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<PubmedArticle><MedlineCitation Status="MEDLINE" Owner="NLM" IndexingMethod="Automated"><PMID Version="1">35955833</PMID><DateCompleted><Year>2022</Year><Month>08</Month><Day>15</Day></DateCompleted><DateRevised><Year>2025</Year><Month>07</Month><Day>28</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1422-0067</ISSN><JournalIssue CitedMedium="Internet"><Volume>23</Volume><Issue>15</Issue><PubDate><Year>2022</Year><Month>Aug</Month><Day>04</Day></PubDate></JournalIssue><Title>International journal of molecular sciences</Title><ISOAbbreviation>Int J Mol Sci</ISOAbbreviation></Journal><ArticleTitle>Importance of GLUT Transporters in Disease Diagnosis and Treatment.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">8698</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.3390/ijms23158698</ELocationID><Abstract><AbstractText>Facilitative sugar transporters (GLUTs) are the primary method of sugar uptake in all mammalian cells. There are 14 different types of those transmembrane proteins, but they transport only a handful of substrates, mainly glucose and fructose. This overlap and redundancy contradict the natural tendency of cells to conserve energy and resources, and has led researchers to hypothesize that different GLUTs partake in more metabolic roles than just sugar transport into cells. Understanding those roles will lead to better therapeutics for a wide variety of diseases and disorders. In this review we highlight recent discoveries of the role GLUTs play in different diseases and disease treatments.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ismail</LastName><ForeName>Abdelrahman</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Michigan Technological University, 1400 Townsend Drive, Houghton, MI 49931, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tanasova</LastName><ForeName>Marina</ForeName><Initials>M</Initials><Identifier Source="ORCID">0000-0003-4771-9533</Identifier><AffiliationInfo><Affiliation>Department of Chemistry, Michigan Technological University, 1400 Townsend Drive, Houghton, MI 49931, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Health Research Institute, Michigan Technological University, Houghton, MI 49931, USA.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R15 CA242401</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GRANT12736422</GrantID><Acronym>NH</Acronym><Agency>NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2022</Year><Month>08</Month><Day>04</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Int J Mol Sci</MedlineTA><NlmUniqueID>101092791</NlmUniqueID><ISSNLinking>1422-0067</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051246">Glucose Transport Proteins, Facilitative</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D026901">Membrane Transport Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>30237-26-4</RegistryNumber><NameOfSubstance UI="D005632">Fructose</NameOfSubstance></Chemical><Chemical><RegistryNumber>IY9XDZ35W2</RegistryNumber><NameOfSubstance UI="D005947">Glucose</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001692" MajorTopicYN="N">Biological Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005632" MajorTopicYN="N">Fructose</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005947" MajorTopicYN="N">Glucose</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051246" MajorTopicYN="Y">Glucose Transport Proteins, Facilitative</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008322" MajorTopicYN="N">Mammals</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D026901" MajorTopicYN="Y">Membrane Transport Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">GLUT inhibitors</Keyword><Keyword MajorTopicYN="N">GLUT therapeutics</Keyword><Keyword MajorTopicYN="N">GLUTs</Keyword><Keyword MajorTopicYN="N">diagnostic biomarkers</Keyword><Keyword MajorTopicYN="N">metabolic diseases</Keyword><Keyword MajorTopicYN="N">sugar transport</Keyword></KeywordList><CoiStatement>The authors declare no conflict of interest.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2022</Year><Month>7</Month><Day>2</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2022</Year><Month>7</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2022</Year><Month>7</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2022</Year><Month>8</Month><Day>12</Day><Hour>1</Hour><Minute>13</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2022</Year><Month>8</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2022</Year><Month>8</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pmc-release"><Year>2022</Year><Month>8</Month><Day>4</Day></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">35955833</ArticleId><ArticleId IdType="pmc">PMC9368955</ArticleId><ArticleId IdType="doi">10.3390/ijms23158698</ArticleId><ArticleId IdType="pii">ijms23158698</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Reckzeh E.S., Waldmann H. Development of Glucose Transporter (GLUT) Inhibitors. Eur. J. Org. Chem. 2020;2020:2321&#x2013;2329. doi: 10.1002/ejoc.201901353.</Citation><ArticleIdList><ArticleId IdType="doi">10.1002/ejoc.201901353</ArticleId><ArticleId IdType="pmc">PMC7217229</ArticleId><ArticleId IdType="pubmed">32421048</ArticleId></ArticleIdList></Reference><Reference><Citation>Boado R.J., Pardridge W.M. The Brain-Type Glucose Transporter Messenger-Rna Is Specifically Expressed at the Blood-Brain-Barrier. Biochem. Bioph. Res. Commun. 1990;166:174&#x2013;179. doi: 10.1016/0006-291X(90)91927-K.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/0006-291X(90)91927-K</ArticleId><ArticleId IdType="pubmed">2302200</ArticleId></ArticleIdList></Reference><Reference><Citation>Pardridge W.M., Boado R.J., Farrell C.R. Brain-Type Glucose Transporter (Glut-1) Is Selectively Localized to the Blood-Brain-Barrier&#x2014;Studies with Quantitative Western Blotting and Insitu Hybridization. J. Biol. Chem. 1990;265:18035&#x2013;18040. doi: 10.1016/S0021-9258(18)38267-X.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/S0021-9258(18)38267-X</ArticleId><ArticleId IdType="pubmed">2211679</ArticleId></ArticleIdList></Reference><Reference><Citation>Farrell C.L., Yang J., Pardridge W.M. GLUT-1 glucose transporter is present within apical and basolateral membranes of brain epithelial interfaces and in microvascular endothelia with and without tight junctions. J. Histochem. Cytochem. 1992;40:193&#x2013;199. doi: 10.1177/40.2.1552163.</Citation><ArticleIdList><ArticleId IdType="doi">10.1177/40.2.1552163</ArticleId><ArticleId IdType="pubmed">1552163</ArticleId></ArticleIdList></Reference><Reference><Citation>Nishimura H., Pallardo F.V., Seidner G.A., Vannucci S., Simpson I.A., Birnbaum M.J. Kinetics of Glut1 and Glut4 Glucose Transporters Expressed in Xenopus Oocytes. J. Biol. Chem. 1993;268:8514&#x2013;8520. doi: 10.1016/S0021-9258(18)52905-7.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/S0021-9258(18)52905-7</ArticleId><ArticleId IdType="pubmed">8473295</ArticleId></ArticleIdList></Reference><Reference><Citation>Uldry M., Ibberson M., Hosokawa M., Thorens B. GLUT2 is a high affinity glucosamine transporter. FEBS Lett. 2002;524:199&#x2013;203. doi: 10.1016/S0014-5793(02)03058-2.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/S0014-5793(02)03058-2</ArticleId><ArticleId IdType="pubmed">12135767</ArticleId></ArticleIdList></Reference><Reference><Citation>Nishioka T., Oda Y., Seino Y., Yamamoto T., Inagaki N., Yano H., Imura H., Shigemoto R., Kikuchi H. Distribution of the glucose transporters in human brain tumors. Cancer Res. 1992;52:3972&#x2013;3979.</Citation><ArticleIdList><ArticleId IdType="pubmed">1617673</ArticleId></ArticleIdList></Reference><Reference><Citation>Krzeslak A., Wojcik-Krowiranda K., Forma E., Jozwiak P., Romanowicz H., Bienkiewicz A., Brys M. Expression of GLUT1 and GLUT3 glucose transporters in endometrial and breast cancers. Pathol. Oncol. Res. POR. 2012;18:721&#x2013;728. doi: 10.1007/s12253-012-9500-5.</Citation><ArticleIdList><ArticleId IdType="doi">10.1007/s12253-012-9500-5</ArticleId><ArticleId IdType="pmc">PMC3342495</ArticleId><ArticleId IdType="pubmed">22270867</ArticleId></ArticleIdList></Reference><Reference><Citation>Kim B.W., Cho H., Chung J.Y., Conway C., Ylaya K., Kim J.H., Hewitt S.M. Prognostic assessment of hypoxia and metabolic markers in cervical cancer using automated digital image analysis of immunohistochemistry. J. Transl. Med. 2013;11:185. doi: 10.1186/1479-5876-11-185.</Citation><ArticleIdList><ArticleId IdType="doi">10.1186/1479-5876-11-185</ArticleId><ArticleId IdType="pmc">PMC3750663</ArticleId><ArticleId IdType="pubmed">23927384</ArticleId></ArticleIdList></Reference><Reference><Citation>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: A marker for poor prognosis. Cancer. 1998;83:34&#x2013;40. doi: 10.1002/(SICI)1097-0142(19980701)83:1&lt;34::AID-CNCR5&gt;3.0.CO;2-E.</Citation><ArticleIdList><ArticleId IdType="doi">10.1002/(SICI)1097-0142(19980701)83:1&lt;34::AID-CNCR5&gt;3.0.CO;2-E</ArticleId><ArticleId IdType="pubmed">9655290</ArticleId></ArticleIdList></Reference><Reference><Citation>Nagase Y., Takata K., Moriyama N., Aso Y., Murakami T., Hirano H. Immunohistochemical localization of glucose transporters in human renal cell carcinoma. J. Urol. 1995;153:798&#x2013;801. doi: 10.1016/S0022-5347(01)67725-5.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/S0022-5347(01)67725-5</ArticleId><ArticleId IdType="pubmed">7861542</ArticleId></ArticleIdList></Reference><Reference><Citation>Younes M., Brown R.W., Stephenson M., Gondo M., Cagle P.T. Overexpression of Glut1 and Glut3 in stage I nonsmall cell lung carcinoma is associated with poor survival. Cancer. 1997;80:1046&#x2013;1051. doi: 10.1002/(SICI)1097-0142(19970915)80:6&lt;1046::AID-CNCR6&gt;3.0.CO;2-7.</Citation><ArticleIdList><ArticleId IdType="doi">10.1002/(SICI)1097-0142(19970915)80:6&lt;1046::AID-CNCR6&gt;3.0.CO;2-7</ArticleId><ArticleId IdType="pubmed">9305704</ArticleId></ArticleIdList></Reference><Reference><Citation>Cantuaria G., Fagotti A., Ferrandina G., Magalhaes A., Nadji M., Angioli R., Penalver M., Mancuso S., Scambia G. GLUT-1 expression in ovarian carcinoma: Association with survival and response to chemotherapy. Cancer. 2001;92:1144&#x2013;1150. doi: 10.1002/1097-0142(20010901)92:5&lt;1144::AID-CNCR1432&gt;3.0.CO;2-T.</Citation><ArticleIdList><ArticleId IdType="doi">10.1002/1097-0142(20010901)92:5&lt;1144::AID-CNCR1432&gt;3.0.CO;2-T</ArticleId><ArticleId IdType="pubmed">11571727</ArticleId></ArticleIdList></Reference><Reference><Citation>Stewart G.D., Gray K., Pennington C.J., Edwards D.R., Riddick A.C., Ross J.A., Habib F.K. Analysis of hypoxia-associated gene expression in prostate cancer: Lysyl oxidase and glucose transporter-1 expression correlate with Gleason score. Oncol. Rep. 2008;20:1561&#x2013;1567. doi: 10.3892/or_00000180.</Citation><ArticleIdList><ArticleId IdType="doi">10.3892/or_00000180</ArticleId><ArticleId IdType="pubmed">19020742</ArticleId></ArticleIdList></Reference><Reference><Citation>Baer S.C., Casaubon L., Younes M. Expression of the human erythrocyte glucose transporter Glut1 in cutaneous neoplasia. J. Am. Acad. Dermatol. 1997;37:575&#x2013;577. doi: 10.1016/S0190-9622(97)70174-9.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/S0190-9622(97)70174-9</ArticleId><ArticleId IdType="pubmed">9344196</ArticleId></ArticleIdList></Reference><Reference><Citation>Haber R.S., Weiser K.R., Pritsker A., Reder I., Burstein D.E. GLUT1 glucose transporter expression in benign and malignant thyroid nodules. Thyroid Off. J. Am. Thyroid Assoc. 1997;7:363&#x2013;367. doi: 10.1089/thy.1997.7.363.</Citation><ArticleIdList><ArticleId IdType="doi">10.1089/thy.1997.7.363</ArticleId><ArticleId IdType="pubmed">9226204</ArticleId></ArticleIdList></Reference><Reference><Citation>Grover-McKay M., Walsh S.A., Seftor E.A., Thomas P.A., Hendrix M.J. Role for glucose transporter 1 protein in human breast cancer. Pathol. Oncol. Res. POR. 1998;4:115&#x2013;120. doi: 10.1007/BF02904704.</Citation><ArticleIdList><ArticleId IdType="doi">10.1007/BF02904704</ArticleId><ArticleId IdType="pubmed">9654596</ArticleId></ArticleIdList></Reference><Reference><Citation>Oran Kwon P.E., Chen S., Corpe C., Lee J.H., Kruhlak M., Levine M. Inhibition of the intestinal glucose transporter GLUT2 by flavonoids. FASEB J. 2007;21:366&#x2013;377. doi: 10.1096/fj.06-6620com.</Citation><ArticleIdList><ArticleId IdType="doi">10.1096/fj.06-6620com</ArticleId><ArticleId IdType="pubmed">17172639</ArticleId></ArticleIdList></Reference><Reference><Citation>Michele Skopec A.G., Karasov W. Flavonoids have differential effects on the glucose absorption in rats and american robins. J. Chem. Ecol. 2010;36:236&#x2013;243. doi: 10.1007/s10886-010-9747-9.</Citation><ArticleIdList><ArticleId IdType="doi">10.1007/s10886-010-9747-9</ArticleId><ArticleId IdType="pubmed">20145981</ArticleId></ArticleIdList></Reference><Reference><Citation>Cheeseman C.I. Glut2 Is the Transporter for Fructose across the Rat Intestinal Basolateral Membrane. Gastroenterology. 1993;105:1050&#x2013;1056. doi: 10.1016/0016-5085(93)90948-C.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/0016-5085(93)90948-C</ArticleId><ArticleId IdType="pubmed">8405848</ArticleId></ArticleIdList></Reference><Reference><Citation>Johnson J.H., Newgard C.B., Milburn J.L., Lodish H.F., Thorens B. The High Km Glucose Transporter of Islets of Langerhans Is Functionally Similar to the Low Affinity Transporter of Liver and Has an Identical Primary Sequence. J. Biol. Chem. 1990;265:6548&#x2013;6551. doi: 10.1016/S0021-9258(19)39181-1.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/S0021-9258(19)39181-1</ArticleId><ArticleId IdType="pubmed">2182619</ArticleId></ArticleIdList></Reference><Reference><Citation>Colville C.A., Seatter M.J., Jess T.J., Gould G.W., Thomas H.M. Kinetic-Analysis of the Liver-Type (Glut2) and Brain-Type (Glut3) Glucose Transporters in Xenopus Oocytes&#x2014;Substrate Specificities and Effects of Transport Inhibitors. Biochem. J. 1993;290:701&#x2013;706. doi: 10.1042/bj2900701.</Citation><ArticleIdList><ArticleId IdType="doi">10.1042/bj2900701</ArticleId><ArticleId IdType="pmc">PMC1132337</ArticleId><ArticleId IdType="pubmed">8457197</ArticleId></ArticleIdList></Reference><Reference><Citation>Goto T., Horita M., Nagai H., Nagatomo A., Nishida N., Matsuura Y., Nagaoka S. Tiliroside, a glycosidic flavonoid, inhibits carbohydrate digestion and glucose absorption in the gastrointestinal tract. Mol. Nutr. Food Res. 2012;56:435&#x2013;445. doi: 10.1002/mnfr.201100458.</Citation><ArticleIdList><ArticleId IdType="doi">10.1002/mnfr.201100458</ArticleId><ArticleId IdType="pubmed">22173993</ArticleId></ArticleIdList></Reference><Reference><Citation>Maher F., Davies-Hill T.M., Lysko P.G., Henneberry R.C., Simpson I.A. Expression of two glucose transporters, GLUT1 and GLUT3, in cultured cerebellar neurons: Evidence for neuron-specific expression of GLUT3. Mol. Cell. Neurosci. 1991;2:351&#x2013;360. doi: 10.1016/1044-7431(91)90066-W.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/1044-7431(91)90066-W</ArticleId><ArticleId IdType="pubmed">19912819</ArticleId></ArticleIdList></Reference><Reference><Citation>Zeller K., Duelli R., Vogel J., Schrock H., Kuschinsky W. Autoradiographic Analysis of the Regional Distribution of Glut3 Glucose Transporters in the Rat-Brain. Brain Res. 1995;698:175&#x2013;179. doi: 10.1016/0006-8993(95)00888-W.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/0006-8993(95)00888-W</ArticleId><ArticleId IdType="pubmed">8581478</ArticleId></ArticleIdList></Reference><Reference><Citation>Mccall A.L., Vanbueren A.M., Moholtsiebert M., Cherry N.J., Woodward W.R. Immunohistochemical Localization of the Neuron-Specific Glucose-Transporter (Glut3) to Neuropil in Adult-Rat Brain. Brain Res. 1994;659:292&#x2013;297. doi: 10.1016/0006-8993(94)90896-6.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/0006-8993(94)90896-6</ArticleId><ArticleId IdType="pubmed">7820678</ArticleId></ArticleIdList></Reference><Reference><Citation>Simpson I.A., Dwyer D., Malide D., Moley K.H., Travis A., Vannucci S.J. The facilitative glucose transporter GLUT3: 20 years of distinction. Am. J. Physiol. Endocrinol. Metab. 2008;295:E242&#x2013;E253. doi: 10.1152/ajpendo.90388.2008.</Citation><ArticleIdList><ArticleId IdType="doi">10.1152/ajpendo.90388.2008</ArticleId><ArticleId IdType="pmc">PMC2519757</ArticleId><ArticleId IdType="pubmed">18577699</ArticleId></ArticleIdList></Reference><Reference><Citation>Arbuckle M.I., Kane S., Porter L.M., Seatter M.J., Gould G.W. Structure-function analysis of liver-type (GLUT2) and brain-type (GLUT3) glucose transporters: Expression of chimeric transporters in Xenopus oocytes suggests an important role for putative transmembrane helix 7 in determining substrate selectivity. Biochemistry. 1996;35:16519&#x2013;16527. doi: 10.1021/bi962210n.</Citation><ArticleIdList><ArticleId IdType="doi">10.1021/bi962210n</ArticleId><ArticleId IdType="pubmed">8987985</ArticleId></ArticleIdList></Reference><Reference><Citation>Masin M., Vazquez J., Rossi S., Groeneveld S., Samson N., Schwalie P.C., Deplancke B., Frawley L.E., Gouttenoire J., Moradpour D., et al. GLUT3 is induced during epithelial-mesenchymal transition and promotes tumor cell proliferation in non-small cell lung cancer. Cancer Metab. 2014;2:11. doi: 10.1186/2049-3002-2-11.</Citation><ArticleIdList><ArticleId IdType="doi">10.1186/2049-3002-2-11</ArticleId><ArticleId IdType="pmc">PMC4122054</ArticleId><ArticleId IdType="pubmed">25097756</ArticleId></ArticleIdList></Reference><Reference><Citation>Baer S., Casaubon L., Schwartz M.R., Marcogliese A., Younes M. Glut3 expression in biopsy specimens of laryngeal carcinoma is associated with poor survival. Laryngoscope. 2002;112:393&#x2013;396. doi: 10.1097/00005537-200202000-00034.</Citation><ArticleIdList><ArticleId IdType="doi">10.1097/00005537-200202000-00034</ArticleId><ArticleId IdType="pubmed">11889403</ArticleId></ArticleIdList></Reference><Reference><Citation>Flavahan W.A., Wu Q.L., Hitomi M., Rahim N., Kim Y., Sloan A.E., Weil R.J., Nakano I., Sarkaria J.N., Stringer B.W., et al. Brain tumor initiating cells adapt to restricted nutrition through preferential glucose uptake. Nat. Neurosci. 2013;16:1373&#x2013;1382. doi: 10.1038/nn.3510.</Citation><ArticleIdList><ArticleId IdType="doi">10.1038/nn.3510</ArticleId><ArticleId IdType="pmc">PMC3930177</ArticleId><ArticleId IdType="pubmed">23995067</ArticleId></ArticleIdList></Reference><Reference><Citation>Bell G.I., Murray J.C., Nakamura Y., Kayano T., Eddy R.L., Fan Y.S., Byers M.G., Shows T.B. Polymorphic human insulin-responsive glucose-transporter gene on chromosome 17p13. Diabetes. 1989;38:1072&#x2013;1075. doi: 10.2337/diab.38.8.1072.</Citation><ArticleIdList><ArticleId IdType="doi">10.2337/diab.38.8.1072</ArticleId><ArticleId IdType="pubmed">2568955</ArticleId></ArticleIdList></Reference><Reference><Citation>Huang S.H., Czech M.P. The GLUT4 glucose transporter. Cell Metab. 2007;5:237&#x2013;252. doi: 10.1016/j.cmet.2007.03.006.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/j.cmet.2007.03.006</ArticleId><ArticleId IdType="pubmed">17403369</ArticleId></ArticleIdList></Reference><Reference><Citation>Burant C.F., Bell G.I. Mammalian Facilitative Glucose Transporters&#x2014;Evidence for Similar Substrate Recognition Sites in Functionally Monomeric Proteins. Biochemistry. 1992;31:10414&#x2013;10420. doi: 10.1021/bi00157a032.</Citation><ArticleIdList><ArticleId IdType="doi">10.1021/bi00157a032</ArticleId><ArticleId IdType="pubmed">1420159</ArticleId></ArticleIdList></Reference><Reference><Citation>Gupta P., Kanwal A., Putcha U.K., Bulani Y., Sojitra B., Khatua T.N., Kuncha M., Banerjee S.K. Cardioprotective effect of ritonavir, an antiviral drug, in isoproterenol induced myocardial necrosis: A new therapeutic implication. J. Transl. Med. 2013;11:80. doi: 10.1186/1479-5876-11-80.</Citation><ArticleIdList><ArticleId IdType="doi">10.1186/1479-5876-11-80</ArticleId><ArticleId IdType="pmc">PMC3623744</ArticleId><ArticleId IdType="pubmed">23531330</ArticleId></ArticleIdList></Reference><Reference><Citation>Kouidhi S., Berrhouma R., Rouissi K., Jarboui S., Clerget-Froidevaux M.S., Seugnet I., Bchir F., Demeneix B., Guissouma H., Elgaaied A.B. Human subcutaneous adipose tissue Glut 4 mRNA expression in obesity and type 2 diabetes. Acta Diabetol. 2013;50:227&#x2013;232. doi: 10.1007/s00592-011-0295-8.</Citation><ArticleIdList><ArticleId IdType="doi">10.1007/s00592-011-0295-8</ArticleId><ArticleId IdType="pubmed">21604201</ArticleId></ArticleIdList></Reference><Reference><Citation>Wu X.H., Freeze H.H. GLUT14, a duplicon of GLUT3, is specifically expressed in testis as alternative splice forms. Genomics. 2002;80:553&#x2013;557. doi: 10.1006/geno.2002.7010.</Citation><ArticleIdList><ArticleId IdType="doi">10.1006/geno.2002.7010</ArticleId><ArticleId IdType="pubmed">12504846</ArticleId></ArticleIdList></Reference><Reference><Citation>Welch R.D., Gorski J. Regulation of glucose transporters by estradiol in the immature rat uterus. Endocrinology. 1999;140:3602&#x2013;3608. doi: 10.1210/endo.140.8.6923.</Citation><ArticleIdList><ArticleId IdType="doi">10.1210/endo.140.8.6923</ArticleId><ArticleId IdType="pubmed">10433217</ArticleId></ArticleIdList></Reference><Reference><Citation>von Wolff M., Ursel S., Hahn U., Steldinger R., Strowitzki T. Glucose transporter proteins (GLUT) in human endometrium: Expression, regulation, and function throughout the menstrual cycle and in early pregnancy. J. Clin. Endocr. Metab. 2003;88:3885&#x2013;3892. doi: 10.1210/jc.2002-021890.</Citation><ArticleIdList><ArticleId IdType="doi">10.1210/jc.2002-021890</ArticleId><ArticleId IdType="pubmed">12915684</ArticleId></ArticleIdList></Reference><Reference><Citation>Inukai K., Katagiri H., Takata K., Asano T., Anai M., Ishihara H., Nakazaki M., Kikuchi M., Yazaki Y., Oka Y. Characterization of Rat Glut5 and Functional-Analysis of Chimeric Proteins of Glut1 Glucose-Transporter and Glut5 Fructose Transporter. Endocrinology. 1995;136:4850&#x2013;4857. doi: 10.1210/endo.136.11.7588216.</Citation><ArticleIdList><ArticleId IdType="doi">10.1210/endo.136.11.7588216</ArticleId><ArticleId IdType="pubmed">7588216</ArticleId></ArticleIdList></Reference><Reference><Citation>Burant C.F., Takeda J., Brotlaroche E., Bell G.I., Davidson N.O. Fructose Transporter in Human Spermatozoa and Small-Intestine Is Glut5. J. Biol. Chem. 1992;267:14523&#x2013;14526. doi: 10.1016/S0021-9258(18)42067-4.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/S0021-9258(18)42067-4</ArticleId><ArticleId IdType="pubmed">1634504</ArticleId></ArticleIdList></Reference><Reference><Citation>McQuade D.T., Plutschack M.B., Seeberger P.H. Passive fructose transporters in disease: A molecular overview of their structural specificity. Org. Biomol. Chem. 2013;11:4909&#x2013;4920. doi: 10.1039/c3ob40805a.</Citation><ArticleIdList><ArticleId IdType="doi">10.1039/c3ob40805a</ArticleId><ArticleId IdType="pubmed">23784005</ArticleId></ArticleIdList></Reference><Reference><Citation>Tatibouet A., Yang J., Morin C., Holman G.D. Synthesis and evaluation of fructose analogues as inhibitors of the D-fructose transporter GLUT5. Bioorganic Med. Chem. 2000;8:1825&#x2013;1833. doi: 10.1016/S0968-0896(00)00108-5.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/S0968-0896(00)00108-5</ArticleId><ArticleId IdType="pubmed">10976531</ArticleId></ArticleIdList></Reference><Reference><Citation>Yang J., Tatibouet A., Hatanaka Y., Holman G.D. Fructose analogues with enhanced affinity for GLUT5. Diabetes. 2001;50:A277.</Citation></Reference><Reference><Citation>Yang J., Dowden J., Tatibouet A., Hatanaka Y., Holman G.D. Development of high-affinity ligands and photoaffinity labels for the D-fructose transporter GLUT5. Biochem. J. 2002;367:533&#x2013;539. doi: 10.1042/bj20020843.</Citation><ArticleIdList><ArticleId IdType="doi">10.1042/bj20020843</ArticleId><ArticleId IdType="pmc">PMC1222899</ArticleId><ArticleId IdType="pubmed">12119043</ArticleId></ArticleIdList></Reference><Reference><Citation>Tanasova M., Fedie J. Molecular Tools for Facilitative Carbohydrate Transporters. ChemBioChem. 2017;18:1774&#x2013;1788. doi: 10.1002/cbic.201700221.</Citation><ArticleIdList><ArticleId IdType="doi">10.1002/cbic.201700221</ArticleId><ArticleId IdType="pubmed">28636761</ArticleId></ArticleIdList></Reference><Reference><Citation>Li Q., Manolescu A., Ritzel M., Yao S., Slugoski M., Young J.D., Chen X.Z., Cheeseman C.I. Cloning and functional characterization of the human GLUT7 isoform SLC2A7 from the small intestine. Am. J. Physiol. Gastrointestin. Liver Physiol. 2004;287:G236&#x2013;G242. doi: 10.1152/ajpgi.00396.2003.</Citation><ArticleIdList><ArticleId IdType="doi">10.1152/ajpgi.00396.2003</ArticleId><ArticleId IdType="pubmed">15033637</ArticleId></ArticleIdList></Reference><Reference><Citation>Doege H., Bocianski A., Scheepers A., Axer H., Eckel J., Joost H.G., Schurmann A. Characterization of human glucose transporter (GLUT) 11 (encoded by SLC2A11), a novel sugar-transport facilitator specifically expressed in heart and skeletal muscle. Biochem. J. 2001;359:443&#x2013;449. doi: 10.1042/bj3590443.</Citation><ArticleIdList><ArticleId IdType="doi">10.1042/bj3590443</ArticleId><ArticleId IdType="pmc">PMC1222165</ArticleId><ArticleId IdType="pubmed">11583593</ArticleId></ArticleIdList></Reference><Reference><Citation>Augustin R., Carayannopoulos M.O., Dowd L.O., Phay J.E., Moley J.F., Moley K.H. Identification and characterization of human glucose transporter-like protein-9 (GLUT9)&#x2014;Alternative splicing alters trafficking. J. Biol. Chem. 2004;279:16229&#x2013;16236. doi: 10.1074/jbc.M312226200.</Citation><ArticleIdList><ArticleId IdType="doi">10.1074/jbc.M312226200</ArticleId><ArticleId IdType="pubmed">14739288</ArticleId></ArticleIdList></Reference><Reference><Citation>Scheepers A., Schmidt S., Manolescu A., Cheeseman C.I., Bell A., Zahn C., Joost H.G., Schurmann A. Characterization of the human SLC2A11 (GLUT11) gene: Alternative promoter usage, function, expression, and subcellular distribution of three isoforms, and lack of mouse orthologue. Mol. Membr. Biol. 2005;22:339&#x2013;351. doi: 10.1080/09687860500166143.</Citation><ArticleIdList><ArticleId IdType="doi">10.1080/09687860500166143</ArticleId><ArticleId IdType="pubmed">16154905</ArticleId></ArticleIdList></Reference><Reference><Citation>Ibberson M., Uldry M., Thorens B. GLUTX1, a novel mammalian glucose transporter expressed in the central nervous system and insulin-sensitive tissues. J. Biol. Chem. 2000;275:4607&#x2013;4612. doi: 10.1074/jbc.275.7.4607.</Citation><ArticleIdList><ArticleId IdType="doi">10.1074/jbc.275.7.4607</ArticleId><ArticleId IdType="pubmed">10671487</ArticleId></ArticleIdList></Reference><Reference><Citation>Rogers S., Macheda M.L., Docherty S.E., Carty M.D., Henderson M.A., Soeller W.C., Gibbs E.M., James D.E., Best J.D. Identification of a novel glucose transporter-like protein-GLUT-12. Am. J. Physiol. Endocrinol. Metab. 2002;282:E733&#x2013;E738. doi: 10.1152/ajpendo.2002.282.3.E733.</Citation><ArticleIdList><ArticleId IdType="doi">10.1152/ajpendo.2002.282.3.E733</ArticleId><ArticleId IdType="pubmed">11832379</ArticleId></ArticleIdList></Reference><Reference><Citation>Ibberson M., Riederer B.M., Uldry M., Guhl B., Roth J., Thorens B. Immunolocalization of GLUTX1 in the testis and to specific brain areas and vasopressin-containing neurons. Endocrinology. 2002;143:276&#x2013;284. doi: 10.1210/endo.143.1.8587.</Citation><ArticleIdList><ArticleId IdType="doi">10.1210/endo.143.1.8587</ArticleId><ArticleId IdType="pubmed">11751619</ArticleId></ArticleIdList></Reference><Reference><Citation>Gawlik V., Schmidt S., Scheepers A., Wennemuth G., Augustin R., Aumuller G., Moser M., Al-Hasani H., Kluge R., Joost H.G., et al. Targeted disruption of Slc2a8 (GLUT8) reduces motility and mitochondrial potential of spermatozoa. Mol. Membr. Biol. 2008;25:224&#x2013;235. doi: 10.1080/09687680701855405.</Citation><ArticleIdList><ArticleId IdType="doi">10.1080/09687680701855405</ArticleId><ArticleId IdType="pmc">PMC2557070</ArticleId><ArticleId IdType="pubmed">18428038</ArticleId></ArticleIdList></Reference><Reference><Citation>Zhao F.Q., Miller P.J., Wall E.H., Zheng Y.C., Dong B., Neville M.C., McFadden T.B. Bovine glucose transporter GLUT8: Cloning, expression, and developmental regulation in mammary gland. BBA-Gene Struct. Expr. 2004;1680:103&#x2013;113. doi: 10.1016/j.bbaexp.2004.09.001.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/j.bbaexp.2004.09.001</ArticleId><ArticleId IdType="pubmed">15488990</ArticleId></ArticleIdList></Reference><Reference><Citation>Carayannopoulos M.O., Chi M.M., Cui Y., Pingsterhaus J.M., McKnight R.A., Mueckler M., Devaskar S.U., Moley K.H. GLUT8 is a glucose transporter responsible for insulin-stimulated glucose uptake in the blastocyst. Proc. Natl. Acad. Sci. USA. 2000;97:7313&#x2013;7318. doi: 10.1073/pnas.97.13.7313.</Citation><ArticleIdList><ArticleId IdType="doi">10.1073/pnas.97.13.7313</ArticleId><ArticleId IdType="pmc">PMC16542</ArticleId><ArticleId IdType="pubmed">10860996</ArticleId></ArticleIdList></Reference><Reference><Citation>Lisinski I., Schurmann A., Joost H.G., Cushman S.W., Al-Hasani H. Targeting of GLUT6 (formerly GLUT9) and GLUT8 in rat adipose cells. Biochem. J. 2001;358:517&#x2013;522. doi: 10.1042/bj3580517.</Citation><ArticleIdList><ArticleId IdType="doi">10.1042/bj3580517</ArticleId><ArticleId IdType="pmc">PMC1222087</ArticleId><ArticleId IdType="pubmed">11513753</ArticleId></ArticleIdList></Reference><Reference><Citation>Piroli G.G., Grillo C.A., Hoskin E.K., Znamensky V., Katz E.B., Milner T.A., McEwen B.S., Charron M.J., Reagan L.P. Peripheral glucose administration stimulates the translocation of GLUT8 glucose transporter to the endoplasmic reticulum in the rat hippocampus. J. Comp. Neurol. 2002;452:103&#x2013;114. doi: 10.1002/cne.10368.</Citation><ArticleIdList><ArticleId IdType="doi">10.1002/cne.10368</ArticleId><ArticleId IdType="pubmed">12271485</ArticleId></ArticleIdList></Reference><Reference><Citation>Rogers S., Docherty S.E., Slavin J.L., Henderson M.A., Best J.D. Differential expression of GLUT12 in breast cancer and normal breast tissue. Cancer Lett. 2003;193:225&#x2013;233. doi: 10.1016/S0304-3835(03)00010-7.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/S0304-3835(03)00010-7</ArticleId><ArticleId IdType="pubmed">12706881</ArticleId></ArticleIdList></Reference><Reference><Citation>Uldry M., Ibberson M., Horisberger J.D., Chatton J.Y., Riederer B.M., Thorens B. Identification of a mammalian H(+)-myo-inositol symporter expressed predominantly in the brain. EMBO J. 2001;20:4467&#x2013;4477. doi: 10.1093/emboj/20.16.4467.</Citation><ArticleIdList><ArticleId IdType="doi">10.1093/emboj/20.16.4467</ArticleId><ArticleId IdType="pmc">PMC125574</ArticleId><ArticleId IdType="pubmed">11500374</ArticleId></ArticleIdList></Reference><Reference><Citation>Goran M.I., Ulijaszek S.J., Ventura E.E. High fructose corn syrup and diabetes prevalence: A global perspective. Glob. Publ. Health. 2013;8:55&#x2013;64. doi: 10.1080/17441692.2012.736257.</Citation><ArticleIdList><ArticleId IdType="doi">10.1080/17441692.2012.736257</ArticleId><ArticleId IdType="pubmed">23181629</ArticleId></ArticleIdList></Reference><Reference><Citation>Nomura K., Yamanouchi T. The role of fructose-enriched diets in mechanisms of nonalcoholic fatty liver disease. J. Nutr. Biochem. 2012;23:203&#x2013;208. doi: 10.1016/j.jnutbio.2011.09.006.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/j.jnutbio.2011.09.006</ArticleId><ArticleId IdType="pubmed">22129639</ArticleId></ArticleIdList></Reference><Reference><Citation>Gaby A.R. Adverse effects of dietary fructose. Altern. Med. Rev. 2005;10:294&#x2013;306.</Citation><ArticleIdList><ArticleId IdType="pubmed">16366738</ArticleId></ArticleIdList></Reference><Reference><Citation>Fan X.J., Liu H.R., Liu M., Wang Y.Y., Qiu L., Cui Y.F. Increased utilization of fructose has a positive effect on the development of breast cancer. PEER J. 2017;5:e3804. doi: 10.7717/peerj.3804.</Citation><ArticleIdList><ArticleId IdType="doi">10.7717/peerj.3804</ArticleId><ArticleId IdType="pmc">PMC5622605</ArticleId><ArticleId IdType="pubmed">28970966</ArticleId></ArticleIdList></Reference><Reference><Citation>Liu H.B., Huang D.S., McArthur D.L., Boros L.G., Nissen N., Heaney A.P. Fructose Induces Transketolase Flux to Promote Pancreatic Cancer Growth. Cancer Res. 2010;70:6368&#x2013;6376. doi: 10.1158/0008-5472.CAN-09-4615.</Citation><ArticleIdList><ArticleId IdType="doi">10.1158/0008-5472.CAN-09-4615</ArticleId><ArticleId IdType="pubmed">20647326</ArticleId></ArticleIdList></Reference><Reference><Citation>Carvalho K.C., Cunha I.W., Rocha R.M., Ayala F.R., Cajaiba M.M., Begnami M.D., Vilela R.S., Paiva G.R., Andrade R.G., Soares F.A. GLUT1 expression in malignant tumors and its use as an immunodiagnostic marker. Clinics. 2011;66:965&#x2013;972. doi: 10.1590/S1807-59322011000600008.</Citation><ArticleIdList><ArticleId IdType="doi">10.1590/S1807-59322011000600008</ArticleId><ArticleId IdType="pmc">PMC3129958</ArticleId><ArticleId IdType="pubmed">21808860</ArticleId></ArticleIdList></Reference><Reference><Citation>Goodwin J., Neugent M.L., Lee S.Y., Choe J.H., Choi H., Jenkins D.M.R., Ruthenborg R.J., Robinson M.W., Jeong J.Y., Wake M., et al. The distinct metabolic phenotype of lung squamous cell carcinoma defines selective vulnerability to glycolytic inhibition. Nat. Commun. 2017;8:15503. doi: 10.1038/ncomms15503.</Citation><ArticleIdList><ArticleId IdType="doi">10.1038/ncomms15503</ArticleId><ArticleId IdType="pmc">PMC5458561</ArticleId><ArticleId IdType="pubmed">28548087</ArticleId></ArticleIdList></Reference><Reference><Citation>Kayano T., Fukumoto H., Eddy R.L., Fan Y.S., Byers M.G., Shows T.B., Bell G.I. Evidence for a Family of Human Glucose Transporter-Like Proteins&#x2014;Sequence and Gene Localization of a Protein Expressed in Fetal Skeletal-Muscle and Other Tissues. J. Biol. Chem. 1988;263:15245&#x2013;15248. doi: 10.1016/S0021-9258(19)37577-5.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/S0021-9258(19)37577-5</ArticleId><ArticleId IdType="pubmed">3170580</ArticleId></ArticleIdList></Reference><Reference><Citation>Zamora-Leon S.P., Golde D.W., Concha I.I., Rivas C.I., DelgadoLopez F., Baselga J., Nualart F., Vera J.C. Expression of the fructose transporter GLUT5 in human breast cancer. Proc. Natl. Acad. Sci. USA. 1996;93:1847&#x2013;1852. doi: 10.1073/pnas.93.5.1847.</Citation><ArticleIdList><ArticleId IdType="doi">10.1073/pnas.93.5.1847</ArticleId><ArticleId IdType="pmc">PMC39870</ArticleId><ArticleId IdType="pubmed">8700847</ArticleId></ArticleIdList></Reference><Reference><Citation>Trayner B.J., Grant T.N., West F.G., Cheeseman C.I. Synthesis and characterization of 6-deoxy-6-fluoro-D-fructose as a potential compound for imaging breast cancer with PET. Bioorganic Med. Chem. 2009;17:5488&#x2013;5495. doi: 10.1016/j.bmc.2009.06.034.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/j.bmc.2009.06.034</ArticleId><ArticleId IdType="pubmed">19586773</ArticleId></ArticleIdList></Reference><Reference><Citation>Bono Y., Mizumoto Y., Nakamura M., Iwadare J., Obata T., Fujiwara H. FDG-PET-positive ovarian thecoma with GLUT5 expression: Five cases. J. Obstet. Gynaecol. Res. 2016;43:599&#x2013;603. doi: 10.1111/jog.13243.</Citation><ArticleIdList><ArticleId IdType="doi">10.1111/jog.13243</ArticleId><ArticleId IdType="pubmed">27987341</ArticleId></ArticleIdList></Reference><Reference><Citation>Wolin K.Y., Carson K., Colditz G.A. Obesity and Cancer. Oncologist. 2010;15:556&#x2013;565. doi: 10.1634/theoncologist.2009-0285.</Citation><ArticleIdList><ArticleId IdType="doi">10.1634/theoncologist.2009-0285</ArticleId><ArticleId IdType="pmc">PMC3227989</ArticleId><ArticleId IdType="pubmed">20507889</ArticleId></ArticleIdList></Reference><Reference><Citation>Rowlands M.A., Gunnell D., Harris R., Vatten L.J., Holly J.M., Martin R.M. Circulating insulin-like growth factor peptides and prostate cancer risk: A systematic review and meta-analysis. Int. J. Cancer. 2009;124:2416&#x2013;2429. doi: 10.1002/ijc.24202.</Citation><ArticleIdList><ArticleId IdType="doi">10.1002/ijc.24202</ArticleId><ArticleId IdType="pmc">PMC2743036</ArticleId><ArticleId IdType="pubmed">19142965</ArticleId></ArticleIdList></Reference><Reference><Citation>Gallagher E.J., LeRoith D. The proliferating role of insulin and insulin-like growth factors in cancer. Trends Endocrin. Met. 2010;21:610&#x2013;618. doi: 10.1016/j.tem.2010.06.007.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/j.tem.2010.06.007</ArticleId><ArticleId IdType="pmc">PMC2949481</ArticleId><ArticleId IdType="pubmed">20663687</ArticleId></ArticleIdList></Reference><Reference><Citation>Graham N.A., Tahmasian M., Kohli B., Komisopoulou E., Zhu M.G., Vivanco I., Teitell M.A., Wu H., Ribas A., Lo R.S., et al. Glucose deprivation activates a metabolic and signaling amplification loop leading to cell death. Mol. Syst. Biol. 2012;8:589&#x2013;904. doi: 10.1038/msb.2012.20.</Citation><ArticleIdList><ArticleId IdType="doi">10.1038/msb.2012.20</ArticleId><ArticleId IdType="pmc">PMC3397414</ArticleId><ArticleId IdType="pubmed">22735335</ArticleId></ArticleIdList></Reference><Reference><Citation>Xie L.L., Wang W.Q. Weight control and cancer preventive mechanisms: Role of insulin growth factor-1-mediated signaling pathways. Exp. Biol. Med. 2013;238:127&#x2013;132. doi: 10.1177/1535370213477602.</Citation><ArticleIdList><ArticleId IdType="doi">10.1177/1535370213477602</ArticleId><ArticleId IdType="pmc">PMC4049068</ArticleId><ArticleId IdType="pubmed">23576795</ArticleId></ArticleIdList></Reference><Reference><Citation>Raffaghello L., Lee C., Safdie F.M., Wei M., Madia F., Bianchi G., Longo V.D. Starvation-dependent differential stress resistance protects normal but not cancer COS against high-dose chemotherapy. Proc. Natl. Acad. Sci. USA. 2008;105:8215&#x2013;8220. doi: 10.1073/pnas.0708100105.</Citation><ArticleIdList><ArticleId IdType="doi">10.1073/pnas.0708100105</ArticleId><ArticleId IdType="pmc">PMC2448817</ArticleId><ArticleId IdType="pubmed">18378900</ArticleId></ArticleIdList></Reference><Reference><Citation>Allen B.G., Bhatia S.K., Anderson C.M., Eichenberger-Gilmore J.M., Sibenaller Z.A., Mapuskar K.A., Schoenfeld J.D., Buatti J.M., Spitz D.R., Fath M.A. Ketogenic diets as an adjuvant cancer therapy: History and potential mechanism. Redox. Biol. 2014;2:963&#x2013;970. doi: 10.1016/j.redox.2014.08.002.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/j.redox.2014.08.002</ArticleId><ArticleId IdType="pmc">PMC4215472</ArticleId><ArticleId IdType="pubmed">25460731</ArticleId></ArticleIdList></Reference><Reference><Citation>Granchi C., Fortunato S., Minutolo F. Anticancer agents interacting with membrane glucose transporters. Medchemcomm. 2016;7:1716&#x2013;1729. doi: 10.1039/C6MD00287K.</Citation><ArticleIdList><ArticleId IdType="doi">10.1039/C6MD00287K</ArticleId><ArticleId IdType="pmc">PMC5198910</ArticleId><ArticleId IdType="pubmed">28042452</ArticleId></ArticleIdList></Reference><Reference><Citation>Tanasova M., Begoyan V.V., Weselinski L.J. Targeting Sugar Uptake and Metabolism for Cancer Identification and Therapy: An Overview. Curr. Top. Med. Chem. 2018;18:467&#x2013;483. doi: 10.2174/1568026618666180523110837.</Citation><ArticleIdList><ArticleId IdType="doi">10.2174/1568026618666180523110837</ArticleId><ArticleId IdType="pubmed">29788891</ArticleId></ArticleIdList></Reference><Reference><Citation>Boel A., Burger J., Vanhomwegen M., Beyens A., Renard M., Barnhoorn S., Casteleyn C., Reinhardt D.P., Descamps B., Vanhove C., et al. Slc2a10 knock-out mice deficient in ascorbic acid synthesis recapitulate aspects of arterial tortuosity syndrome and display mitochondrial respiration defects. Hum. Mol. Genet. 2020;29:1476&#x2013;1488. doi: 10.1093/hmg/ddaa071.</Citation><ArticleIdList><ArticleId IdType="doi">10.1093/hmg/ddaa071</ArticleId><ArticleId IdType="pubmed">32307537</ArticleId></ArticleIdList></Reference><Reference><Citation>Shi Y., Zhang Y., Ran F., Liu J., Lin J., Hao X., Ding L., Ye Q. Let-7a-5p inhibits triple-negative breast tumor growth and metastasis through GLUT12-mediated warburg effect. Cancer Lett. 2020;495:53&#x2013;65. doi: 10.1016/j.canlet.2020.09.012.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/j.canlet.2020.09.012</ArticleId><ArticleId IdType="pubmed">32946964</ArticleId></ArticleIdList></Reference><Reference><Citation>Jacquier V., Gitenay D., Fritsch S., Bonnet S., Gy&#x151;rffy B., Jalaguier S., Linares L.K., Cavaill&#xe8;s V., Teyssier C. RIP140 inhibits glycolysis-dependent proliferation of breast cancer cells by regulating GLUT3 expression through transcriptional crosstalk between hypoxia induced factor and p53. Cell. Mol. Life Sci. CMLS. 2022;79:270. doi: 10.1007/s00018-022-04277-3.</Citation><ArticleIdList><ArticleId IdType="doi">10.1007/s00018-022-04277-3</ArticleId><ArticleId IdType="pmc">PMC9061696</ArticleId><ArticleId IdType="pubmed">35501580</ArticleId></ArticleIdList></Reference><Reference><Citation>W&#x142;odarczyk J., W&#x142;odarczyk M., Zieli&#x144;ska M., J&#x119;drzejczak B., Dziki &#x141;., Fichna J. Blockade of fructose transporter protein GLUT5 inhibits proliferation of colon cancer cells: Proof of concept for a new class of anti-tumor therapeutics. Pharmacol. Rep. 2021;73:939&#x2013;945. doi: 10.1007/s43440-021-00281-9.</Citation><ArticleIdList><ArticleId IdType="doi">10.1007/s43440-021-00281-9</ArticleId><ArticleId IdType="pmc">PMC8180478</ArticleId><ArticleId IdType="pubmed">34052986</ArticleId></ArticleIdList></Reference><Reference><Citation>Shen Z., Li Z., Liu Y., Li Y., Feng X., Zhan Y., Lin M., Fang C., Fang Y., Deng H. GLUT5-KHK axis-mediated fructose metabolism drives proliferation and chemotherapy resistance of colorectal cancer. Cancer Lett. 2022;534:215617. doi: 10.1016/j.canlet.2022.215617.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/j.canlet.2022.215617</ArticleId><ArticleId IdType="pubmed">35257833</ArticleId></ArticleIdList></Reference><Reference><Citation>Caruana B.T., Byrne F.L. The NF-&#x3ba;B signalling pathway regulates GLUT6 expression in endometrial cancer. Cell. Signal. 2020;73:109688. doi: 10.1016/j.cellsig.2020.109688.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/j.cellsig.2020.109688</ArticleId><ArticleId IdType="pubmed">32512041</ArticleId></ArticleIdList></Reference><Reference><Citation>Zeng Z., Nian Q., Chen N., Zhao M., Zheng Q., Zhang G., Zhao Z., Chen Y., Wang J., Zeng J., et al. Ginsenoside Rg3 inhibits angiogenesis in gastric precancerous lesions through downregulation of Glut1 and Glut4. Biomed. Pharmacother. 2022;145:112086. doi: 10.1016/j.biopha.2021.112086.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/j.biopha.2021.112086</ArticleId><ArticleId IdType="pubmed">34799220</ArticleId></ArticleIdList></Reference><Reference><Citation>Fu M., Liu Y., Cheng H., Xu K., Wang G. Coptis chinensis and dried ginger herb combination inhibits gastric tumor growth by interfering with glucose metabolism via LDHA and SLC2A1. J. Ethnopharmacol. 2022;284:114771. doi: 10.1016/j.jep.2021.114771.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/j.jep.2021.114771</ArticleId><ArticleId IdType="pubmed">34737010</ArticleId></ArticleIdList></Reference><Reference><Citation>Bai Y., Ye B., Li T., Wang R., Qi X. H22954, a long non-coding RNA, inhibits glucose uptake in leukemia cells in a GLUT10-dependent manner. Hematology. 2022;27:469&#x2013;475. doi: 10.1080/16078454.2022.2061112.</Citation><ArticleIdList><ArticleId IdType="doi">10.1080/16078454.2022.2061112</ArticleId><ArticleId IdType="pubmed">35413230</ArticleId></ArticleIdList></Reference><Reference><Citation>Olszewski K., Barsotti A., Feng X.-J., Momcilovic M., Liu K.G., Kim J.-I., Morris K., Lamarque C., Gaffney J., Yu X., et al. Inhibition of glucose transport synergizes with chemical or genetic disruption of mitochondrial metabolism and suppresses TCA cycle-deficient tumors. Cell Chem. Biol. 2022;29:423&#x2013;435.e410. doi: 10.1016/j.chembiol.2021.10.007.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/j.chembiol.2021.10.007</ArticleId><ArticleId IdType="pubmed">34715056</ArticleId></ArticleIdList></Reference><Reference><Citation>Hayashi K., Noguchi-Shinohara M., Sato T., Hosomichi K., Kannon T., Abe C., Domoto C., Yuki-Nozaki S., Mori A., Horimoto M., et al. Effects of functional variants of vitamin C transporter genes on apolipoprotein E E4-associated risk of cognitive decline: The Nakajima study. PLoS ONE. 2021;16:e0259663. doi: 10.1371/journal.pone.0259663.</Citation><ArticleIdList><ArticleId IdType="doi">10.1371/journal.pone.0259663</ArticleId><ArticleId IdType="pmc">PMC8592483</ArticleId><ArticleId IdType="pubmed">34780525</ArticleId></ArticleIdList></Reference><Reference><Citation>Basu S., Liu C., Zhou X.K., Nishiguchi R., Ha T., Chen J., Johncilla M., Yantiss R.K., Montrose D.C., Dannenberg A.J. GLUT5 is a determinant of dietary fructose-mediated exacerbation of experimental colitis. Am. J. Physiol. Gastrointest. Liver Physiol. 2021;321:G232&#x2013;G242. doi: 10.1152/ajpgi.00059.2021.</Citation><ArticleIdList><ArticleId IdType="doi">10.1152/ajpgi.00059.2021</ArticleId><ArticleId IdType="pubmed">34133236</ArticleId></ArticleIdList></Reference><Reference><Citation>Sun Y., Lu L., Li L., Wang J. An advance about the genetic causes of epilepsy. E3S Web Conf. 2021;271:03068. doi: 10.1051/e3sconf/202127103068.</Citation><ArticleIdList><ArticleId IdType="doi">10.1051/e3sconf/202127103068</ArticleId></ArticleIdList></Reference><Reference><Citation>Patan&#xe8; F., Pasquetti E., Sullo F., Tosto M., Romano C., Salafia S., Falsaperla R. SLC2A1 and Its Related Epileptic Phenotypes. J. Pediatric Neurol. 2022 doi: 10.1055/s-0041-1728668.</Citation><ArticleIdList><ArticleId IdType="doi">10.1055/s-0041-1728668</ArticleId></ArticleIdList></Reference><Reference><Citation>Lee H., Kim E., Shin E.-A., Shon J.C., Sun H., Kim J.E., Jung J.W., Lee H., Pinanga Y., Song D.-G., et al. Crosstalk between TM4SF5 and GLUT8 regulates fructose metabolism in hepatic steatosis. Mol. Metab. 2022;58:101451. doi: 10.1016/j.molmet.2022.101451.</Citation><ArticleIdList><ArticleId IdType="doi">10.1016/j.molmet.2022.101451</ArticleId><ArticleId IdType="pmc">PMC8866669</ArticleId><ArticleId IdType="pubmed">35123128</ArticleId></ArticleIdList></Reference><Reference><Citation>Wu Z., Wen Y., Fan G., He H., Zhou S., Chen L. HEMGN and SLC2A1 might be potential diagnostic biomarkers of steroid-induced osteonecrosis of femoral head: Study based on WGCNA and DEGs screening. BMC Musculoskelet. Disord. 2021;22:85. doi: 10.1186/s12891-021-03958-7.</Citation><ArticleIdList><ArticleId IdType="doi">10.1186/s12891-021-03958-7</ArticleId><ArticleId IdType="pmc">PMC7811219</ArticleId><ArticleId IdType="pubmed">33451334</ArticleId></ArticleIdList></Reference><Reference><Citation>Shi Y.-L., Zhang Y.-P., Luo H., Xu F., Gao J.-M., Shi J.-S., Gong Q.-H. Trilobatin, a Natural Food Additive, Exerts Anti-Type 2 Diabetes Effect Mediated by Nrf2/ARE and IRS-1/GLUT2 Signaling Pathways. Front. Pharmacol. 2022;13:828473. doi: 10.3389/fphar.2022.828473.</Citation><ArticleIdList><ArticleId IdType="doi">10.3389/fphar.2022.828473</ArticleId><ArticleId IdType="pmc">PMC8829035</ArticleId><ArticleId IdType="pubmed">35153796</ArticleId></ArticleIdList></Reference><Reference><Citation>Ye X., Chen W., Tu P., Jia R., Liu Y., Tang Q., Chen C., Yang C., Zheng X., Chu Q. Antihyperglycemic effect of an anthocyanin, cyanidin-3-O-glucoside, is achieved by regulating GLUT-1 via the Wnt/&#x3b2;-catenin-WISP1 signaling pathway. Food Funct. 2022;13:4612&#x2013;4623. doi: 10.1039/D1FO03730G.</Citation><ArticleIdList><ArticleId IdType="doi">10.1039/D1FO03730G</ArticleId><ArticleId IdType="pubmed">35357376</ArticleId></ArticleIdList></Reference><Reference><Citation>Shao R., Liao X., Lan Y., Zhang H., Jiao L., Du Q., Han D., Ai Q., Mai K., Wan M. Vitamin D regulates insulin pathway and glucose metabolism in zebrafish (Danio rerio) FASEB J. 2022;36:e22330. doi: 10.1096/fj.202200334RR.</Citation><ArticleIdList><ArticleId IdType="doi">10.1096/fj.202200334RR</ArticleId><ArticleId IdType="pubmed">35474468</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></PubmedArticle></PubmedArticleSet>