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Journal articles on the topic 'GLUT12'

Author: Grafiati

Published: 10 September 2021

Last updated: 17 July 2025

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1

Stuart, Charles A., Deling Yin, Mary E. A. Howell, Rhesa J. Dykes, John J. Laffan, and Arny A. Ferrando. "Hexose transporter mRNAs for GLUT4, GLUT5, and GLUT12 predominate in human muscle." American Journal of Physiology-Endocrinology and Metabolism 291, no. 5 (2006): E1067—E1073. http://dx.doi.org/10.1152/ajpendo.00250.2006.

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In the past few years, 8 additional members of the facilitative hexose transporter family have been identified, giving a total of 14 members of the SLC2A family of membrane-bound hexose transporters. To determine which of the new hexose transporters were expressed in muscle, mRNA concentrations of 11 glucose transporters (GLUTs) were quantified and compared. RNA from muscle from 10 normal volunteers was subjected to RT-PCR. Primers were designed that amplified 78- to 241-base fragments, and cDNA standards were cloned for GLUT1, GLUT2, GLUT3, GLUT4, GLUT5, GLUT6, GLUT8, GLUT9, GLUT10, GLUT11, G

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2

Pyla, Rajkumar, Ninu Poulose, John Y. Jun, and Lakshman Segar. "Expression of conventional and novel glucose transporters, GLUT1, -9, -10, and -12, in vascular smooth muscle cells." American Journal of Physiology-Cell Physiology 304, no. 6 (2013): C574—C589. http://dx.doi.org/10.1152/ajpcell.00275.2012.

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Intimal hyperplasia is characterized by exaggerated proliferation of vascular smooth muscle cells (VSMCs). Enhanced VSMC growth is dependent on increased glucose uptake and metabolism. Facilitative glucose transporters (GLUTs) are comprised of conventional GLUT isoforms (GLUT1–5) and novel GLUT isoforms (GLUT6–14). Previous studies demonstrate that GLUT1 overexpression or GLUT10 downregulation contribute to phenotypic changes in VSMCs. To date, the expression profile of all 14 GLUT isoforms has not been fully examined in VSMCs. Using the proliferative and differentiated phenotypes of human aor

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3

Schaan, Beatriz D’Agord, and Ubiratan Fabres Machado. "Glucose transporters in animal models of diabetes and hypertension." American Journal of Physiology-Renal Physiology 291, no. 3 (2006): F702—F703. http://dx.doi.org/10.1152/ajprenal.00065.2006.

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Renal tubular glucose reabsorption is mediated by facilitative glucose transporter (GLUT) proteins and energy-dependent sodium glucose luminal transporters. Glucose transport in the diabetic kidney is upregulated and has been implicated in the pathogenesis of progressive diabetic nephropathy. Hyperglycemia, hypertension, and activation of the renin-angiotensin system are believed important in the development of the disease. The present study examines the renal expression of the facilitative glucose transporters GLUT1 and GLUT12 in rat models of diabetic nephropathy. Sprague-Dawley and transgen

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4

Linden, Kelly C., Carrie L. DeHaan, Yuan Zhang, et al. "Renal expression and localization of the facilitative glucose transporters GLUT1 and GLUT12 in animal models of hypertension and diabetic nephropathy." American Journal of Physiology-Renal Physiology 290, no. 1 (2006): F205—F213. http://dx.doi.org/10.1152/ajprenal.00237.2004.

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Renal tubular glucose reabsorption is mediated by facilitative glucose transporter (GLUT) proteins and energy-dependent sodium glucose luminal transporters. Glucose transport in the diabetic kidney is upregulated and has been implicated in the pathogenesis of progressive diabetic nephropathy. Hyperglycemia, hypertension, and activation of the renin-angiotensin system are believed important in the development of the disease. The present study examines the renal expression of the facilitative glucose transporters GLUT1 and GLUT12 in rat models of diabetic nephropathy. Sprague-Dawley and transgen

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5

Matsuo, Shunsuke, Miki Hiasa, and Hiroshi Omote. "Functional characterization and tissue localization of the facilitative glucose transporter GLUT12." Journal of Biochemistry 168, no. 6 (2020): 611–20. http://dx.doi.org/10.1093/jb/mvaa090.

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Abstract Facilitative glucose transporters (GLUTs) play crucial roles in glucose utilization and homeostasis. GLUT12 was initially isolated as a novel GLUT4-like transporter involved in insulin-dependent glucose transport. However, tissue distribution and biochemical properties of GLUT12 are not well understood. In this study, we investigated the basic kinetic properties and tissue distribution of GLUT12. Human GLUT12 and GLUT1 were overexpressed and purified using Ni-NTA column chromatography. Reconstituted proteoliposomes showed time-dependent d-glucose transport activity, which was inhibite

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6

Stuart, Charles A., Mary E. A. Howell, Yi Zhang, and Deling Yin. "Insulin-Stimulated Translocation of Glucose Transporter (GLUT) 12 Parallels That of GLUT4 in Normal Muscle." Journal of Clinical Endocrinology & Metabolism 94, no. 9 (2009): 3535–42. http://dx.doi.org/10.1210/jc.2009-0162.

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Context: GLUT4 is the predominant glucose transporter isoform expressed in fat and muscle. In GLUT4 null mice, insulin-stimulated glucose uptake into muscle was diminished but not eliminated, suggesting that another insulin-sensitive system was present. Objective: This study was intended to determine whether insulin caused GLUT12 translocation in muscle. Design: Six normal volunteers had muscle biopsies before and after euglycemic insulin infusions. Setting: Infusions and biopsies were performed in an outpatient clinic. Participants: Subjects were nonobese, young adults with no family history

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7

Pujol-Giménez, Jonai, Alejandra Pérez, Alejandro M. Reyes, Donald D. F. Loo, and Maria Pilar Lostao. "Functional characterization of the human facilitative glucose transporter 12 (GLUT12) by electrophysiological methods." American Journal of Physiology-Cell Physiology 308, no. 12 (2015): C1008—C1022. http://dx.doi.org/10.1152/ajpcell.00343.2014.

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GLUT12 is a member of the facilitative family of glucose transporters. The goal of this study was to characterize the functional properties of GLUT12, expressed in Xenopus laevis oocytes, using radiotracer and electrophysiological methods. Our results showed that GLUT12 is a facilitative sugar transporter with substrate selectivity: d-glucose ≥ α-methyl-d-glucopyranoside (α-MG) > 2-deoxy-d-glucose(2-DOG) > d-fructose = d-galactose. α-MG is a characteristic substrate of the Na+/glucose (SGLT) family and has not been shown to be a substrate of any of the GLUTs. In the absence of sugar, 22N

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8

Wood, I. Stuart, and Paul Trayhurn. "Glucose transporters (GLUT and SGLT): expanded families of sugar transport proteins." British Journal of Nutrition 89, no. 1 (2003): 3–9. http://dx.doi.org/10.1079/bjn2002763.

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The number of known glucose transporters has expanded considerably over the past 2 years. At least three, and up to six, Na+-dependent glucose transporters (SGLT1–SGLT6; gene name SLC5A) have been identified. Similarly, thirteen members of the family of facilitative sugar transporters (GLUT1–GLUT12 and HMIT; gene name SLC2A) are now recognised. These various transporters exhibit different substrate specificities, kinetic properties and tissue expression profiles. The number of distinct gene products, together with the presence of several different transporters in certain tissues and cells (for

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9

Barrett, Montana Renae, and Michael Scott Davis. "Conditioning-induced expression of novel glucose transporters in canine skeletal muscle homogenate." PLOS ONE 18, no. 5 (2023): e0285424. http://dx.doi.org/10.1371/journal.pone.0285424.

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Athletic conditioning can increase the capacity for insulin-stimulated skeletal muscle glucose uptake through increased sarcolemmal expression of GLUT4 and potentially additional novel glucose transporters. We used a canine model that has previously demonstrated conditioning-induced increases in basal, insulin- and contraction-stimulated glucose uptake to identify whether expression of glucose transporters other than GLUT4 was upregulated by athletic conditioning. Skeletal muscle biopsies were obtained from 12 adult Alaskan Husky racing sled dogs before and after a full season of conditioning

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10

Pouliot, Frederic, Salma Meizou, Cassandra Ringuette Goulet, et al. "GLUT1 expression in high-risk prostate cancer: Correlation with 18F-FDG-PET/CT and clinical outcome." Journal of Clinical Oncology 38, no. 6_suppl (2020): 291. http://dx.doi.org/10.1200/jco.2020.38.6_suppl.291.

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291 Background: Tumour FDG-uptake is of prognostic value in high-risk and metastatic prostate cancer (PCa). The aim of this study is to investigate the underlying glucose metabolism mechanisms of 18F-FDG-uptake on PET/CT imaging in PCa. Methods: Retrospective analysis was conducted for 94 patients diagnosed with a Gleason sum ≥8 at biopsy who underwent 18F-FDG-PET/CT imaging before radical prostatectomy. GLUT1, GLUT12 and HK2 expression were blindly scored after immunohistochemistry on radical prostatectomy specimens by 3 pathologists. 18F-FDG-uptake in primary lesion was measured by a blinded

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11

Gil-Iturbe, Eva, Elisa Félix-Soriano, Neira Sáinz, et al. "Effect of aging and obesity on GLUT12 expression in small intestine, adipose tissue, muscle, and kidney and its regulation by docosahexaenoic acid and exercise in mice." Applied Physiology, Nutrition, and Metabolism 45, no. 9 (2020): 957–67. http://dx.doi.org/10.1139/apnm-2019-0721.

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Obesity is characterized by excessive fat accumulation and inflammation. Aging has also been characterized as an inflammatory condition, frequently accompanied by accumulation of visceral fat. Beneficial effects of exercise and n-3 long-chain polyunsaturated fatty acids in metabolic disorders have been described. Glucose transporter 12 (GLUT12) is one of the less investigated members of the GLUT family. Glucose, insulin, and tumor necrosis factor alpha (TNF-α) induce GLUT12 translocation to the membrane in muscle, adipose tissue, and intestine. We aimed to investigate GLUT12 expression in obes

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12

Wilson-O’Brien, Amy L., Carrie L. DeHaan, and Suzanne Rogers. "Mitogen-Stimulated and Rapamycin-Sensitive Glucose Transporter 12 Targeting and Functional Glucose Transport in Renal Epithelial Cells." Endocrinology 149, no. 3 (2007): 917–24. http://dx.doi.org/10.1210/en.2007-0985.

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We hypothesized that glucose transporter 12 (GLUT12) is involved in regulation of glucose flux in distal renal tubules in response to elevated glucose. We used the Madin-Darby canine kidney polarized epithelial cell model and neutralizing antibodies to analyze GLUT12 targeting and directional GLUT12-mediated glucose transport. At physiological glucose concentrations, GLUT12 was localized to a perinuclear position. High glucose and serum treatment resulted in GLUT12 localization to the apical membrane. This mitogen-stimulated targeting of GLUT12 was inhibited by rapamycin, the specific inhibito

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13

Kyrtata, Natalia, Ben Dickie, Hedley Emsley, and Laura Parkes. "Glucose transporters in Alzheimer's disease." BJPsych Open 7, S1 (2021): S265—S266. http://dx.doi.org/10.1192/bjo.2021.707.

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BackgroundPhysiological brain function depends on tight glucose regulation, including transport and phosphorylation, the first step in its metabolism. Impaired glucose regulation is increasingly implicated in the pathophysiology of Alzheimer's disease (AD). Glucose hypometabolism in AD may be at least partly due to impaired glucose transport at the blood-brain barrier (BBB). Glucose transporters (GLUTs) are an integral component of the BBB. There is evidence of a significant reduction in vascular and non-vascular forms of GLUT1 and GLUT3 in AD brains compared to age-matched controls. Glucose t

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14

Chandler, Jenalle D., Elizabeth D. Williams, John L. Slavin, James D. Best, and Suzanne Rogers. "Expression and localization of GLUT1 and GLUT12 in prostate carcinoma." Cancer 97, no. 8 (2003): 2035–42. http://dx.doi.org/10.1002/cncr.11293.

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15

White, Mark A., Efrosini Tsouko, Chenchu Lin, et al. "GLUT12 promotes prostate cancer cell growth and is regulated by androgens and CaMKK2 signaling." Endocrine-Related Cancer 25, no. 4 (2018): 453–69. http://dx.doi.org/10.1530/erc-17-0051.

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Despite altered metabolism being an accepted hallmark of cancer, it is still not completely understood which signaling pathways regulate these processes. Given the central role of androgen receptor (AR) signaling in prostate cancer, we hypothesized that AR could promote prostate cancer cell growth in part through increasing glucose uptake via the expression of distinct glucose transporters. Here, we determined that AR directly increased the expression ofSLC2A12, the gene that encodes the glucose transporter GLUT12. In support of these findings, gene signatures of AR activity correlated withSLC

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16

Ware, Bruce, Marie Bevier, Yoshinori Nishijima, Suzanne Rogers, Cynthia A. Carnes, and Véronique A. Lacombe. "Chronic heart failure selectively induces regional heterogeneity of insulin-responsive glucose transporters." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 301, no. 5 (2011): R1300—R1306. http://dx.doi.org/10.1152/ajpregu.00822.2010.

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Glucose uptake across the sarcolemma is regulated by a family of membrane proteins called glucose transporters (GLUTs), which includes GLUT4 (the major cardiac isoform) and GLUT12 (a novel, second insulin-sensitive isoform). Potential regional patterns in glucose transport across the cardiac chambers have not been examined; thus, we hypothesized that insulin-responsive GLUT4 and -12 protein and gene expression would be chamber specific in healthy subjects and during chronic heart failure (HF). Using a canine model of tachypacing-induced, progressive, chronic HF, total GLUT protein and messenge

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17

Toyoda, Yu, Tappei Takada, Hiroshi Miyata, et al. "Identification of GLUT12/SLC2A12 as a urate transporter that regulates the blood urate level in hyperuricemia model mice." Proceedings of the National Academy of Sciences 117, no. 31 (2020): 18175–77. http://dx.doi.org/10.1073/pnas.2006958117.

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Recent genome-wide association studies have revealed some genetic loci associated with serum uric acid levels and susceptibility to gout/hyperuricemia which contain potential candidates of physiologically important urate transporters. One of these novel loci is located upstream ofSGK1andSLC2A12, suggesting that variations in these genes increase the risks of hyperuricemia and gout. We herein focused onSLC2A12encoding a transporter, GLUT12, the physiological function of which remains unclear. As GLUT12 belongs to the same protein family as a well-recognized urate transporter GLUT9, we hypothesi

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18

Yu, Qinghua, Liqi Zhu, Jian Lin, et al. "Functional Analyse of GLUT1 and GLUT12 in Glucose Uptake in Goat Mammary Gland Epithelial Cells." PLoS ONE 8, no. 5 (2013): e65013. http://dx.doi.org/10.1371/journal.pone.0065013.

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19

Purcell, S. H., L. B. Aerni-Flessner, A. R. Willcockson, K. A. Diggs-Andrews, S. J. Fisher, and K. H. Moley. "Improved Insulin Sensitivity by GLUT12 Overexpression in Mice." Diabetes 60, no. 5 (2011): 1478–82. http://dx.doi.org/10.2337/db11-0033.

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20

Miller, Peter J., Kiera A. Finucane, Megan Hughes, and Feng-Qi Zhao. "Cloning and Expression of Bovine Glucose Transporter GLUT12." Mammalian Genome 16, no. 11 (2005): 873–83. http://dx.doi.org/10.1007/s00335-005-0080-5.

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21

Macheda, Maria, Elizabeth Williams, James Best, Mary Wlodek, and Suzanne Rogers. "Expression and localisation of GLUT1 and GLUT12 glucose transporters in the pregnant and lactating rat mammary gland." Cell and Tissue Research 311, no. 1 (2003): 91–97. http://dx.doi.org/10.1007/s00441-002-0661-5.

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22

Gaster, M., A. Handberg, A. Sch�rmann, H. G. Joost, H. Beck-Nielsen, and H. D. Schr�der. "GLUT11, but not GLUT8 or GLUT12, is expressed in human skeletal muscle in a fibre type-specific pattern." Pfl�gers Archiv European Journal of Physiology 448, no. 1 (2004): 105–13. http://dx.doi.org/10.1007/s00424-003-1219-4.

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23

Rogers, Suzanne, Jenalle D. Chandler, Alison L. Clarke, Steven Petrou, and James D. Best. "Glucose transporter GLUT12-functional characterization in Xenopus laevis oocytes." Biochemical and Biophysical Research Communications 308, no. 3 (2003): 422–26. http://dx.doi.org/10.1016/s0006-291x(03)01417-7.

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24

Chen, Bei, Yunfeng Wang, Manying Geng, Xi Lin, and Wenxue Tang. "Localization of Glucose Transporter 10 to Hair Cells’ Cuticular Plate in the Mouse Inner Ear." BioMed Research International 2018 (June 14, 2018): 1–7. http://dx.doi.org/10.1155/2018/7817453.

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This study aimed to investigate the localization pattern of glucose transporters (Gluts) in mouse cochlea. Genome-wide gene expression analysis using CodeLink™ bioarrays indicated that Glut1 and Glut10 were highly expressed (~10-fold) in mouse cochlea compared with the other members of glucose transporters (Glut2-6, Glut8, and Glut9). Semiquantitative RT-PCR and western blotting confirmed that Glut10 expression in mouse cochlea was high throughout the embryogenesis and postnatal development. Immunofluorescent staining showed that Glut10 protein was localized in the cuticular plate of the outer

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Pehlivanoglu, Suray, Ozge Burcu Sahan, Sebnem Pehlivanoglu, and Kadriye Aktas Kont. "Epithelial mesenchymal transition regulator TWIST1 transcription factor stimulates glucose uptake through upregulation of GLUT1, GLUT3, and GLUT12 in vitro." In Vitro Cellular & Developmental Biology - Animal 57, no. 10 (2021): 933–43. http://dx.doi.org/10.1007/s11626-021-00635-w.

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26

Pujol-Gimenez, Jonai, Eva Martisova, Alberto Perez-Mediavilla, María Pilar Lostao, and Maria J. Ramirez. "Expression of the Glucose Transporter GLUT12 in Alzheimer's Disease Patients." Journal of Alzheimer's Disease 42, no. 1 (2014): 97–101. http://dx.doi.org/10.3233/jad-132498.

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27

Gude, N. M., J. L. Stevenson, S. Rogers, et al. "GLUT12 Expression in Human Placenta in First Trimester and Term." Placenta 24, no. 5 (2003): 566–70. http://dx.doi.org/10.1053/plac.2002.0925.

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28

Gil-Iturbe, Eva, Maite Solas, Mar Cuadrado-Tejedo, et al. "GLUT12 Expression in Brain of Mouse Models of Alzheimer’s Disease." Molecular Neurobiology 57, no. 2 (2019): 798–805. http://dx.doi.org/10.1007/s12035-019-01743-1.

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29

Zhou, Y., P. L. Kaye, and M. Pantaleon. "48. Cloning and characterisation of mouse GLUT12 in preimplantation embryos." Reproduction, Fertility and Development 15, no. 9 (2003): 48. http://dx.doi.org/10.1071/srb03ab48.

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30

DeBosch, Brian J., Maggie Chi, and Kelle H. Moley. "Glucose Transporter 8 (GLUT8) Regulates Enterocyte Fructose Transport and Global Mammalian Fructose Utilization." Endocrinology 153, no. 9 (2012): 4181–91. http://dx.doi.org/10.1210/en.2012-1541.

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Enterocyte fructose absorption is a tightly regulated process that precedes the deleterious effects of excess dietary fructose in mammals. Glucose transporter (GLUT)8 is a glucose/fructose transporter previously shown to be expressed in murine intestine. The in vivo function of GLUT8, however, remains unclear. Here, we demonstrate enhanced fructose-induced fructose transport in both in vitro and in vivo models of enterocyte GLUT8 deficiency. Fructose exposure stimulated [14C]-fructose uptake and decreased GLUT8 protein abundance in Caco2 colonocytes, whereas direct short hairpin RNA-mediated G

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31

Rogers, Suzanne, Susan E. Docherty, John L. Slavin, Michael A. Henderson, and James D. Best. "Differential expression of GLUT12 in breast cancer and normal breast tissue." Cancer Letters 193, no. 2 (2003): 225–33. http://dx.doi.org/10.1016/s0304-3835(03)00010-7.

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32

Gude, N. M., J. L. Stevenson, P. Murthi, et al. "Expression of GLUT12 in the fetal membranes of the human placenta." Placenta 26, no. 1 (2005): 67–72. http://dx.doi.org/10.1016/j.placenta.2004.04.006.

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33

Jiménez-Amilburu, Vanesa, Susanne Jong-Raadsen, Jeroen Bakkers, Herman P. Spaink, and Rubén Marín-Juez. "GLUT12 deficiency during early development results in heart failure and a diabetic phenotype in zebrafish." Journal of Endocrinology 224, no. 1 (2014): 1–15. http://dx.doi.org/10.1530/joe-14-0539.

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Cardiomyopathies-associated metabolic pathologies (e.g., type 2 diabetes and insulin resistance) are a leading cause of mortality. It is known that the association between these pathologies works in both directions, for which heart failure can lead to metabolic derangements such as insulin resistance. This intricate crosstalk exemplifies the importance of a fine coordination between one of the most energy-demanding organs and an equilibrated carbohydrate metabolism. In this light, to assist in the understanding of the role of insulin-regulated glucose transporters (GLUTs) and the development o

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34

Pujol-Gimenez, Jonai, Fátima Pérez de Heredia, Miguel Angel Idoate, Rachel Airley, María Pilar Lostao, and Andrew Robert Evans. "Could GLUT12 be a Potential Therapeutic Target in Cancer Treatment? A Preliminary Report." Journal of Cancer 6, no. 2 (2015): 139–43. http://dx.doi.org/10.7150/jca.10429.

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35

Zhou, Yuchan, Peter L. Kaye, and Marie Pantaleon. "Identification of the facilitative glucose transporter 12 gene Glut12 in mouse preimplantation embryos." Gene Expression Patterns 4, no. 6 (2004): 621–31. http://dx.doi.org/10.1016/j.modgep.2004.04.010.

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36

Waller, Amanda P., Michael George, Anuradha Kalyanasundaram, et al. "GLUT12 functions as a basal and insulin-independent glucose transporter in the heart." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1832, no. 1 (2013): 121–27. http://dx.doi.org/10.1016/j.bbadis.2012.09.013.

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37

Gil-Iturbe, Eva, Rosa Castilla-Madrigal, Jaione Barrenetxe, Ana Cristina Villaro, and María Pilar Lostao. "GLUT12 expression and regulation in murine small intestine and human Caco-2 cells." Journal of Cellular Physiology 234, no. 4 (2018): 4396–408. http://dx.doi.org/10.1002/jcp.27231.

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38

Fam, Barbara C., Laura J. Rose, Rebecca Sgambellone, Zheng Ruan, Joseph Proietto, and Sofianos Andrikopoulos. "Normal muscle glucose uptake in mice deficient in muscle GLUT4." Journal of Endocrinology 214, no. 3 (2012): 313–27. http://dx.doi.org/10.1530/joe-12-0032.

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Skeletal muscle insulin resistance is a major characteristic underpinning type 2 diabetes. Impairments in the insulin responsiveness of the glucose transporter,Glut4 (Slc2a4), have been suggested to be a contributing factor to this disturbance. We have produced muscle-specificGlut4knockout (KO) mice using Cre/LoxP technology on a C57BL6/J background and shown undetectable levels of GLUT4 in both skeletal muscle and heart. Our aim was to determine whether complete deletion of muscle GLUT4 does in fact lead to perturbations in glucose homoeostasis. Glucose tolerance, glucose turnover and 2-deoxy

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Houbrechts, Anne M., An Beckers, Pieter Vancamp, et al. "Age-Dependent Changes in Glucose Homeostasis in Male Deiodinase Type 2 Knockout Zebrafish." Endocrinology 160, no. 11 (2019): 2759–72. http://dx.doi.org/10.1210/en.2019-00445.

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Abstract Thyroid hormones (THs) are crucial regulators of glucose metabolism and insulin sensitivity. Moreover, inactivating mutations in type 2 deiodinase (DIO2), the major TH-activating enzyme, have been associated with type 2 diabetes mellitus in both humans and mice. We studied the link between Dio2 deficiency and glucose homeostasis in fasted males of two different Dio2 knockout (KO) zebrafish lines. Young adult Dio2KO zebrafish (6 to 9 months) were hyperglycemic. Both insulin and glucagon expression were increased, whereas β and α cell numbers in the main pancreatic islet were similar to

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40

McMillin, Shawna L., Parker L. Evans, William M. Taylor, et al. "Muscle-Specific Ablation of Glucose Transporter 1 (GLUT1) Does Not Impair Basal or Overload-Stimulated Skeletal Muscle Glucose Uptake." Biomolecules 12, no. 12 (2022): 1734. http://dx.doi.org/10.3390/biom12121734.

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Glucose transporter 1 (GLUT1) is believed to solely mediate basal (insulin-independent) glucose uptake in skeletal muscle; yet recent work has demonstrated that mechanical overload, a model of resistance exercise training, increases muscle GLUT1 levels. The primary objective of this study was to determine if GLUT1 is necessary for basal or overload-stimulated muscle glucose uptake. Muscle-specific GLUT1 knockout (mGLUT1KO) mice were generated and examined for changes in body weight, body composition, metabolism, systemic glucose regulation, muscle glucose transporters, and muscle [3H]-2-deoxyg

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41

Maaßen, Tjorge, Siranush Vardanyan, Anton Brosig, et al. "Monosomy-3 Alters the Expression Profile of the Glucose Transporters GLUT1-3 in Uveal Melanoma." International Journal of Molecular Sciences 21, no. 24 (2020): 9345. http://dx.doi.org/10.3390/ijms21249345.

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Monosomy-3 in uveal melanoma (UM) cells increases the risk of fatal metastases. The gene encoding the low-affinity glucose transporter GLUT2 resides on chromosome 3q26.2. Here, we analyzed the expression of the glucose transporters GLUT1, GLUT2, and GLUT3 with regard to the histological and clinical factors by performing immunohistochemistry on the primary tumors of n = 33 UM patients. UMs with monosomy-3 exhibited a 57% lower immunoreactivity for GLUT2 and a 1.8×-fold higher ratio of GLUT1 to total GLUT1-3. The combined levels of GLUT1-3 proteins were reduced in the irradiated but not the non

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42

Aghayan, M., L. V. Rao, R. M. Smith, et al. "Developmental expression and cellular localization of glucose transporter molecules during mouse preimplantation development." Development 115, no. 1 (1992): 305–12. http://dx.doi.org/10.1242/dev.115.1.305.

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Two general mechanisms mediate glucose transport, one is a sodium-coupled glucose transporter found in the apical border of intestinal and kidney epithelia, while the other is a sodium-independent transport system. Of the latter, several facilitated transporters have been identified, including GLUT1 (erythrocyte/brain), GLUT2 (liver) and GLUT4 (adipose/muscle) isoforms. In this study, we used Western-blot analysis and high resolution immunoelectron microscopy (IEM) to investigate the stage-related expression and cellular localization of GLUT1, 2 and 4. The Western blot results demonstrate that

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Mohani, Chandra Irwanadi, Achmad Rudijanto, Aulanni’am ., and Setyawati Soeharto. "DLBS3233 reduces inflammatory marker on kidney by increasing expression GLUT1 and GLUT2 in diabetic rats." F1000Research 11 (August 23, 2022): 976. http://dx.doi.org/10.12688/f1000research.123091.1.

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Introduction: Diabetic kidney disease (DKD), as a diabetes mellitus type 2 (DMT2) complications, is getting more prevalent nowadays. Inflammation is one of the renal injury mechanisms evaluated through the surge in in TNF-α and NF-κβ expression. Impaired expression of gluten transporter 1 (GLUT1) and GLUT2 reduces glucose uptake. DBLS3233 is a novel anti-diabetes agent and Indonesian herbal product responsible for glucose control and upregulation of insulin signal transduction. We performed an experiment on DLBS3233 to examine the response of TNF-α and NF-κβ and the expression of GLUT 1 and GL

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Coudert, Edouard, Géraldine Pascal, Joëlle Dupont, et al. "Phylogenesis and Biological Characterization of a New Glucose Transporter in the Chicken (Gallus gallus), GLUT12." PLOS ONE 10, no. 10 (2015): e0139517. http://dx.doi.org/10.1371/journal.pone.0139517.

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Flessner, Lauren B., and Kelle H. Moley. "Similar [DE]XXXL[LI] Motifs Differentially Target GLUT8 and GLUT12 in Chinese Hamster Ovary Cells." Traffic 10, no. 3 (2009): 324–33. http://dx.doi.org/10.1111/j.1600-0854.2008.00866.x.

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Matsuzaka, Takashi, and Hitoshi Shimano. "GLUT12: a second insulin-responsive glucose transporters as an emerging target for type 2 diabetes." Journal of Diabetes Investigation 3, no. 2 (2011): 130–31. http://dx.doi.org/10.1111/j.2040-1124.2011.00177.x.

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Dominguez, J. H., K. Camp, L. Maianu, and W. T. Garvey. "Glucose transporters of rat proximal tubule: differential expression and subcellular distribution." American Journal of Physiology-Renal Physiology 262, no. 5 (1992): F807—F812. http://dx.doi.org/10.1152/ajprenal.1992.262.5.f807.

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In the late proximal tubule, glucose reabsorption progressively lowers the concentration of luminal glucose, and concentrative glucose influx increases to ensure complete glucose reabsorption. The change in glucose influx is effected by luminal Na(+)-dependent glucose transporters (Na(+)-GLUT), which exhibit higher Na(+)-to-glucose stoichiometric ratios in the late proximal tubule. In this work, the corresponding changes in the axial distribution of basolateral glucose efflux transporters (GLUTs) were examined. mRNAs encoding high-affinity facilitative basolateral transporter GLUT1, low-affini

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Pujol-Giménez, Jonai, Jaione Barrenetxe, Pedro González-Muniesa, and Maria Pilar Lostao. "The facilitative glucose transporter GLUT12: what do we know and what would we like to know?" Journal of Physiology and Biochemistry 69, no. 2 (2012): 325–33. http://dx.doi.org/10.1007/s13105-012-0213-8.

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Macheda, Maria, Darren Kelly, James Best, and Suzanne Rogers. "Expression during rat fetal development of GLUT12 - a member of the class III hexose transporter family." Anatomy and Embryology 205, no. 5-6 (2002): 441–52. http://dx.doi.org/10.1007/s00429-002-0263-8.

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Macheda, Maria L., Darren J. Kelly, James D. Best, and Suzanne Rogers. "Expression during rat fetal development of GLUT12 – a member of the class III hexose transporter family." Anatomy and Embryology 206, no. 4 (2003): 335. http://dx.doi.org/10.1007/s00429-002-0303-4.

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