruvate dehydrogenase kinase 1 (PDK1), and phosphofructokinase 1 (PFK1). Furthermore, RSV is known as an activator of SIRT1 and has been related to diabetes progress as a target for its treatment, inflammation, and neuroprotection. There are data suggesting that RSV has hypoglycemic properties in diabetic rats and restore glycolytic enzyme activities.

With respect to the repertoire of glycolytic isoenzymes involved in the action of RSV, Iqbal et al. observed that RSV down-regulate pyruvate kinase 2 (PKM2) expression by inhibiting mTOR signaling and suppressed cancer metabolism, characterized by a decreased glucose uptake, lower lactate production (aerobic glycolysis), and reduced anabolism (macromolecule synthesis) in various cancer cell lines. Recently, it was observed that RSV, by targeting PKM2 and ERK1/2, destabilizes BCL-2 protein level finally leading to apoptosis in human melanoma cells. In addition, the re-expression of the embryonic isoenzyme M2 of pyruvate kinase in cancerous cells has been related to a stronger glycolytic phenotype and a proliferative advantage in hypoxic conditions. HK2 seems to be associated with mitochondria, linking ATP production in this organelle to cytosolic glucose phosphorylation. The release of mitochondrial HK2 could explain the increase in cytosolic hexokinase activity implicated in the onset of apoptosis. In cardiomyocytes, during anoxia/deoxygenation injury, RSV exerts a protective effect by promoting the linkage of voltage-dependent anion channel 1 (VDAC1) to HK2. HK2 links up with VDAC1 forming a polymeric channel that finally stimulates cell survival.

Recently, RSV showed a decrease in mRNA and protein levels of GLUT1, HK2, PFK1, and PKM2 which finally caused inhibition of aerobic glycolysis in a study of VEGF-angiogenesis in human umbilical vein endothelial cells, putting forth the role of RSV in the regulation of pathological angiogenesis.

Specifically, RSV exerts effects on the GLUT1 transporter at different levels, such as:

(a) A direct inhibitory action on the protein, which has been demonstrated by kinetic assays on cancer cells (116) and interrupting the traffic to the plasma membrane.

(b) An inhibitory effect on mRNA expression for GLUT

(c) Regulating many transcription factors that in turn regulate the expression of GLUT1 such as HIF-1alpha and c-Myc

(d) Regulating GLUT1 expression through various signaling pathways such as: AMPK, Wnt, Jnk kinases, sirtuins and histone deacetylases.

(e) Also regulating miRNA expression of GLUT1.

RSV also is able to regulate glucose uptake, metabolism and signaling pathway in cancer cells through regulation of specific microRNAs (miRNAs). Resveratrol affects the miRNA machinery in positive and negative manners; it is suggested that this regulatory activity is likely to be advantageous for cancer treatment and prevention. There are many miRNAs that are dysregulated in cancers. In resveratrol-treated prostate cancer cells there are significant upregulations of 28 miRNAs and downregulations of 23 miRNAs. Among these, two miRNA clusters, such as miR-17-92 and miR-106ab, are known oncomirs. Subsequent analyses showed significant downregulation of these oncomirs in resveratrol-treated prostate cancer cells. In the case of breast cancer, miR-663 and miR-744 have been found to negatively regulate eEF1A2, resveratrol induces a 4.5-fold upregulation of miR-663 and a two-fold increase in miR-744, resveratrol also controls breast cancer cell proliferation by inducing tumor-suppressive miRNAs (miR-34a, miR-424, and miR-503) via the p53 pathway and then by suppressing heterogeneous nuclear ribonucleoprotein A1 (HNRNPA1), which is associated with tumor progression. There are many interesting studies about the molecular mechanisms associating resveratrol and miRNA regulation in cancer. For example, resveratrol targets the oncogenic expression of miR-21, thus blocking the PI3K-Akt signaling, and it also reduces MMP2 via upregulation of miR-328 in osteosarcoma cells.

Several miRNAs have an important impact on metabolism in cancer cells. Some miRNAs such as miR-150 were consistently decreased in cell lines and osteosarcoma tissues as compared to osteoblast cells and normal bone; the ectopic overexpression of miR-150 inhibits osteosarcoma cell proliferation and suppresses glucose uptake. On the other hand, loss of function of miR-150 enhanced osteosarcoma cell proliferation and increased glucose uptake and lactate secretion. In colon cancer cells, the miRNA-143 overexpression inhibits glucose uptake and glucose transporter 1 (GLUT1) expression. Many miRNAs are associated to regulated GLUTs expression, for example; miR-21a-5p, miR-29a-3p, miR-29c-3p, miR-93-5p, miR-106b-5p, miR-133a-3p, miR-133b-3p, miR-222-3p, and miR-223-3p have been reported to directly and/or indirectly regulate the GLUT4 expression; and their expressions are altered principally in the diabetes condition.

Recent evidences demonstrate that miRNAs play important roles in certain effects of resveratrol on cell metabolism. Pyruvate kinase M2 (PKM2) has been found to be overexpressed in different cancers; it has been shown that resveratrol represses PKM2 by increasing the expression of miR-326. Also, resveratrol improves mitochondrial function. Specifically, the miR-27b was significantly induced in a dose-dependent way in skeletal muscle and C2C12 myoblast treated with resveratrol, and miR-27b overexpression improves mitochondrial function in a Sirt1-dependent manner.

5. Inhibition of GLUT1 by Other Small Molecules

Because of the relevance of GLUT1 in cancer, GLUT1 is a potential target for therapy with small molecule inhibitors. GLUT1 is inhibited by small natural and synthetic molecules belonging to different families of organic compounds. Table 3 lists different small molecule inhibitors that have been characterized by testing natural compounds or libraries of preexisting compounds. Several of these molecules can be obtained directly from the diet, as they are found in fruits and leaves (e.g., grapes), and bind directly to the transporter. Examples include phloretin and cytochalasin B, flavones and flavonoids, and tyrosine-kinase inhibitors. Also, we have characterized the effect of NDGA, gossypol, methylxanthines, and resveratrol in glucose uptake using kinetic analyses. These natural compounds showed different patterns of inhibition, including acting as competitive, noncompetitive and mixed inhibitors. Although these kinetic analyses provide evidence on the effects of small molecules on GLUT1, little is known about the structural or functional details behind the inhibition. For example, the exact binding sites are unknown, although the current knowledge points to its binding to the extracellular or intracellular face of the transporter. Even in the case of competitive inhibition, it is not clear whether these small molecules bind to the glucose binding site or to a second site that makes glucose or inhibitor binding mutually exclusive, or both.

6. Conclusion and Final Remarks

Natural products have been the inspiration and the source of drugs and medicines that we currently use. RSV, due to its hypoglycemic and inhibitory of glucose uptake properties, emerged as an alternative for different diseases such as diabetes and cancer. Throughout this manuscript, we have reviewed the importance of RSV and GLUT1 in glucose metabolism since metabolic alterations are a hallmark of cancer. Also, we have described everything related to the structure, regulation, expression, and overexpression of GLUT1 used as diagnostic for cancer. All this important information has served as a basis for the design of transport inhibitory molecules in different target cells. The latest structural data made it possible to design in silico specific inhibitors of GLUTs, to be validated in vitro and in vivo. Transport experiments in cells are difficult, which makes this goal tough. While all cells need glucose to live, partial inhibition of transport and specifically GLUT1 as mono-therapy was unsuccessful. New and novel combinatorial strategies that could use GLUT1 inhibitors such as RSV with anticancer conventional drugs for therapy are promising, decreasing the side effects of and maximizing the therapeutic effects.

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    Christlieb S.B., Strandholdt C.N., Olsen B.B., Mylam K.J., Larsen T.S., Nielsen A.L., Rohde M., Gerke O., Olsen K.E., Møller M.B., et al. Dual time-point FDG PET/CT and FDG uptake and related enzymes in lymphadenopathies: Preliminary results. Eur. J. Nucl. Med. Mol. Imaging. 2016;43:1824-1836.

    Not in our library10.1007/s00259-016-3385-6

  26. 26.

    Fantin V.R., St-Pierre J., Leder P. Attenuation of LDH-A expression uncovers a link between glycolysis, mitochondrial physiology, and tumor maintenance. Cancer Cell. 2006;9:425-434.

    Not in our library10.1016/j.ccr.2006.04.023

  27. 27.
    A unique glucose-dependent apoptotic pathway induced by c-Myc · 1998
    Not checked
  28. 28.

    Zu X.L., Guppy M. Cancer metabolism: Facts, fantasy, and fiction. Biochem. Biophys. Res. Commun. 2004;313:459-465.

    Not in our library10.1016/j.bbrc.2003.11.136

  29. 29.

    Rodríguez-Enríquez S., Carreño-Fuentes L., Gallardo-Pérez J.C., Saavedra E., Quezada H., Vega A., Marín-Hernández A., Olín-Sandoval V., Torres-Márquez M.E., Moreno-Sánchez R. Oxidative phosphorylation is impaired by prolonged hypoxia in breast and possibly in cervix carcinoma. Int. J. Biochem. Cell Biol. 2010;42:1744-1751.

    Not in our library10.1016/j.biocel.2010.07.010

  30. 30.

    Elwood J.C., Lin Y.-C., Cristofalo V.J., Weinhouse S., Morris H.P. Glucose Utilization in Homogenates of the Morris Hepatoma 5123 and Related Tumors. Cancer Res. 1963;23:906-913.

    Not in our library

  31. 31.

    Kallinowski F., Schlenger K.H., Kloes M., Stohrer M., Vaupel P. Tumor blood flow: The principal modulator of oxidative and glycolytic metabolism, and of the metabolic micromilieu of human tumor xenografts in vivo. Int. J. Cancer. 2018;44:266-272.

    Not in our library10.1002/ijc.2910440214

  32. 32.

    Balaban R.S., Bader J.P. Studies on the relationship between glycolysis and (Na++K+)-ATPase in cultured cells. Biochim. Biophys. Acta—Mol. Cell Res. 1984;804:419-426.

    Not in our library10.1016/0167-4889(84)90069-7

  33. 33.

    Griguer C.E., Oliva C.R., Gillespie G.Y. Glucose metabolism heterogeneity in human and mouse malignant glioma cell lines. J. Neurooncol. 2005;74:123-133.

    Not in our library10.1007/s11060-004-6404-6

  34. 34.

    Bouzier A.-K., Voisin P., Goodwin R., Canioni P., Merle M. Glucose and Lactate Metabolism in C6 Glioma Cells: Evidence for the Preferential Utilization of Lactate for Cell Oxidative Metabolism. Dev. Neurosci. 1998;20:331-338.

    Not in our library10.1159/000017328

  35. 35.

    Rossignol R., Gilkerson R., Aggeler R., Yamagata K., Remington S.J., Capaldi R.A. Energy Substrate Modulates Mitochondrial Structure and Oxidative Capacity in Cancer Cells. Cancer Res. 2004;64:985-993.

    Not in our library10.1158/0008-5472.can-03-1101

  36. 36.

    Smolková K., Bellance N., Scandurra F., Génot E., Gnaiger E., Plecitá-Hlavatá L., Ježek P., Rossignol R. Mitochondrial bioenergetic adaptations of breast cancer cells to aglycemia and hypoxia. J. Bioenerg. Biomembr. 2010;42:55-67.

    Not in our library10.1007/s10863-009-9267-x

  37. 37.

    Moreno-Sánchez R., Rodríguez-Enríquez S., Marín-Hernández A., Saavedra E. Energy metabolism in tumor cells. FEBS J. 2007;274:1393-1418.

    Not in our library10.1111/j.1742-4658.2007.05686.x

  38. 38.

    Samudio I., Fiegl M., McQueen T., Clise-Dwyer K., Andreeff M. The Warburg effect in leukemia-stroma cocultures is mediated by mitochondrial uncoupling associated with uncoupling protein 2 activation. Cancer Res. 2008;68:5198-5205.

    Not in our library10.1158/0008-5472.can-08-0555

  39. 39.

    Samudio I., Harmancey R., Fiegl M., Kantarjian H., Konopleva M., Korchin B., Kaluarachchi K., Bornmann W., Duvvuri S., Taegtmeyer H., et al. Pharmacologic inhibition of fatty acid oxidation sensitizes human leukemia cells to apoptosis induction. J. Clin. Invest. 2010;120:142-156.

    Not in our library10.1172/jci38942

  40. 40.

    Vélez J., Hail N., Konopleva M., Zeng Z., Kojima K., Samudio I., Andreeff M. Mitochondrial Uncoupling and the Reprograming of Intermediary Metabolism in Leukemia Cells. Front. Oncol. 2013;3:67.

    Not in our library10.3389/fonc.2013.00067

  41. 41.

    Baffy G. Mitochondrial uncoupling in cancer cells: Liabilities and opportunities. Biochim. Biophys. Acta. Bioenerg. 2017;1858:655-664.

    Not in our library10.1016/j.bbabio.2017.01.005

  42. 42.

    Esteves P., Pecqueur C., Alves-Guerra M.-C. UCP2 induces metabolic reprogramming to inhibit proliferation of cancer cells. Mol. Cell. Oncol. 2015;2:e975024.

    Not in our library10.4161/23723556.2014.975024

  43. 43.

    Wuest M., Hamann I., Bouvet V., Glubrecht D., Marshall A., Trayner B., Soueidan O.-M., Krys D., Wagner M., Cheeseman C., et al. Molecular Imaging of GLUT1 and GLUT5 in Breast Cancer: A Multitracer Positron Emission Tomography Imaging Study in Mice. Mol. Pharmacol. 2018;93:79-89.

    Not in our library10.1124/mol.117.110007

  44. 44.

    Liberti M.V., Locasale J.W. The Warburg Effect: How Does it Benefit Cancer Cells? Trends Biochem. Sci. 2016;41:211-218.

    Not in our library10.1016/j.tibs.2015.12.001

  45. 45.

    Mueckler M., Thorens B. The SLC2 (GLUT) family of membrane transporters. Mol. Aspects Med. 2013;34:121-138.

    Not in our library10.1016/j.mam.2012.07.001

  46. 46.

    Chen L.-Q., Cheung L.S., Feng L., Tanner W., Frommer W.B. Transport of Sugars. Annu. Rev. Biochem. 2015;84:865-894.

    Not in our library10.1146/annurev-biochem-060614-033904

  47. 47.

    Feng L., Frommer W.B. Structure and function of SemiSWEET and SWEET sugar transporters. Trends Biochem. Sci. 2015;40:480-486.

    Not in our library10.1016/j.tibs.2015.05.005

  48. 48.

    Deng D., Yan N. GLUT, SGLT, and SWEET: Structural and mechanistic investigations of the glucose transporters. Protein Sci. 2015;25:546-558.

    Not in our library10.1002/pro.2858

  49. 49.

    Wright E.M., Ghezzi C., Loo D.D.F. Novel and Unexpected Functions of SGLTs. Physiology. 2017;32:435-443.

    Not in our library10.1152/physiol.00021.2017

  50. 50.

    Sosso D., Luo D., Li Q.-B., Sasse J., Yang J., Gendrot G., Suzuki M., Koch K.E., McCarty D.R., Chourey P.S., et al. Seed filling in domesticated maize and rice depends on SWEET-mediated hexose transport. Nat. Genet. 2015;47:1489.

    Not in our library10.1038/ng.3422

  51. 51.

    Lin I.W., Sosso D., Chen L.-Q., Gase K., Kim S.-G., Kessler D., Klinkenberg P.M., Gorder M.K., Hou B.-H., Qu X.-Q., et al. Nectar secretion requires sucrose phosphate synthases and the sugar transporter SWEET9. Nature. 2014;508:546.

    Not in our library10.1038/nature13082

  52. 52.

    Chen L.-Q., Hou B.-H., Lalonde S., Takanaga H., Hartung M.L., Qu X.-Q., Guo W.-J., Kim J.-G., Underwood W., Chaudhuri B., et al. Sugar transporters for intercellular exchange and nutrition of pathogens. Nature. 2010;468:527.

    Not in our library10.1038/nature09606

  53. 53.

    Thorens B., Mueckler M. Glucose transporters in the 21st Century. Am. J. Physiol. Metab. 2009;298:E141-E145.

    Not in our library10.1152/ajpendo.00712.2009

  54. 54.

    Burant C.F., Bell G.I. Mammalian facilitative glucose transporters: Evidence for similar substrate recognition sites in functionally monomeric proteins. Biochemistry. 1992;31:10414-10420.

    Not in our library10.1021/bi00157a032

  55. 55.

    Ojeda P., Pérez A., Ojeda L., Vargas-Uribe M., Rivas C.I., Salas M., Vera J.C., Reyes A.M. Noncompetitive blocking of human GLUT1 hexose transporter by methylxanthines reveals an exofacial regulatory binding site. Am. J. Physiol. Physiol. 2012;303:C530-C539.

    Not in our library10.1152/ajpcell.00145.2012

  56. 56.

    Leto D., Saltiel A.R. Regulation of glucose transport by insulin: Traffic control of GLUT4. Nat. Rev. Mol. Cell Biol. 2012;13:383.

    Not in our library10.1038/nrm3351

  57. 57.

    Yan N. A Glimpse of Membrane Transport through Structures—Advances in the Structural Biology of the GLUT Glucose Transporters. J. Mol. Biol. 2017;429:2710-2725.

    Not in our library10.1016/j.jmb.2017.07.009

  58. 58.

    Deng D., Xu C., Sun P., Wu J., Yan C., Hu M., Yan N. Crystal structure of the human glucose transporter GLUT1. Nature. 2014;510:121.

    Not in our library10.1038/nature13306

  59. 59.

    Kapoor K., Finer-Moore J.S., Pedersen B.P., Caboni L., Waight A., Hillig R.C., Bringmann P., Heisler I., Müller T., Siebeneicher H., et al. Mechanism of inhibition of human glucose transporter GLUT1 is conserved between cytochalasin B and phenylalanine amides. Proc. Natl. Acad. Sci. USA. 2016;113:4711-4716.

    Not in our library10.1073/pnas.1603735113

  60. 60.

    Nomura N., Verdon G., Kang H.J., Shimamura T., Nomura Y., Sonoda Y., Hussien S.A., Qureshi A.A., Coincon M., Sato Y., et al. Structure and mechanism of the mammalian fructose transporter GLUT5. Nature. 2015;526:397.

    Not in our library10.1038/nature14909

  61. 61.

    Deng D., Sun P., Yan C., Ke M., Jiang X., Xiong L., Ren W., Hirata K., Yamamoto M., Fan S., et al. Molecular basis of ligand recognition and transport by glucose transporters. Nature. 2015;526:391.

    Not in our library10.1038/nature14655

  62. 62.

    Kumar S., Nussinov R. Close-Range Electrostatic Interactions in Proteins. ChemBioChem. 2002;3:604-617.

    Not in our library10.1002/1439-7633(20020703)3:7<604::aid-cbic604>3.0.co;2-x

  63. 63.

    Yan N. Structural advances for the major facilitator superfamily (MFS) transporters. Trends Biochem. Sci. 2013;38:151-159.

    Not in our library10.1016/j.tibs.2013.01.003

  64. 64.

    Quistgaard E.M., Löw C., Guettou F., Nordlund P. Understanding transport by the major facilitator superfamily (MFS): Structures pave the way. Nat. Rev. Mol. Cell Biol. 2016;17:123.

    Not in our library10.1038/nrm.2015.25

  65. 65.
    GLUT1 expression in malignant tumors and its use as an immunodiagnostic marker · 2011
    Not checked
  66. 66.

    Parente P., Coli A., Massi G., Mangoni A., Fabrizi M.M., Bigotti G. Immunohistochemical expression of the glucose transporters Glut-1 and Glut-3 in human malignant melanomas and benign melanocytic lesions. J. Exp. Clin. Cancer Res. 2008;27:34.

    Not in our library10.1186/1756-9966-27-34

  67. 67.

    Oh S., Kim H., Nam K., Shin I. Silencing of Glut1 induces chemoresistance via modulation of Akt/GSK-3β/β-catenin/survivin signaling pathway in breast cancer cells. Arch. Biochem. Biophys. 2017;636:110-122.

    Not in our library10.1016/j.abb.2017.08.009

  68. 68.

    Younes M., Brown R.W., Mody D.R., Fernandez L., Laucirica R. GLUT1 expression in human breast carcinoma: Correlation with known prognostic markers. Anticancer Res. 1995;15:2895-2898.

    Not in our library

  69. 69.

    Cantuaria G., Magalhaes A., Penalver M., Angioli R., Braunschweiger P., Gomez-Marin O., Kanhoush R., Gomez-Fernandez C., Nadji M. Expression of GLUT-1 Glucose Transporter in Borderline and Malignant Epithelial Tumors of the Ovary. Gynecol. Oncol. 2000;79:33-37.

    Not in our library10.1006/gyno.2000.5910

  70. 70.

    Semaan A., Munkarah A.R., Arabi H., Bandyopadhyay S., Seward S., Kumar S., Qazi A., Hussein Y., Morris R.T., Ali-Fehmi R. Expression of GLUT-1 in epithelial ovarian carcinoma: Correlation with tumor cell proliferation, angiogenesis, survival and ability to predict optimal cytoreduction. Gynecol. Oncol. 2011;121:181-186.

    Not in our library10.1016/j.ygyno.2010.11.019

  71. 71.

    Chandler J.D., Williams E.D., Slavin J.L., Best J.D., Rogers S. Expression and localization of GLUT1 and GLUT12 in prostate carcinoma. Cancer. 2003;97:2035-2042.

    Not in our library10.1002/cncr.11293

  72. 72.

    Reinicke K., Sotomayor P., Cisterna P., Delgado C., Nualart F., Godoy A. Cellular distribution of Glut-1 and Glut-5 in benign and malignant human prostate tissue. J. Cell. Biochem. 2011;113:553-562.

    Not in our library10.1002/jcb.23379

  73. 73.

    Grabellus F., Nagarajah J., Bockisch A., Schmid K.W., Sheu S.-Y. Glucose Transporter 1 Expression, Tumor Proliferation, and Iodine/Glucose Uptake in Thyroid Cancer With Emphasis on Poorly Differentiated Thyroid Carcinoma. Clin. Nucl. Med. 2012;37:121-127.

    Not in our library10.1097/rlu.0b013e3182393599

  74. 74.

    Cooper R., Sarioğlu S., Sökmen S., Füzün M., Küpelioğlu A., Valentine H., Görken I.B., Airley R., West C. Glucose transporter-1 (GLUT-1): A potential marker of prognosis in rectal carcinoma? Br. J. Cancer. 2003;89:870.

    Not in our library10.1038/sj.bjc.6601202

  75. 75.

    Abdou A.G., Eldien M.M.S., Elsakka D. GLUT-1 Expression in Cutaneous Basal and Squamous Cell Carcinomas. Int. J. Surg. Pathol. 2015;23:447-453.

    Not in our library10.1177/1066896915589968

  76. 76.

    Haber R.S., Rathan A., Weiser K.R., Pritsker A., Itzkowitz S.H., Bodian C., Slater G., Weiss A., Burstein D.E. GLUT1 glucose transporter expression in colorectal carcinoma. Cancer. 2000;83:34-40.

    Not in our library10.1002/(sici)1097-0142(19980701)83:1<34::aid-cncr5>3.0.co;2-e

  77. 77.

    Jun Y.J., Jang S.M., Han H.L., Lee K.H., Jang K.S., Paik S.S. Clinicopathologic signifcance of GULT1 expression and its correlation with Apaf-1 in colorectal adenocarcinomas. World J. Gastroenterol. 2011;17:1866-1873.

    Not in our library10.3748/wjg.v17.i14.1866

  78. 78.

    Sakashita M., Aoyama N., Minami R., Maekawa S., Kuroda K., Shirasaka D., Ichihara T., Kuroda Y., Maeda S., Kasuga M. Glut1 expression in T1 and T2 stage colorectal carcinomas: Its relationship to clinicopathological features. Eur. J. Cancer. 2001;37:204-209.

    Not in our library10.1016/s0959-8049(00)00371-3

  79. 79.

    Giatromanolaki A., Sivridis E., Arelaki S., Koukourakis M.I. Expression of enzymes related to glucose metabolism in non-small cell lung cancer and prognosis. Exp. Lung Res. 2017;43:167-174.

    Not in our library10.1080/01902148.2017.1328714

  80. 80.
    Glut1 and Glut3 as Potential Prognostic Markers for Oral Squamous Cell Carcinoma · 2010
    No notice
  81. 81.

    Oliver R.J., Woodwards R.T.M., Sloan P., Thakker N.S., Stratford I.J., Airley R.E. Prognostic value of facilitative glucose transporter Glut-1 in oral squamous cell carcinomas treated by surgical resection: Results of EORTC Translational Research Fund studies. Eur. J. Cancer. 2004;40:503-507.

    Not in our library10.1016/j.ejca.2003.10.024

  82. 82.

    Choi Y.S., Kim S.J., Kim D.S., Park S.J., Park Y., Shin H.J., Jung K.-Y., Baek S.-K., Shin B.K., Choi J.W., et al. Glucose Transporter-1 Expression in Squamous Cell Carcinoma of the Tongue. Cancer Res. Treat. 2007;39:109-115.

    Not in our library10.4143/crt.2007.39.3.109

  83. 83.

    Chiba I., Ogawa K., Morioka T., Shimoji H., Sunagawa N.A.O., Iraha S., Nishimaki T., Yoshimi N., Murayama S. Clinical significance of GLUT-1 expression in patients with esophageal cancer treated with concurrent chemoradiotherapy. Oncol. Lett. 2011;2:21-28.

    Not in our library10.3892/ol.2010.199

  84. 84.

    Lee J.-H., Kim Y.-W., Chang S.-G. Glucose Transporter-1 Expression in Urothelial Papilloma of the Bladder. Urol. Int. 2005;74:268-271.

    Not in our library10.1159/000083561

  85. 85.

    Nes J.A.P., Griewank K.G., Schmid K.-W., Grabellus F. Immunocytochemical analysis of glucose transporter protein-1 (GLUT-1) in typical, brain invasive, atypical and anaplastic meningioma. Neuropathology. 2014;35:24-36.

    Not in our library10.1111/neup.12148

  86. 86.

    Luo X.-M., Zhou S.-H., Fan J. Glucose Transporter-1 as a New Therapeutic Target in Laryngeal Carcinoma. J. Int. Med. Res. 2010;38:1885-1892.

    Not in our library10.1177/147323001003800601

  87. 87.

    Fang J., Luo X.-M., Yao H.-T., Zhou S.-H., Ruan L.-X., Yan S.-X. Expression of Glucose Transporter-1, Hypoxia-Inducible Factor-1α, Phosphatidylinositol 3-Kinase and Protein Kinase B (Akt) in Relation to [18F]Fluorodeoxyglucose Uptake in Nasopharyngeal Diffuse Large B-Cell Lymphoma: A Case Report and Literature Review. J. Int. Med. Res. 2010;38:2160-2168.

    Not in our library10.1177/147323001003800632

  88. 88.

    Basturk O., Singh R., Kaygusuz E., Balci S., Dursun N., Culhaci N., Adsay N.V. GLUT-1 Expression in Pancreatic Neoplasia: Implications in Pathogenesis, Diagnosis, and Prognosis. Pancreas. 2011;40:187-192.

    Not in our library10.1097/mpa.0b013e318201c935

  89. 89.

    Chan D.A., Sutphin P.D., Nguyen P., Turcotte S., Lai E.W., Banh A., Reynolds G.E., Chi J.-T., Wu J., Solow-Cordero D.E., et al. Targeting GLUT1 and the Warburg Effect in Renal Cell Carcinoma by Chemical Synthetic Lethality. Sci. Transl. Med. 2011;3:94ra70.

    Not in our library10.1126/scitranslmed.3002394

  90. 90.

    Nagase Y., Takata K., Moriyama N., Aso Y., Murakami T., Hirano H. Investigative Urology: Immunohistochemical Localization of Glucose Transporters in Human Renal Cell Carcinoma. J. Urol. 1995;153:798-801.

    Not in our library10.1016/s0022-5347(01)67725-5

  91. 91.

    Amann T., Hellerbrand C. GLUT1 as a therapeutic target in hepatocellular carcinoma. Expert Opin. Ther. Targets. 2009;13:1411-1427.

    Not in our library10.1517/14728220903307509

  92. 92.

    Ogawa J., Inoue H., Koide S. Glucose-transporter-type-I-gene amplification correlates with Sialyl-Lewis-X synthesis and proliferation in lung cancer. Int. J. Cancer. 1998;74:189-192.

    Not in our library10.1002/(sici)1097-0215(19970422)74:2<189::aid-ijc9>3.0.co;2-v

  93. 93.

    Rudlowski C., Becker A.J., Schroder W., Rath W., Büttner R., Moser M. GLUT1 Messenger RNA and Protein Induction Relates to the Malignant Transformation of Cervical Cancer. Am. J. Clin. Pathol. 2003;120:691-698.

    Not in our library10.1309/4kynqm5862jw2gd7

  94. 94.
    The prognostic value of GLUT1 in cancers: a systematic review and meta-analysis · 2017
    No notice
  95. 95.
    Glucose transporter GLUT1 expression and clinical outcome in solid tumors: a systematic review and meta-analysis · 2017
    No notice
  96. 96.

    Okino S.T., Chichester C.H., Withlock J.P. Hypoxia-indicible mammalian gene expression analysed in vivo at a TATA-driven promoter and at an-initiator-driven promoter. J. Biol. Chem. 1998;273:23837.

    Not in our library10.1074/jbc.273.37.23837

  97. 97.

    Zelzer E., Levy Y., Kahana C., Shilo B., Rubinstein M., Cohen B. Insulin induces transcription of target genes through the hypoxia-inducible factor HIF-1α/ARNT. EMBO J. 1998;17:5085-5094.

    Not in our library10.1093/emboj/17.17.5085

  98. 98.

    Ebert B.L., Firth J.D., Peter J., Ebert B.L., Firth J.D., Ratcliffe P.J. Cell Biology and Metabolism: Hypoxia and Mitochondrial Inhibitors Regulate Expression of Glucose Transporter-1 via Distinct Cis-acting Sequences Hypoxia and Mitochondrial Inhibitors Regulate Expression of Glucose Transporter-1 via Distinct Cis-acting Seq. J. Biol. Chem. 1995;270:29083-29089.

    Not in our library10.1074/jbc.270.49.29083

  99. 99.

    Osthus R.C., Shim H., Kim S., Li Q., Reddy R., Mukherjee M., Xu Y., Wonsey D., Lee L.A., Dang C.V. Deregulation of glucose transporter 1 and glycolytic gene expression by c-Myc. J. Biol. Chem. 2000;275:21797-21800.

    Not in our library10.1074/jbc.c000023200

  100. 100.

    Chen C., Pore N., Behrooz A., Ismail-Beigi F., Maity A. Regulation of glut1 mRNA by hypoxia-inducible factor-1. Interaction between H-ras and hypoxia. J. Biol. Chem. 2001;276:9519-9525.

    Not in our library10.1074/jbc.m010144200

  101. 101.

    Yun J., Rago C., Cheong I., Pagliarini R., Angenendt P., Rajagopalan H., Schmidt K., Willson J.K.V., Markowitz S., Zhou S., et al. Glucose Deprivation Contributes to the Development of KRAS Pathway Mutations in Tumor Cells. Science. 2009;325:1555-1559.

    Not in our library10.1126/science.1174229

  102. 102.

    Jacobs S.R., Herman C.E., MacIver N.J., Wofford J.A., Wieman H.L., Hammen J.J., Rathmell J.C. Glucose Uptake Is Limiting in T Cell Activation and Requires CD28-Mediated Akt-Dependent and Independent Pathways. J. Immunol. 2008;180:4476-4486.

    Not in our library10.4049/jimmunol.180.7.4476

  103. 103.

    Wofford J.A., Wieman H.L., Jacobs S.R., Zhao Y., Rathmell J.C. IL-7 promotes Glut1 trafficking and glucose uptake via STAT5-mediated activation of Akt to support T-cell survival. Blood. 2008;111:2101-2111.

    Not in our library10.1182/blood-2007-06-096297

  104. 104.

    Barthel A., Okino S.T., Liao J., Nakatani K., Li J., Whitlock J.P., Roth R.A. Regulation of GLUT1 gene transcription by the serine/threonine kinase Akt1. J. Biol. Chem. 1999;274:20281-20286.

    Not in our library10.1074/jbc.274.29.20281

  105. 105.

    Qi C., Pekala P.H. The Influence of mRNA Stability on Glucose Transporter (GLUT1) Gene Expression. Biochem. Biophys. Res. Commun. 1999;263:265-269.

    Not in our library10.1006/bbrc.1999.1328

  106. 106.

    Wei S., Fan Q., Liang Y., Xiaodong Z., Ma Y., Zhihong Z., Hua X., Su D., Sun H., Li H., et al. Promotion of glycolysis by HOTAIR through GLUT1 upregulation via mTOR signaling. Oncol. Rep. 2017;38:1902-1908.

    Not in our library10.3892/or.2017.5840

  107. 107.

    Yuan G., Zhao Y., Wu D., Gao C. Mir-150 Up-Regulates Glut1 and Increases Glycolysis in Osteosarcoma Cells. Asian Pac. J. Cancer Prev. 2017;18:1127-1131.

    Not in our library10.22034/apjcp.2017.18.4.1127

  108. 108.

    Zambrano A., Jara E., Murgas P., Jara C., Castro M.A., Angulo C., Concha I.I. Cytokine stimulation promotes increased glucose uptake via translocation at the plasma membrane of GLUT1 in HEK293 cells. J. Cell. Biochem. 2010;110:1471-1480.

    Not in our library10.1002/jcb.22711

  109. 109.

    Wieman H.L., Wofford J.A., Rathmell J.C. Cytokine Stimulation Promotes Glucose Uptake via Phosphatidylinositol-3 Kinase/Akt Regulation of Glut1 Activity and Trafficking. Mol. Biol. Cell. 2007;18:1437-1446.

    Not in our library10.1091/mbc.e06-07-0593

  110. 110.

    Melstrom L.G., Salabat M.R., Ding X.-Z., Milam B.M., Strouch M., Pelling J.C., Bentrem D.J. Apigenin Inhibits the GLUT-1 Glucose Transporter and the Phosphoinositide 3-Kinase/Akt Pathway in Human Pancreatic Cancer Cells. Pancreas. 2008;37:426-431.

    Not in our library10.1097/mpa.0b013e3181735ccb

  111. 111.

    Bishayee A. Cancer Prevention and Treatment with Resveratrol: From Rodent Studies to Clinical Trials. Cancer Prev. Res. 2009;2:409-418.

    Not in our library10.1158/1940-6207.capr-08-0160

  112. 112.

    Pirola L., Fröjdö S. Resveratrol: One molecule, many targets. IUBMB Life. 2008;60:323-332.

    Not in our library10.1002/iub.47

  113. 113.

    Subramanian L., Youssef S., Bhattacharya S., Kenealey J., Polans A.S., van Ginkel P.R. Resveratrol: Challenges in Translation to the Clinic—A Critical Discussion. Clin. Cancer Res. 2010;16:5942-5948.

    Not in our library10.1158/1078-0432.ccr-10-1486

  114. 114.

    Vera J.C., Reyes A.M., Velásquez F.V., Rivas C.I., Zhang R.H., Strobel P., Slebe J.C., Núñez-Alarcón J., Golde D.W. Direct Inhibition of the Hexose Transporter GLUT1 by Tyrosine Kinase Inhibitors. Biochemistry. 2001;40:777-790.

    Not in our library10.1021/bi001660j

  115. 115.

    Vera J.C., Reyes A.M., Cárcamo J.G., Velásquez F.V., Rivas C.I., Zhang R.H., Strobel P., Iribarren R., Scher H.I., Slebe J.C., et al. Genistein is a natural inhibitor of hexose and dehydroascorbic acid transport through the glucose transporter, GLUT1. J. Biol. Chem. 1996;271:8719-8724.

    Not in our library10.1074/jbc.271.15.8719

  116. 116.

    Salas M., Obando P., Ojeda L., Ojeda P., Pérez A., Vargas-Uribe M., Rivas C.I., Vera J.C., Reyes A.M. Resolution of the direct interaction with and inhibition of the human GLUT1 hexose transporter by resveratrol from its effect on glucose accumulation. Am. J. Physiol. Physiol. 2013;305:C90-C99.

    Not in our library10.1152/ajpcell.00387.2012

  117. 117.

    Kueck A., Opipari A.W., Griffith K.A., Tan L., Choi M., Huang J., Wahl H., Liu J.R. Resveratrol inhibits glucose metabolism in human ovarian cancer cells. Gynecol. Oncol. 2007;107:450-457.

    Not in our library10.1016/j.ygyno.2007.07.065

  118. 118.

    Opipari A.W., Tan L., Boitano A.E., Sorenson D.R., Aurora A., Liu J.R. Resveratrol-induced Autophagocytosis in Ovarian Cancer Cells. Cancer Res. 2004;64:696-703.

    Not in our library10.1158/0008-5472.can-03-2404

  119. 119.

    Liu Y., Tong L., Luo Y., Li X., Chen G., Wang Y. Resveratrol inhibits the proliferation and induces the apoptosis in ovarian cancer cells via inhibiting glycolysis and targeting AMPK/mTOR signaling pathway. J. Cell. Biochem. 2018;119:6162-6172.

    Not in our library10.1002/jcb.26822

  120. 120.

    Chen S., Zhao Z., Ke L., Li Z., Li W., Zhang Z., Zhou Y., Feng X., Zhu W. Resveratrol improves glucose uptake in insulin-resistant adipocytes via Sirt1. J. Nutr. Biochem. 2018;55:209-218.

    Not in our library10.1016/j.jnutbio.2018.02.007

  121. 121.

    Varshney P., Dey C.S. Resveratrol regulates neuronal glucose uptake and insulin sensitivity via P21-activated kinase 2 (PAK2). Biochem. Biophys. Res. Commun. 2017;485:372-378.

    Not in our library10.1016/j.bbrc.2017.02.070

  122. 122.

    Delmas D., Lancon A., Colin D., Jannin B., Latruffe N. Resveratrol as a Chemopreventive Agent: A Promising Molecule for Fighting Cancer. Curr. Drug Targets. 2006;7:423-442.

    Not in our library10.2174/138945006776359331

  123. 123.

    Baur J.A., Sinclair D.A. Therapeutic potential of resveratrol: The in vivo evidence. Nat. Rev. Drug Discov. 2006;5:493.

    Not in our library10.1038/nrd2060

  124. 124.

    Park S.-J., Ahmad F., Philp A., Baar K., Williams T., Luo H., Ke H., Rehmann H., Taussig R., Brown A.L., et al. Resveratrol ameliorates aging-related metabolic phenotypes by inhibiting cAMP phosphodiesterases. Cell. 2012;148:421-433.

    Not in our library10.1016/j.cell.2012.01.017

  125. 125.

    Alarcón de la Lastra C., Villegas I. Resveratrol as an anti-inflammatory and anti-aging agent: Mechanisms and clinical implications. Mol. Nutr. Food Res. 2005;49:405-430.

    Not in our library10.1002/mnfr.200500022

  126. 126.

    Meeran S.M., Katiyar S.K. Cell cycle control as a basis for cancer chemoprevention through dietary agents. Front. Biosci. 2008;13:2191-2202.

    Not in our library10.2741/2834

  127. 127.

    Van Ginkel P.R., Sareen D., Subramanian L., Walker Q., Darjatmoko S.R., Lindstrom M.J., Kulkarni A., Albert D.M., Polans A.S. Resveratrol Inhibits Tumor Growth of Human Neuroblastoma and Mediates Apoptosis by Directly Targeting Mitochondria. Clin. Cancer Res. 2007;13:5162-5169.

    Not in our library10.1158/1078-0432.ccr-07-0347

  128. 128.

    Dai H., Deng H.-B., Wang Y.-H., Guo J.-J. Resveratrol inhibits the growth of gastric cancer via the Wnt/β-catenin pathway. Oncol. Lett. 2018;16:1579-1583.

    Not in our library10.3892/ol.2018.8772

  129. 129.

    Kleszcz R., Paluszczak J., Krajka-Kuźniak V., Baer-Dubowska W. The inhibition of c-MYC transcription factor modulates the expression of glycolytic and glutaminolytic enzymes in FaDu hypopharyngeal carcinoma cells. Adv. Clin. Exp. Med. 2018;27:735-742.

    Not in our library10.17219/acem/68979

  130. 130.

    Puissant A., Auberger P. AMPK- and p62/SQSTM1-dependent autophagy mediate Resveratrol-induced cell death in chronic myelogenous leukemia. Autophagy. 2010;6:655-657.

    Not in our library10.4161/auto.6.5.12126

  131. 131.

    Puissant A., Robert G., Fenouille N., Luciano F., Cassuto J.-P., Raynaud S., Auberger P. Resveratrol Promotes Autophagic Cell Death in Chronic Myelogenous Leukemia Cells via JNK-Mediated p62/SQSTM1 Expression and AMPK Activation. Cancer Res. 2010;70:1042-1052.

    Not in our library10.1158/0008-5472.can-09-3537

  132. 132.

    Zhang Y., Tian F., Xiao Q., Hu Y., Li J., Jiang F., Liu Y. Exploiting the Role of Resveratrol in Rat Mitochondrial Permeability Transition. J. Membr. Biol. 2013;246:365-373.

    Not in our library10.1007/s00232-013-9540-0

  133. 133.

    Song J., Yang B., Jia X., Li M., Tan W., Ma S., Shi X., Feng L. Distinctive Roles of Sirtuins on Diabetes, Protective or Detrimental? Front. Endocrinol. 2018;9:724.

    Not in our library10.3389/fendo.2018.00724

  134. 134.

    Zhong L., Mostoslavsky R. SIRT6: A master epigenetic gatekeeper of glucose metabolism. Transcription. 2010;1:17-21.

    Not in our library10.4161/trns.1.1.12143

  135. 135.

    Dembic M., Andersen H.S., Bastin J., Doktor T.K., Corydon T.J., Sass J.O., Costa A.L., Djouadi F., Andresen B.S. Next generation sequencing of RNA reveals novel targets of resveratrol with possible implications for Canavan disease. Mol. Genet. Metab. 2019;126:64-76.

    Not in our library10.1016/j.ymgme.2018.10.004

  136. 136.
    The expression of Sirtuins 1 and 4 in peripheral blood leukocytes from patients with type 2 diabetes · 2011
    Not checked
  137. 137.
    Neuroprotective Mechanisms of Resveratrol in Alzheimer’s Disease: Role of SIRT1 · 2018
    No notice
  138. 138.

    Palsamy P., Subramanian S. Resveratrol, a natural phytoalexin, normalizes hyperglycemia in streptozotocin-nicotinamide induced experimental diabetic rats. Biomed. Pharmacother. 2008;62:598-605.

    Not in our library10.1016/j.biopha.2008.06.037

  139. 139.

    Palsamy P., Subramanian S. Modulatory effects of resveratrol on attenuating the key enzymes activities of carbohydrate metabolism in streptozotocin–nicotinamide-induced diabetic rats. Chem. Biol. Interact. 2009;179:356-362.

    Not in our library10.1016/j.cbi.2008.11.008

  140. 140.

    Iqbal M.A., Gupta V., Gopinath P., Mazurek S., Bamezai R.N.K. Pyruvate kinase M2 and cancer: An updated assessment. FEBS Lett. 2014;588:2685-2692.

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

  141. 141.

    Zhao H., Han L., Jian Y., Ma Y., Yan W., Chen X., Xu H., Li L. Resveratrol induces apoptosis in human melanoma cell through negatively regulating Erk/PKM2/Bcl-2 axis. Onco. Targets. Ther. 2018;11:8995-9006.

    Not in our library10.2147/ott.s186247

  142. 142.

    Christofk H.R., Vander Heiden M.G., Harris M.H., Ramanathan A., Gerszten R.E., Wei R., Fleming M.D., Schreiber S.L., Cantley L.C. The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth. Nature. 2008;452:230.

    Not in our library10.1038/nature06734

  143. 143.

    Wenner C.E. Cell signaling and cancer-possible targets for therapy. J. Cell. Physiol. 2010;223:299-308.

    Not in our library10.1002/jcp.22021

  144. 144.

    Tian M., Xie Y., Meng Y., Ma W., Tong Z., Yang X., Lai S., Zhou Y., He M., Liao Z. Resveratrol protects cardiomyocytes against anoxia/reoxygenation via dephosphorylation of VDAC1 by Akt-GSK3 β pathway. Eur. J. Pharmacol. 2019;843:80-87.

    Not in our library10.1016/j.ejphar.2018.11.016

  145. 145.

    Zhang D., Yip Y.M., Li L. In silico construction of HK2-VDAC1 complex and investigating the HK2 binding-induced molecular gating mechanism of VDAC1. Mitochondrion. 2016;30:222-228.

    Not in our library10.1016/j.mito.2016.08.009

  146. 146.

    Hu W.-H., Duan R., Xia Y.-T., Xiong Q.-P., Wang H.-Y., Chan G.K.-L., Liu S.-Y., Dong T.T.-X., Qin Q.-W., Tsim K.W.-K. Binding of Resveratrol to Vascular Endothelial Growth Factor Suppresses Angiogenesis by Inhibiting the Receptor Signaling. J. Agric. Food Chem. 2019;67:1127-1137.

    Not in our library10.1021/acs.jafc.8b05977

  147. 147.

    Gwak H., Haegeman G., Tsang B.K., Song Y.S. Cancer-specific interruption of glucose metabolism by resveratrol is mediated through inhibition of Akt/GLUT1 axis in ovarian cancer cells. Mol. Carcinog. 2015;54:1529-1540.

    Not in our library10.1002/mc.22227

  148. 148.

    Warnke I., Jocken J.W.E., Schoop R., Toepfer C., Goralczyk R., Schwager J. Combinations of bio-active dietary constituents affect human white adipocyte function in-vitro. Nutr. Metab. (Lond). 2016;13:84.

    Not in our library10.1186/s12986-016-0143-5

  149. 149.

    Wu H., He L., Shi J., Hou X., Zhang H., Zhang X., An Q., Fan F. Resveratrol inhibits VEGF-induced angiogenesis in human endothelial cells associated with suppression of aerobic glycolysis via modulation of PKM2 nuclear translocation. Clin. Exp. Pharmacol. Physiol. 2018;45:1265-1273.

    Not in our library10.1111/1440-1681.13017

  150. 150.

    Lappas M., Andrikopoulos S., Permezel M. Hypoxanthine–xanthine oxidase down-regulates GLUT1 transcription via SIRT1 resulting in decreased glucose uptake in human placenta. J. Endocrinol. 2012;213:49-57.

    Not in our library10.1530/joe-11-0355

  151. 151.

    Jung K.-H., Lee J.H., Quach C.H.T., Paik J.-Y., Oh H., Park J.W., Lee E.J., Moon S.-H., Lee K.-H. Resveratrol Suppresses Cancer Cell Glucose Uptake by Targeting Reactive Oxygen Species–Mediated Hypoxia-Inducible Factor-1α Activation. J. Nucl. Med. 2013;54:2161-2167.

    Not in our library10.2967/jnumed.112.115436

  152. 152.

    Vislovukh A., Kratassiouk G., Porto E., Gralievska N., Beldiman C., Pinna G., El’skaya A., Harel-Bellan A., Negrutskii B., Groisman I. Proto-oncogenic isoform A2 of eukaryotic translation elongation factor eEF1 is a target of miR-663 and miR-744. Br. J. Cancer. 2013;108:2304.

    Not in our library10.1038/bjc.2013.243

  153. 153.

    Yu Y.-H., Chen H.-A., Chen P.-S., Cheng Y.-J., Hsu W.-H., Chang Y.-W., Chen Y.-H., Jan Y., Hsiao M., Chang T.-Y., et al. MiR-520h-mediated FOXC2 regulation is critical for inhibition of lung cancer progression by resveratrol. Oncogene. 2012;32:431.

    Not in our library10.1038/onc.2012.74

  154. 154.

    Liu P., Liang H., Xia Q., Li P., Kong H., Lei P., Wang S., Tu Z. Resveratrol induces apoptosis of pancreatic cancers cells by inhibiting miR-21 regulation of BCL-2 expression. Clin. Transl. Oncol. 2013;15:741-746.

    Not in our library10.1007/s12094-012-0999-4

  155. 155.

    Tili E., Michaille J.-J., Alder H., Volinia S., Delmas D., Latruffe N., Croce C.M. Resveratrol modulates the levels of microRNAs targeting genes encoding tumor-suppressors and effectors of TGFβ signaling pathway in SW480 cells. Biochem. Pharmacol. 2010;80:2057-2065.

    Not in our library10.1016/j.bcp.2010.07.003

  156. 156.

    Kumazaki M., Noguchi S., Yasui Y., Iwasaki J., Shinohara H., Yamada N., Akao Y. Anti-cancer effects of naturally occurring compounds through modulation of signal transduction and miRNA expression in human colon cancer cells. J. Nutr. Biochem. 2013;24:1849-1858.

    Not in our library10.1016/j.jnutbio.2013.04.006

  157. 157.

    Pandima Devi K., Rajavel T., Daglia M., Nabavi S.F., Bishayee A., Nabavi S.M. Targeting miRNAs by polyphenols: Novel therapeutic strategy for cancer. Semin. Cancer Biol. 2017;46:146-157.

    Not in our library10.1016/j.semcancer.2017.02.001

  158. 158.

    Dhar S., Hicks C., Levenson A.S. Resveratrol and prostate cancer: Promising role for microRNAs. Mol. Nutr. Food Res. 2011;55:1219-1229.

    Not in our library10.1002/mnfr.201100141

  159. 159.

    Otsuka K., Yamamoto Y., Ochiya T. Regulatory role of resveratrol, a microRNA-controlling compound, in HNRNPA1 expression, which is associated with poor prognosis in breast cancer. Oncotarget. 2018;9:24718-24730.

    Not in our library10.18632/oncotarget.25339

  160. 160.
    Resveratrol Reduces Prostate Cancer Growth and Metastasis by Inhibiting the Akt/MicroRNA-21 Pathway · 2012
    No notice
  161. 161.

    Yang S.-F., Lee W.-J., Tan P., Tang C.-H., Hsiao M., Hsieh F.-K., Chien M.-H. Upregulation of miR-328 and inhibition of CREB-DNA-binding activity are critical for resveratrol-mediated suppression of matrix metalloproteinase-2 and subsequent metastatic ability in human osteosarcomas. Oncotarget. 2014;6:2736-2753.

    Not in our library10.18632/oncotarget.3088

  162. 162.

    Zhao J., Chen Y., Liu F., Yin M. Overexpression of miRNA-143 Inhibits Colon Cancer Cell Proliferation by Inhibiting Glucose Uptake. Arch. Med. Res. 2018;49:497-503.

    Not in our library10.1016/j.arcmed.2018.12.009

  163. 163.

    Esteves J.V., Enguita F.J., Machado U.F. MicroRNAs-Mediated Regulation of Skeletal Muscle GLUT4 Expression and Translocation in Insulin Resistance. J. Diabetes Res. 2017;2017:7267910.

    Not in our library10.1155/2017/7267910

  164. 164.

    Wu H., Wang Y., Wu C., Yang P., Li H., Li Z. Resveratrol Induces Cancer Cell Apoptosis through MiR-326/PKM2-Mediated ER Stress and Mitochondrial Fission. J. Agric. Food Chem. 2016;64:9356-9367.

    Not in our library10.1021/acs.jafc.6b04549

  165. 165.

    Zhou X., Zuo S., Xin W. miR-27b overexpression improves mitochondrial function in a Sirt1-dependent manner. J. Physiol. Biochem. 2015;71:753-762.

    Not in our library10.1007/s13105-015-0439-3

  166. 166.

    Tan L., Wang W., He G., Kuick R.D., Gossner G., Kueck A.S., Wahl H., Opipari A.W., Liu J.R. Resveratrol inhibits ovarian tumor growth in an in vivo mouse model. Cancer. 2016;122:722-729.

    Not in our library10.1002/cncr.29793

  167. 167.

    Breen D.M., Sanli T., Giacca A., Tsiani E. Stimulation of muscle cell glucose uptake by resveratrol through sirtuins and AMPK. Biochem. Biophys. Res. Commun. 2008;374:117-122.

    Not in our library10.1016/j.bbrc.2008.06.104

  168. 168.

    Araújo J.R., Pereira A.C., Correia-Branco A., Keating E., Martel F. Oxidative stress induced by tert-butylhydroperoxide interferes with the placental transport of glucose: In vitro studies with BeWo cells. Eur. J. Pharmacol. 2013;720:218-226.

    Not in our library10.1016/j.ejphar.2013.10.023

  169. 169.

    Zhao Y., Butler E.B., Tan M. Targeting cellular metabolism to improve cancer therapeutics. Cell Death Dis. 2013;4:e532.

    Not in our library10.1038/cddis.2013.60

  170. 170.

    Afzal I., Cunningham P., Naftalin R.J. Interactions of ATP, oestradiol, genistein and the anti-oestrogens, faslodex (ICI 182780) and tamoxifen, with the human erythrocyte glucose transporter, GLUT1. Biochem. J. 2002;365:707-719.

    Not in our library10.1042/bj20011624

  171. 171.

    Pérez A., Ojeda P., Ojeda L., Salas M., Rivas C.I., Vera J.C., Reyes A.M. Hexose Transporter GLUT1 Harbors Several Distinct Regulatory Binding Sites for Flavones and Tyrphostins. Biochemistry. 2011;50:8834-8845.

    Not in our library10.1021/bi200748b

  172. 172.

    Leon D., Parada D., Vargas-Uribe M., Perez A.A., Ojeda L., Zambrano A., Reyes A.M., Salas M. Effect of nordihydroguaiaretic acid on cell viability and glucose transport in human leukemic cell lines. FEBS Open Bio. 2016;6:1000-1007.

    Not in our library10.1002/2211-5463.12106

  173. 173.

    Pérez A., Ojeda P., Valenzuela X., Ortega M., Sánchez C., Ojeda L., Castro M., Cárcamo J.G., Rauch M.C., Concha I.I., et al. Endofacial competitive inhibition of the glucose transporter 1 activity by gossypol. Am. J. Physiol. Physiol. 2009;297:C86-C93.

    Not in our library10.1152/ajpcell.00501.2008

  174. 174.

    Azevedo C., Correia-Branco A., Araújo J.R., Guimarães J.T., Keating E., Martel F. The Chemopreventive Effect of the Dietary Compound Kaempferol on the MCF-7 Human Breast Cancer Cell Line Is Dependent on Inhibition of Glucose Cellular Uptake. Nutr. Cancer. 2015;67:504-513.

    Not in our library10.1080/01635581.2015.1002625

  175. 175.

    Gunnink L.K., Alabi O.D., Kuiper B.D., Gunnink S.M., Schuiteman S.J., Strohbehn L.E., Hamilton K.E., Wrobel K.E., Louters L.L. Curcumin directly inhibits the transport activity of GLUT1. Biochimie. 2016;125:179-185.

    Not in our library10.1016/j.biochi.2016.03.014

  176. 176.

    León D., Uribe E., Zambrano A., Salas M. Implications of resveratrol on glucose uptake and metabolism. Molecules. 2017;22:398.

    Not in our library10.3390/molecules22030398

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