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Journal articles on the topic 'GLUT-6'

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Published: 4 June 2025

Last updated: 1 August 2025

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1

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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2

Navarrete Santos, Anne, Sarah Tonack, Michaela Kirstein, Silke Kietz, and Bernd Fischer. "Two insulin-responsive glucose transporter isoforms and the insulin receptor are developmentally expressed in rabbit preimplantation embryos." Reproduction 128, no. 5 (2004): 503–16. http://dx.doi.org/10.1530/rep.1.00203.

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Glucose is the most important energy substrate for mammalian blastocysts. Its uptake is mediated by glucose transporters (GLUT). In muscle and adipocyte cells insulin stimulates glucose uptake by activation of the insulin receptor (IR) pathway and translocation of GLUT4. GLUT4 is expressed in bovine preimplantation embryos. A new insulin-responsive isoform, GLUT8, was recently described in mouse blastocysts. Thus, potentially, two insulin-responsive isoforms are expressed in early embryos. The mechanism of insulin action on embryonic cells, however, is still not clear. In the present study exp

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3

Rana, Natasha, Marwa A. Aziz, Ahmed K. Oraby, et al. "Towards Selective Binding to the GLUT5 Transporter: Synthesis, Molecular Dynamics and In Vitro Evaluation of Novel C-3-Modified 2,5-Anhydro-D-mannitol Analogs." Pharmaceutics 14, no. 4 (2022): 828. http://dx.doi.org/10.3390/pharmaceutics14040828.

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Deregulation and changes in energy metabolism are emergent and important biomarkers of cancer cells. The uptake of hexoses in cancer cells is mediated by a family of facilitative hexose membrane-transporter proteins known as Glucose Transporters (GLUTs). In the clinic, numerous breast cancers do not show elevated glucose metabolism (which is mediated mainly through the GLUT1 transporter) and may use fructose as an alternative energy source. The principal fructose transporter in most cancer cells is GLUT5, and its mRNA was shown to be elevated in human breast cancer. This offers an alternative

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4

Colville, C. A., M. J. Seatter, and G. W. Gould. "Analysis of the structural requirements of sugar binding to the liver, brain and insulin-responsive glucose transporters expressed in oocytes." Biochemical Journal 294, no. 3 (1993): 753–60. http://dx.doi.org/10.1042/bj2940753.

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We have expressed the liver (GLUT 2), brain (GLUT 3) and insulin-responsive (GLUT 4) glucose transporters in oocytes from Xenopus laevis by microinjection of in vitro-transcribed mRNA. Using a range of halogeno- and deoxy-glucose analogues, and other hexoses, we have studied the structural basis of sugar binding to these different isoforms. We show that a hydrogen bond to the C-3 position is involved in sugar binding for all three isoforms, but that the direction of this hydrogen bond is different in GLUT 2 from either GLUT 1, 3 or 4. Hydrogen-bonding at the C-4 position is also involved in su

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5

Chin, Edward, A. Musa Zamah, Daniel Landau, et al. "Changes in Facilitative Glucose Transporter Messenger Ribonucleic Acid Levels in the Diabetic Rat Kidney*." Endocrinology 138, no. 3 (1997): 1267–75. http://dx.doi.org/10.1210/endo.138.3.5015.

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Abstract Facilitative glucose transporter (GLUTs 1, 2, 4, and 5) messenger RNAs (mRNAs) are differentially distributed in the rat nephron: GLUT1 is widely expressed, GLUT4 is selectively concentrated in thick ascending limbs, and GLUT2 and 5 are exclusively localized in proximal tubules, consistent with differential roles for these transporters in renal glucose handling. In the present study, quantitative in situ hybridization was used to evaluate changes in these mRNA levels during acute (2 and 7 days) and chronic (30, 90, and 180 days) streptozotocin-induced diabetes mellitus (STZ-DM). Medul

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6

Navarrete Santos, Anne, Sarah Tonack, Michaela Kirstein, Marie Pantaleon, Peter Kaye, and Bernd Fischer. "Insulin acts via mitogen-activated protein kinase phosphorylation in rabbit blastocysts." Reproduction 128, no. 5 (2004): 517–26. http://dx.doi.org/10.1530/rep.1.00204.

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The addition of insulin during in vitro culture has beneficial effects on rabbit preimplantation embryos leading to increased cell proliferation and reduced apoptosis. We have previously described the expression of the insulin receptor (IR) and the insulin-responsive glucose transporters (GLUT) 4 and 8 in rabbit preimplantation embryos. However, the effects of insulin on IR signaling and glucose metabolism have not been investigated in rabbit embryos. In the present study, the effects of 170 nM insulin on IR, GLUT4 and GLUT8 mRNA levels, Akt and Erk phosphorylation, GLUT4 translocation and met

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7

Metzger, Shulamit, Samir Nusair, David Planer та ін. "Inhibition of Hepatic Gluconeogenesis and Enhanced Glucose Uptake Contribute to the Development of Hypoglycemia in Mice Bearing Interleukin-1β- Secreting Tumor". Endocrinology 145, № 11 (2004): 5150–56. http://dx.doi.org/10.1210/en.2004-0323.

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Abstract Mice bearing IL-1β-secreting tumor were used to study the chronic effect of IL-1β on glucose metabolism. Mice were injected with syngeneic tumor cells transduced with the human IL-1β gene. Serum IL-1β levels increased exponentially with time. Secretion of IL-1β from the developed tumors was associated with decreased food consumption, reduced body weight, and reduced blood glucose levels. Body composition analysis revealed that IL-1β caused a significant loss in fat tissue without affecting lean body mass and water content. Hepatic phosphoenolpyruvate carboxykinase and glucose-6-phosph

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8

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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9

Ortiz, P. A., and H. C. Haspel. "Differential control of the functional cell surface expression and content of hexose transporter GLUT-1 by glucose and glucose metabolism in murine fibroblasts." Biochemical Journal 295, no. 1 (1993): 67–72. http://dx.doi.org/10.1042/bj2950067.

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The present paper evaluates the contributions of glucose and its metabolites to the post-translational regulation of hexose transport and GLUT-1 content in murine fibroblasts. The effects of 3-O-methylglucose, a nearly non-metabolizable glucose analogue, on 2-deoxyglucose-uptake, cell-surface expression and content of GLUT-1, glucose 6-phosphate levels, and phosphoglucose isomerase (PGI) and hexokinase activities of murine fibroblasts were compared with those of glucose and fructose. Glucose (EC50 approximately 6 mM) or 3-O-methylglucose (EC50 approximately 12 mM), which are substrates of GLUT

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10

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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11

Haber, R. S., C. M. Wilson, S. P. Weinstein, A. Pritsker, and S. W. Cushman. "Thyroid hormone increases the partitioning of glucose transporters to the plasma membrane in ARL 15 cells." American Journal of Physiology-Endocrinology and Metabolism 269, no. 3 (1995): E605—E610. http://dx.doi.org/10.1152/ajpendo.1995.269.3.e605.

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The stimulation of glucose transport by 3,5,3'-triiodo-L-thyronine (T3) in the liver-derived ARL 15 cell line is only partly attributable to increased GLUT-1 glucose transporter gene expression. To test the hypothesis that T3 increases the partitioning of GLUT-1 to the cell surface, we quantitated surface GLUT-1 using the photolabel ATB-[3H]BMPA. In control cells only approximately 20% of total cellular GLUT-1 was present at the cell surface. T3 treatment (100 nM) for 6 h increased the rate of 2-deoxy-[3H]glucose (2-DG) uptake by 30, 92, and 95% in three experiments and increased surface GLUT-

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12

Hogan, A., S. Heyner, M. J. Charron, et al. "Glucose transporter gene expression in early mouse embryos." Development 113, no. 1 (1991): 363–72. http://dx.doi.org/10.1242/dev.113.1.363.

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The glucose transporter (GLUT) isoforms responsible for glucose uptake in early mouse embryos have been identified. GLUT 1, the isoform present in nearly every tissue examined including adult brain and erythrocytes, is expressed throughout preimplantation development. GLUT 2, which is normally present in adult liver, kidney, intestine and pancreatic beta cells is expressed from the 8-cell stage onward. GLUT 4, an insulin-recruitable isoform, which is expressed in adult fat and muscle, is not expressed at any stage of preimplantation development or in early postimplantation stage embryos. Genet

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13

Reijrink, Melanie, Stefanie A. de Boer, Ines F. Antunes, et al. "[18F]FDG Uptake in Adipose Tissue Is Not Related to Inflammation in Type 2 Diabetes Mellitus." Molecular Imaging and Biology 23, no. 1 (2020): 117–26. http://dx.doi.org/10.1007/s11307-020-01538-0.

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Abstract Purpose 2-deoxy-2-[18F]fluoro-d-glucose ([18F]FDG) uptake is a marker of metabolic activity and is therefore used to measure the inflammatory state of several tissues. This radionuclide marker is transported through the cell membrane via glucose transport proteins (GLUTs). The aim of this study is to investigate whether insulin resistance (IR) or inflammation plays a role in [18F]FDG uptake in adipose tissue (AT). Procedures This study consisted of an in vivo clinical part and an ex vivo mechanistic part. In the clinical part, [18F]FDG uptake in abdominal visceral AT (VAT) and subcuta

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14

Purwanto, Bambang, Sundari Indah Wiyasihati, Putri Ayu Masyitha, Kristanti Wanito Wigati, and Irfiansyah Irwadi. "Golden sea cucumber extract revives glucose transporter-4 and interleukin-6 protein level in diabetic mouse muscle." Veterinary World 12, no. 5 (2019): 684–88. http://dx.doi.org/10.14202/vetworld.2019.684-688.

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Background: Streptozotocin (STZ)-induced free radical oxidant activity resulted in muscle wasting due to protein carbonyl (PC), glucose transporter-4 (Glut-4), and interleukin-6 (IL-6) protein alteration. Antioxidant ingredient in the golden sea cucumber extract was found in promising level to inhibit free radical activity. Aim: This study was aimed to investigate the effect of golden sea cucumber extract on PC, IL-6, and Glut-4 level of STZ-induced diabetes mouse. Materials and Methods: This study was performed using mice, which were grouped into non-diabetes, diabetes, and diabetes-treated e

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15

Kandror, K. V., and P. F. Pilch. "Compartmentalization of protein traffic in insulin-sensitive cells." American Journal of Physiology-Endocrinology and Metabolism 271, no. 1 (1996): E1—E14. http://dx.doi.org/10.1152/ajpendo.1996.271.1.e1.

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Insulin-sensitive cells, adipocytes and myocytes, translocate a number of intracellular proteins to the cell surface in response to insulin. Among these proteins are glucose transporters 1 and 4 (GLUT-1 and GLUT-4, respectively), receptors for insulin-like growth factor II (IGF-II)/mannose 6-phosphate (Man-6-P) and transferrin, the aminopeptidase gp 160, caveolin, and a few others. In the case of insulin-activated glucose transport, this translocation has been proven to be the major, if not the only regulatory mechanism of this process. It seems likely that the cell surface recruitment of the

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16

Hwang, Daw-Yang, and Faramarz Ismail-Beigi. "Stimulation of GLUT-1 glucose transporter expression in response to hyperosmolarity." American Journal of Physiology-Cell Physiology 281, no. 4 (2001): C1365—C1372. http://dx.doi.org/10.1152/ajpcell.2001.281.4.c1365.

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Glucose transporter isoform-1 (GLUT-1) expression is stimulated in response to stressful conditions. Here we examined the mechanisms mediating the enhanced expression of GLUT-1 by hyperosmolarity. GLUT-1 mRNA, GLUT-1 protein, and glucose transport increased after exposure of Clone 9 cells to 600 mosmol/l (produced by addition of mannitol). The stimulation of glucose transport was biphasic: in the early phase (0–6 h) a ∼2.5-fold stimulation of glucose uptake was associated with no change in the content of GLUT-1 mRNA, GLUT-1 protein, or GLUT-1 in the plasma membrane, whereas the ∼17-fold stimul

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17

Lin, Baozhen, Sean Coughlin, and Paul F. Pilch. "Bidirectional regulation of uncoupling protein-3 and GLUT-4 mRNA in skeletal muscle by cold." American Journal of Physiology-Endocrinology and Metabolism 275, no. 3 (1998): E386—E391. http://dx.doi.org/10.1152/ajpendo.1998.275.3.e386.

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To elucidate the possible role of the mitochondrial uncoupling protein (UCP)-3 in skeletal muscle as a regulator of adaptive thermogenesis and energy balance, we examined the modulation by cold exposure (5°C) of UCP-3 and glucose transporter isoform GLUT-4 mRNAs in male Sprague-Dawley rats. In skeletal muscle, UCP-3 and GLUT-4 mRNAs increased two- to threefold between 6 and 24 h of cold exposure and then decreased to 50% of the control value after 6 days in the cold. In contrast, skeletal muscle UCP-2 mRNA showed a small increase on day 3 and returned to normal after 6 days. The bidirectional

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18

Ehrhardt, R. A., and A. W. Bell. "Developmental increases in glucose transporter concentration in the sheep placenta." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 273, no. 3 (1997): R1132—R1141. http://dx.doi.org/10.1152/ajpregu.1997.273.3.r1132.

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To explore the molecular basis for the gestational increase in glucose transport capacity of the sheep placenta in vivo, placentas from twin-pregnant ewes at days 75, 110, and 140 postcoitus (n = 6/group) were analyzed for glucose transporter (GT) concentration. Concentration (pmol/mg protein) of D-glucose-inhibitable binding sites, measured by [3H]cytochalasin B binding analysis, increased 3.4 times from mid- to late pregnancy. Concurrently, abundance of GLUT-1 and GLUT-3 protein, measured by immunoblotting with specific polyclonal antibodies, increased 2.3 and 2.9 times, respectively, while

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19

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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Levitsky, L. L., Q. Zheng, K. Mink, and D. B. Rhoads. "GLUT-1 and GLUT-2 mRNA, protein, and glucose transporter activity in cultured fetal and adult hepatocytes." American Journal of Physiology-Endocrinology and Metabolism 267, no. 1 (1994): E88—E94. http://dx.doi.org/10.1152/ajpendo.1994.267.1.e88.

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To understand glycogenesis in the fetal hepatocyte, we examined glucose transport in cultured fetal and adult male rat hepatocytes. GLUT-1 mRNA was detected in fetal hepatocytes at isolation but in adult hepatocytes only after culture. GLUT-1 mRNA was more abundant in fetal than in adult hepatocytes (P < 0.005). GLUT-1 protein paralleled its message. GLUT-2 mRNA was more abundant in adult than in fetal hepatocytes (P < 0.05), and abundance did not change during culture, but GLUT-2 protein was discordantly regulated. There was more GLUT-2 protein in fetal hepatocytes at 45 h (P < 0.025

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Taouis, Mohammed, Carine Dagou, Céline Ster, Georges Durand, Michèle Pinault, and Jacques Delarue. "n-3 Polyunsaturated fatty acids prevent the defect of insulin receptor signaling in muscle." American Journal of Physiology-Endocrinology and Metabolism 282, no. 3 (2002): E664—E671. http://dx.doi.org/10.1152/ajpendo.00320.2001.

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A high-fat diet containing polyunsaturated fatty acids (PUFA: n-3 or n-6) given for 4 wk to 5-wk-old male Wistar rats induced a clear hyperglycemia (10.4 ± 0.001 mmol/l for n-6 rats and 10.1 ± 0.001 for n-3 rats) and hyperinsulinemia (6.6 ± 0.8 ng/ml for n-6 rats and 6.4 ± 1.3 for n-3 rats), signs of insulin resistance. In liver, both diets (n-3 and n-6) significantly reduced insulin receptor (IR) number, IR and IR substrate (IRS)-1 tyrosine phosphorylation, and phosphatidylinositol (PI) 3′-kinase activity. In contrast, in leg muscle, IR density, as determined by Western blotting, was not affe

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22

Marshall, Bess Adkins, Polly A. Hansen, Nancy J. Ensor, M. Allison Ogden, and Mike Mueckler. "GLUT-1 or GLUT-4 transgenes in obese mice improve glucose tolerance but do not prevent insulin resistance." American Journal of Physiology-Endocrinology and Metabolism 276, no. 2 (1999): E390—E400. http://dx.doi.org/10.1152/ajpendo.1999.276.2.e390.

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Insulin-stimulated glucose uptake is defective in patients with type 2 diabetes. To determine whether transgenic glucose transporter overexpression in muscle can prevent diabetes induced by a high-fat, high-sugar diet, singly (GLUT-1, GLUT-4) and doubly (GLUT-1 and -4) transgenic mice were placed on a high-fat, high-sugar diet or a standard chow diet. On the high-fat, high-sugar diet, wild-type but not transgenic mice developed fasting hyperglycemia and glucose intolerance (peak glucose of 337 ± 19 vs. 185–209 mg/dl in the same groups on the high-fat, high-sugar diet and 293 ± 13 vs. 166–194 m

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23

Burcelin, R., M. Eddouks, J. Kande, R. Assan, and J. Girard. "Evidence that GLUT-2 mRNA and protein concentrations are decreased by hyperinsulinaemia and increased by hyperglycaemia in liver of diabetic rats." Biochemical Journal 288, no. 2 (1992): 675–79. http://dx.doi.org/10.1042/bj2880675.

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GLUT-2, glucokinase (GK) and phosphoenolpyruvate carboxykinase (PEPCK) mRNA expression was studied in the liver of chronically catheterized diabetic rats during the 3 days after an intravenous injection of 65 mg of streptozotocin (STZ)/kg. At 6 h after the STZ injection, portal plasma insulin levels were 270 +/- 32 mu-units/ml and blood glucose was 1.4 +/- 0.4 mmol/l, owing to pancreatic beta-cell destruction. GLUT-2 and PEPCK mRNA concentrations were rapidly and dramatically decreased (> 90%), whereas GK mRNA was increased. After 30 h, plasma insulin concentrations were lower than 5 mu-uni

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Karim, Sumera, Evaggelia Liaskou, Janine Fear, et al. "Dysregulated hepatic expression of glucose transporters in chronic disease: contribution of semicarbazide-sensitive amine oxidase to hepatic glucose uptake." American Journal of Physiology-Gastrointestinal and Liver Physiology 307, no. 12 (2014): G1180—G1190. http://dx.doi.org/10.1152/ajpgi.00377.2013.

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Insulin resistance is common in patients with chronic liver disease (CLD). Serum levels of soluble vascular adhesion protein-1 (VAP-1) are also increased in these patients. The amine oxidase activity of VAP-1 stimulates glucose uptake via translocation of transporters to the cell membrane in adipocytes and smooth muscle cells. We aimed to document human hepatocellular expression of glucose transporters (GLUTs) and to determine if VAP-1 activity influences receptor expression and hepatic glucose uptake. Quantitative PCR and immunocytochemistry were used to study human liver tissue and cultured

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Zhou, Min, Gino Vallega, Konstantin V. Kandror, and Paul F. Pilch. "Insulin-mediated translocation of GLUT-4-containing vesicles is preserved in denervated muscles." American Journal of Physiology-Endocrinology and Metabolism 278, no. 6 (2000): E1019—E1026. http://dx.doi.org/10.1152/ajpendo.2000.278.6.e1019.

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Skeletal muscle denervation decreases insulin-sensitive glucose uptake into this tissue as a result of marked GLUT-4 protein downregulation (∼20% of controls). The process of insulin-stimulated glucose transport in muscle requires the movement or translocation of intracellular GLUT-4-rich vesicles to the cell surface, and it is accompanied by the translocation of several additional vesicular cargo proteins. Thus examining GLUT-4 translocation in muscles from denervated animals allows us to determine whether the loss of a major cargo protein, GLUT-4, affects the insulin-dependent behavior of th

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COHEN, Naomi R., David A. KNECHT, and Harvey F. LODISH. "Functional expression of rat GLUT 1 glucose transporter in Dictyostelium discoideum." Biochemical Journal 315, no. 3 (1996): 971–75. http://dx.doi.org/10.1042/bj3150971.

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To facilitate expression of the rat GLUT 1 glucose transporter cDNA in Dictyostelium discoideum, we mutated the 5´ end of the coding sequence such that the codons for the first ten amino acids conformed to preferred Dictyostelium codon usage. As determined by Western-blot analysis, a population of Dictyostelium transformed with the mutated cDNA expressed non-glycosylated GLUT 1 protein. Cell lines expressing GLUT 1 transport radiolabelled 2-deoxy-D-glucose at a rate 6–10 times that of cell lines transformed with vector alone. The initial rate of inward transport of 2-deoxy-D-glucose was stimul

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Leturque, A., C. Postic, P. Ferre, and J. Girard. "Nutritional regulation of glucose transporter in muscle and adipose tissue of weaned rats." American Journal of Physiology-Endocrinology and Metabolism 260, no. 4 (1991): E588—E593. http://dx.doi.org/10.1152/ajpendo.1991.260.4.e588.

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The role of glucose transporters GLUT-1 and GLUT-4 in the development of insulin sensitivity at weaning in rat skeletal muscles and adipose tissue was studied in relation to the nutritional changes when suckling rats shift from a high-fat (HF) to a high-carbohydrate (HCHO) diet. Insulin stimulated the translocation of GLUT-4 protein from an intracellular pool to the plasma membrane in adipocytes from suckling and HCHO- or HF-weaned rats. The GLUT-4 protein and the insulin stimulation were threefold higher in adipocytes from HCHO-weaned rats than in suckling or HF-weaned rats. GLUT-4 mRNA and p

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Kuo, C. H., Z. Ding, and J. L. Ivy. "Interaction of exercise training and clenbuterol on GLUT-4 protein in muscle of obese Zucker rats." American Journal of Physiology-Endocrinology and Metabolism 271, no. 5 (1996): E847—E854. http://dx.doi.org/10.1152/ajpendo.1996.271.5.e847.

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Chronic administration of clenbuterol, a beta 2-adrenergic agonist, attenuates the exercise training-induced improvement in muscle insulin resistance of the obese Zucker rat. The present study was conducted to determine whether clenbuterol also attenuates the increase in muscle GLUT-4 protein that occurs with exercise training and whether the action of clenbuterol is related to its ability to downregulate the beta-adrenergic receptors. Female obese Zucker rats were randomly assigned to one of the following four groups: control (CON, n = 7), clenbuterol (CL, n = 8), exercise training (TR, n = 8

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Buglio, Daniela, Wendy Schober, Rooha Contractor, et al. "High Glucose Activates AKT Signaling and Induces Upregulation of Genes Encoding Glycolytic Enzymes Glut-1 and HK-2 in Acute Lymphocytic Leukemia." Blood 104, no. 11 (2004): 2049. http://dx.doi.org/10.1182/blood.v104.11.2049.2049.

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Abstract Background: Hyperglycemia represents a common side effect of steroid therapy and is not uncommon during treatment of patients with acute lymphocytic leukemia (ALL). Our recent retrospective study in 278 adult patients with ALL demonstrated that hyperglycemia during induction chemotherapy occurred in up to 37% of patients and was associated with a shorter median complete remission duration and a shorter median survival (Cancer 2004 Mar 15;100(6):1179–85). The serine/threonine AKT, a major downstream PI3K target, promotes continued cell growth and metabolism by increasing glucose uptake

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LOON, Luc J. C. VAN, Robyn MURPHY, Audrey M. OOSTERLAAR, et al. "Creatine supplementation increases glycogen storage but not GLUT-4 expression in human skeletal muscle." Clinical Science 106, no. 1 (2004): 99–106. http://dx.doi.org/10.1042/cs20030116.

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It has been speculated that creatine supplementation affects muscle glucose metabolism in humans by increasing muscle glycogen storage and up-regulating GLUT-4 protein expression. In the present study, we assessed the effects of creatine loading and prolonged supplementation on muscle glycogen storage and GLUT-4 mRNA and protein content in humans. A total of 20 subjects participated in a 6-week supplementation period during which creatine or a placebo was ingested. Muscle biopsies were taken before and after 5 days of creatine loading (20 g·day-1) and after 6 weeks of continued supplementation

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Corpe, C. P., and C. F. Burant. "Hexose transporter expression in rat small intestine: effect of diet on diurnal variations." American Journal of Physiology-Gastrointestinal and Liver Physiology 271, no. 1 (1996): G211—G216. http://dx.doi.org/10.1152/ajpgi.1996.271.1.g211.

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In rodents, a number of intestinal digestive and absorptive processes demonstrate a diurnal pattern of activity. To investigate if the jejunal hexose transporters are regulated in such a diurnal fashion, the levels for the glucose and fructose transporter mRNA and proteins were determined at 6-h intervals over a 24-h control fed period. SGLT-1, GLUT-2, and GLUT-5 mRNA levels increased between two- and eightfold before the onset of peak feeding. GLUT-5 protein levels also varied in a diurnal fashion but were out of phase with the observed changes in GLUT-5 mRNA levels. In contrast, GLUT-2 prote

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Ren, J. M., C. F. Semenkovich, and J. O. Holloszy. "Adaptation of muscle to creatine depletion: effect on GLUT-4 glucose transporter expression." American Journal of Physiology-Cell Physiology 264, no. 1 (1993): C146—C150. http://dx.doi.org/10.1152/ajpcell.1993.264.1.c146.

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Feeding rats beta-guanidinopropionic acid (beta-GPA), a creatine analogue, results in depletion of creatine and phosphocreatine and induces increases in mitochondrial oxidative enzymes and hexokinase in skeletal muscle. Comparisons of different muscle types and studies of the adaptation to exercise suggest that 1) the levels of the insulin-responsive glucose transporter (GLUT-4), mitochondrial oxidative enzymes, and hexokinase may be coregulated and 2) GLUT-4 content can determine maximal glucose transport activity in muscle. To further evaluate these possibilities, we examined the effects of

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Zhou, Min, Lidia Sevilla, Gino Vallega, et al. "Insulin-dependent protein trafficking in skeletal muscle cells." American Journal of Physiology-Endocrinology and Metabolism 275, no. 2 (1998): E187—E196. http://dx.doi.org/10.1152/ajpendo.1998.275.2.e187.

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We have established a simple procedure for the separation of intracellular pool(s) of glucose transporter isoform GLUT-4-containing vesicles from the surface sarcolemma and T tubule membranes of rat skeletal myocytes. This procedure enabled us to immunopurify intracellular GLUT-4-containing vesicles and to demonstrate that 20–30% of the receptors for insulin-like growth factor II/mannose 6-phosphate and transferrin are colocalized with GLUT-4 in the same vesicles. Using our new fractionation procedure as well as cell surface biotinylation, we have shown that these receptors are translocated fr

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McCoy, M., J. Proietto, and M. Hargreaves. "Skeletal muscle GLUT-4 and postexercise muscle glycogen storage in humans." Journal of Applied Physiology 80, no. 2 (1996): 411–15. http://dx.doi.org/10.1152/jappl.1996.80.2.411.

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The purpose of this study was to examine the relationship between skeletal muscle GLUT-4 protein and postexercise glycogen storage in human subjects fed adequate carbohydrate. Eleven men completed 2 h of cycling, and a biopsy of the vastus lateralis was performed immediately after exercise cessation for the determination of muscle GLUT-4 protein and glycogen concentrations, glycogen synthase activity, and citrate synthase activity. The subjects ingested meals providing 2.0 g carbohydrate/kg body weight at 0, 2, and 4 h postexercise, and a second biopsy was performed 6 h postexercise. Muscle gl

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Ishihara, H., T. Asano, H. Katagiri, et al. "Expression of GLUT-4 glucose transporter in unweighted soleus muscle of normal and STZ-induced diabetic rats." American Journal of Physiology-Endocrinology and Metabolism 264, no. 2 (1993): E301—E307. http://dx.doi.org/10.1152/ajpendo.1993.264.2.e301.

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Effects of 6 days of hindlimb suspension on expression of glucose transporters were studied in the skeletal muscle of nondiabetic and streptozotocin-induced diabetic rats. Although total membrane protein recovered from soleus muscles tended to decrease with suspension, GLUT-4 protein concentration (amount per gram membrane protein) was increased by 66 and 91% compared with weight-bearing control in nondiabetic and diabetic rats, respectively. Therefore, the amount of GLUT-4 protein in whole soleus muscle did not decrease with the hindlimb suspension in normal and diabetic rats. In contrast, hi

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Lee, A. D., P. A. Hansen, J. Schluter, E. A. Gulve, J. Gao, and J. O. Holloszy. "Effects of epinephrine on insulin-stimulated glucose uptake and GLUT-4 phosphorylation in muscle." American Journal of Physiology-Cell Physiology 273, no. 3 (1997): C1082—C1087. http://dx.doi.org/10.1152/ajpcell.1997.273.3.c1082.

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beta-Adrenergic stimulation has been reported to inhibit insulin-stimulated glucose transport in adipocytes. This effect has been attributed to a decrease in the intrinsic activity of the GLUT-4 isoform of the glucose transporter that is mediated by phosphorylation of GLUT-4. Early studies showed no inhibition of insulin-stimulated glucose transport by epinephrine in skeletal muscle. The purpose of this study was to determine the effect of epinephrine on GLUT-4 phosphorylation, and reevaluate the effect of beta-adrenergic stimulation on insulin-activated glucose transport, in skeletal muscle.

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Cao, Heping, and Kandan Sethumadhavan. "Plant Polyphenol Gossypol Induced Cell Death and Its Association with Gene Expression in Mouse Macrophages." Biomolecules 13, no. 4 (2023): 624. http://dx.doi.org/10.3390/biom13040624.

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Gossypol is a complex plant polyphenol reported to be cytotoxic and anti-inflammatory, but little is known about its effect on gene expression in macrophages. The objective of this study was to explore gossypol’s toxicity and its effect on gene expression involved in the inflammatory response, glucose transport and insulin signaling pathways in mouse macrophages. Mouse RAW264.7 macrophages were treated with multiple concentrations of gossypol for 2–24 h. Gossypol toxicity was estimated by MTT assay and soluble protein content. qPCR analyzed the expression of anti-inflammatory tristetraprolin f

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Burcelin, R., R. L. Printz, J. Kande, R. Assan, D. K. Granner, and J. Girard. "Regulation of glucose transporter and hexokinase II expression in tissues of diabetic rats." American Journal of Physiology-Endocrinology and Metabolism 265, no. 3 (1993): E392—E401. http://dx.doi.org/10.1152/ajpendo.1993.265.3.e392.

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Glucose transport and phosphorylation are decreased in muscle and adipose tissue in diabetes mellitus. The glucose transporter GLUT-4 and hexokinase II (HK II) are the main isoforms of proteins involved in glucose transport and phosphorylation in insulin-sensitive tissues, adipose tissue, skeletal muscle, and heart. The molecular mechanisms responsible for the decrease of glucose transport and phosphorylation have been studied during the first 3 days after streptozotocin (STZ) administration in adult male Wistar rats. GLUT-4 mRNA and protein and HK II mRNA and enzyme activity were measured. Af

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Youngren, J. F., and R. J. Barnard. "Effects of acute and chronic exercise on skeletal muscle glucose transport in aged rats." Journal of Applied Physiology 78, no. 5 (1995): 1750–56. http://dx.doi.org/10.1152/jappl.1995.78.5.1750.

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The purpose of this study was to investigate the effects of acute and chronic exercise on skeletal muscle glucose transport in aged rats by using an isolated sarcolemmal membrane preparation. In 24-mo-old female Fischer 344 rats, a maximum dose of insulin increased glucose transport from 43 +/- 6 to 82 +/- 6 pmol.mg protein-1.15 s-1. A 45-min bout of exhaustive treadmill running increased glucose transport to the same maximum level (88 +/- 5 pmol.mg protein-1.15 s-1). Eight weeks of progressive exercise training resulted in a 65% increase in succinic dehydrogenase activity in hindlimb muscles

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Greco-Perotto, R., E. Wertheimer, B. Jeanrenaud, E. Cerasi, and S. Sasson. "Glucose regulates its transport in L8 myocytes by modulating cellular trafficking of the transporter GLUT-1." Biochemical Journal 286, no. 1 (1992): 157–63. http://dx.doi.org/10.1042/bj2860157.

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The effect of culture conditions simulating hypo- and hyper-glycaemia on glucose transport and on the subcellular localization of the glucose transporter GLUT-1 was studied in L8 myocytes. Incubation of the cells with 20 mM-glucose for 25 h decreased the rate of 2-deoxy-D-[3H]glucose (dGlc) uptake to 0.106 +/- 0.016 nmol/min per 10(6) cells compared with 0.212 +/- 0.025 in cells maintained at 2 mM-glucose (final glucose concentrations at the end of the incubation period were 16-17 mM and 0.7-1.0 mM respectively). An additional 5 h incubation of these cells with medium containing the opposite g

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Kamga-Simo, F. D. Y., G. P. Kamatou, C. Ssemakalu, and L. J. Shai. "Cassia Abbreviata Enhances Glucose Uptake and Glucose Transporter 4 Translocation in C2C12 Mouse Skeletal Muscle Cells." Journal of Evidence-Based Integrative Medicine 26 (January 1, 2021): 2515690X2110063. http://dx.doi.org/10.1177/2515690x211006333.

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Background. This study aim at assessing C. abbreviata aqueous extracts for its potential to exhibit anti-diabetic activity in skeletal muscle cells. In addition to the toxicological and glucose absorption studies, the action of C. abbreviata extracts on some major genes involved in the insulin signaling pathway was established. Methods. The in vitro cytotoxic effects C. abbreviata was evaluated on muscle cells using the MTT assay and the in vitro glucose uptake assay conducted using a modified glucose oxidase method described by Van de Venter et al. (2008). The amount of GLUT-4 on cell surface

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AFZAL, Iram, Philip CUNNINGHAM, and Richard J. NAFTALIN. "Interactions of ATP, oestradiol, genistein and the anti-oestrogens, faslodex (ICI 182780) and tamoxifen, with the human erythrocyte glucose transporter, GLUT1." Biochemical Journal 365, no. 3 (2002): 707–19. http://dx.doi.org/10.1042/bj20011624.

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17β-Oestradiol (ED when subscript to K) and the phytoestrogen isoflavone genistein (GEN) inhibit glucose transport in human erythrocytes and erythrocyte ghosts. The selective oestrogen receptor modulators or anti-oestrogens, faslodex (ICI 182780) (FAS) and tamoxifen (TAM), competitively antagonize oestradiol inhibition of glucose exit from erythrocytes (Ki(ED/FAS) = 2.84±0.16μM and Ki(ED/TAM) = 100±2nM). Faslodex has no significant inhibitory effect on glucose exit, but tamoxifen alone inhibits glucose exit (Ki(TAM) = 300±100nM). In ghosts, ATP (1–4mM) competitively antagonizes oestradiol, gen

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Shetty, M., J. N. Loeb, and F. Ismail-Beigi. "Enhancement of glucose transport in response to inhibition of oxidative metabolism: pre- and posttranslational mechanisms." American Journal of Physiology-Cell Physiology 262, no. 2 (1992): C527—C532. http://dx.doi.org/10.1152/ajpcell.1992.262.2.c527.

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Addition of 5 mM sodium azide to Clone 9 cells, a rat liver cell line characterized by intracellular glucose concentrations of less than 10% that of the external medium and limited glycogen stores, results in a 50-80% reduction in cell ATP content within 20 min which then recovers to near-basal levels within 1 h and is subsequently maintained at normal levels for 24 h despite continuing the presence of the inhibitor. Associated with this adaptive response is a striking stimulation of facilitated glucose transport, mediated by the GLUT-1 transporter, that exhibits "early" and "late" phases that

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Kawanaka, Kentaro, Izumi Tabata, Shigeru Katsuta, and Mitsuru Higuchi. "Changes in insulin-stimulated glucose transport and GLUT-4 protein in rat skeletal muscle after training." Journal of Applied Physiology 83, no. 6 (1997): 2043–47. http://dx.doi.org/10.1152/jappl.1997.83.6.2043.

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Kawanaka, Kentaro, Izumi Tabata, Shigeru Katsuta, and Mitsuru Higuchi. Changes in insulin-stimulated glucose transport and GLUT-4 protein in rat skeletal muscle after training. J. Appl. Physiol. 83(6): 2043–2047, 1997.—After running training, which increased GLUT-4 protein content in rat skeletal muscle by <40% compared with control rats, the training effect on insulin-stimulated maximal glucose transport (insulin responsiveness) in skeletal muscle was short lived (24 h). A recent study reported that GLUT-4 protein content in rat epitrochlearis muscle increased dramatically (∼2-fold) after

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Spolarics, Z. "Endotoxin stimulates gene expression of ROS-eliminating pathways in rat hepatic endothelial and Kupffer cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 270, no. 4 (1996): G660—G666. http://dx.doi.org/10.1152/ajpgi.1996.270.4.g660.

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Reactive oxygen species (ROS) are mediators of cellular injury and play a putative role in the onset of hepatic damage during endotoxemia or sepsis. It has been suggested that induction of glucose-6-phosphate (G-6-P) dehydrogenase, the key enzyme of the hexose monophosphate shunt (HMS), may support ROS-producing or ROS-eliminating pathways in hepatic endothelial and Kupffer cells during endotoxemia. The aim of the study was to assess in vivo lipopolysaccharide (LPS)-induced alterations in rat gene expression of selected enzymes that are in functional relationship with the HMS. mRNA levels and

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Yuningsih, Dyah Woro Kartiko Kusumo Wardani, Mulyohadi Ali, et al. "The effect of Centella asiatica ethanolic extract on expression of glucose transporter 1 and osteocalcin on stunting larvae of Zebrafish (Danio rerio)." GSC Biological and Pharmaceutical Sciences 19, no. 3 (2022): 178–89. http://dx.doi.org/10.30574/gscbps.2022.19.3.0230.

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Stunting is known as length for age below minus two standard deviations (<-2 SD) of the WHO Child Growth Standard nutritional status. Several causes are identified, including exposure to pesticides (rotenone), which works by inhibiting mitochondrial complex I as an ATP-producing site and generate oxidative stress that affects glucose delivery and bone elongation involving GLUT 1 and osteocalcin. Centella asiatica is a high antioxidant herbal plant with anti-inflammatory properties. This study aimed to investigate the effect of Centella asiatica ethanolic extract on the rotenone-induced stun

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Kristiansen, S., M. Hargreaves, and E. A. Richter. "Exercise-induced increase in glucose transport, GLUT-4, and VAMP-2 in plasma membrane from human muscle." American Journal of Physiology-Endocrinology and Metabolism 270, no. 1 (1996): E197—E201. http://dx.doi.org/10.1152/ajpendo.1996.270.1.e197.

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A major effect of muscle contractions is an increase in sarcolemmal glucose transport. We have used a recently developed technique to produce sarcolemmal giant vesicles from human muscle biopsy samples obtained before and after exercise. Six men exercised for 10 min at 50% maximal O2 uptake (Vo2max) and then to fatigue at 100% Vo2max (5.7 +/- 0.2 min). Vesicle glucose transport at 5 mM increased from 3.3 +/- 0.6 pmol.microgram-1.min-1 at rest to 6.6 +/- 1.0 pmol.microgram-1.min-1 at fatigue (mean +/- SE, n = 6, P < 0.05). This increase in glucose transport was associated with a 1.6-fold inc

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Osborn, Brett A., June T. Daar, Richard A. Laddaga, Fred D. Romano, and Dennis J. Paulson. "Exercise training increases sarcolemmal GLUT-4 protein and mRNA content in diabetic heart." Journal of Applied Physiology 82, no. 3 (1997): 828–34. http://dx.doi.org/10.1152/jappl.1997.82.3.828.

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Osborn, Brett A., June T. Daar, Richard A. Laddaga, Fred D. Romano, and Dennis J. Paulson. Exercise training increases sarcolemmal GLUT-4 protein and mRNA content in diabetic heart. J. Appl. Physiol. 82(3): 828–834, 1997.—This study determined whether dynamic exercise training of diabetic rats would increase the expression of the GLUT-4 glucose transport protein in prepared cardiac sarcolemmal membranes. Four groups were compared: sedentary control, sedentary diabetic, trained control, and trained diabetic. Diabetes was induced by intravenous streptozotocin (60 mg/kg). Trained control and diab

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Host, Helen H., Polly A. Hansen, Lorraine A. Nolte, May M. Chen, and John O. Holloszy. "Glycogen supercompensation masks the effect of a traininginduced increase in GLUT-4 on muscle glucose transport." Journal of Applied Physiology 85, no. 1 (1998): 133–38. http://dx.doi.org/10.1152/jappl.1998.85.1.133.

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Endurance exercise training induces a rapid increase in the GLUT-4 isoform of the glucose transporter in muscle. In fasted rats, insulin-stimulated muscle glucose transport is increased in proportion to the increase in GLUT-4. There is evidence that high muscle glycogen may decrease insulin-stimulated glucose transport. This study was undertaken to determine whether glycogen supercompensation interferes with the increase in glucose transport associated with an exercise-induced increase in GLUT-4. Rats were trained by means of swimming for 6 h/day for 2 days. Rats fasted overnight after the las

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Kern, M., P. L. Dolan, R. S. Mazzeo, J. A. Wells, and G. L. Dohm. "Effect of aging and exercise on GLUT-4 glucose transporters in muscle." American Journal of Physiology-Endocrinology and Metabolism 263, no. 2 (1992): E362—E367. http://dx.doi.org/10.1152/ajpendo.1992.263.2.e362.

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This study was conducted to investigate whether changes in muscle glucose transporter GLUT-4 protein might be associated with a previously reported deterioration in glucose tolerance with aging, and, furthermore, to determine whether exercise training could increase GLUT-4 protein levels in older animals. GLUT-4 protein concentration was measured in soleus, gastrocnemius, and extensor digitorum longus muscles of trained (10 or 15 wk treadmill running) and untrained young (6-8 mo), middle-aged (15-17 mo), and old (27-29 mo) Fischer 344 rats. All GLUT-4 protein values were expressed as a percent

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