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Journal articles on the topic 'GluTR'

Author: Grafiati

Published: 4 June 2021

Last updated: 8 February 2022

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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

Inukai, Kouichi, Annette M. Shewan, Wendy S. Pascoe, Shigehiro Katayama, David E. James, and Yoshitomo Oka. "Carboxy Terminus of Glucose Transporter 3 Contains an Apical Membrane Targeting Domain." Molecular Endocrinology 18, no. 2 (2004): 339–49. http://dx.doi.org/10.1210/me.2003-0089.

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Abstract We previously demonstrated that distinct facilitative glucose transporter isoforms display differential sorting in polarized epithelial cells. In Madin-Darby canine kidney (MDCK) cells, glucose transporter 1 and 2 (GLUT1 and GLUT2) are localized to the basolateral cell surface whereas GLUTs 3 and 5 are targeted to the apical membrane. To explore the molecular mechanisms underlying this asymmetric distribution, we analyzed the targeting of chimeric glucose transporter proteins in MDCK cells. Replacement of the carboxy-terminal cytosolic tail of GLUT1, GLUT2, or GLUT4 with that from GLU

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3

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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4

Ali, Raafay S., Morag F. Dick, Saad Muhammad, et al. "Glucose transporter expression and regulation following a fast in the ruby-throated hummingbird, Archilochus colubris." Journal of Experimental Biology 223, no. 20 (2020): jeb229989. http://dx.doi.org/10.1242/jeb.229989.

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ABSTRACTHummingbirds, subsisting almost exclusively on nectar sugar, face extreme challenges to blood sugar regulation. The capacity for transmembrane sugar transport is mediated by the activity of facilitative glucose transporters (GLUTs) and their localisation to the plasma membrane (PM). In this study, we determined the relative protein abundance of GLUT1, GLUT2, GLUT3 and GLUT5 via immunoblot using custom-designed antibodies in whole-tissue homogenates and PM fractions of flight muscle, heart and liver of ruby-throated hummingbirds (Archilochus colubris). The GLUTs examined were detected i

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5

Rayner, D. V., Moira E. A. Thomas, and Paul Trayhurn. "Glucose transporters (GLUTs 1–4) and their mRNAs in regions of the rat brain: insulin-sensitive transporter expression in the cerebellum." Canadian Journal of Physiology and Pharmacology 72, no. 5 (1994): 476–79. http://dx.doi.org/10.1139/y94-069.

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Major regions of the rat brain have been examined for the presence of glucose transporters (GLUTs 1–4) and their mRNAs. Both the mRNA and immunoreactive protein for GLUT1 and GLUT3 were found in each brain region (medulla, pons, cerebellum, midbrain, hypothalamus, thalamus, hippocampus, parietal cortex). The mRNA and protein for GLUT4 were identified in the cerebellum, but not elsewhere in the brain. GLUT2 protein and mRNA were not detected in any region of the brain. Although GLUT1 and GLUT3 are the major brain glucose transporters, the presence of GLUT4 in the cerebellum suggests that insuli

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6

LISINSKI, Ivonne, Annette SCHÜRMANN, Hans-Georg JOOST, Samuel W. CUSHMAN, and Hadi AL-HASANI. "Targeting of GLUT6 (formerly GLUT9) and GLUT8 in rat adipose cells." Biochemical Journal 358, no. 2 (2001): 517–22. http://dx.doi.org/10.1042/bj3580517.

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The subcellular targeting of the two recently cloned novel mammalian glucose transporters, GLUT6 {previously referred to as GLUT9 [Doege, Bocianski, Joost and Schürmann (2000) Biochem. J. 350, 771–776]} and GLUT8, was analysed by expression of haemagglutinin (HA)-epitope-tagged GLUTs in transiently transfected primary rat adipose cells. Similar to HA-GLUT4, both transporters, HA-GLUT6 and HA-GLUT8, were retained in intracellular compartments in non-stimulated cells. In contrast, mutation of the N-terminal dileucine motifs in both constructs led to constitutive expression of the proteins on the

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7

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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8

Zhang, Shihai, Qing Yang, Man Ren, et al. "Effects of isoleucine on glucose uptake through the enhancement of muscular membrane concentrations of GLUT1 and GLUT4 and intestinal membrane concentrations of Na+/glucose co-transporter 1 (SGLT-1) and GLUT2." British Journal of Nutrition 116, no. 4 (2016): 593–602. http://dx.doi.org/10.1017/s0007114516002439.

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AbstractKnowledge of regulation of glucose transport contributes to our understanding of whole-body glucose homoeostasis and human metabolic diseases. Isoleucine has been reported to participate in regulation of glucose levels in many studies; therefore, this study was designed to examine the effect of isoleucine on intestinal and muscular GLUT expressions. In an animal experiment, muscular GLUT and intestinal GLUT were determined in weaning pigs fed control or isoleucine-supplemented diets. Supplementation of isoleucine in the diet significantly increased piglet average daily gain, enhanced G

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9

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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10

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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11

Machado, Ubiratan Fabres. "Transportadores de glicose." Arquivos Brasileiros de Endocrinologia & Metabologia 42, no. 6 (1998): 413–21. http://dx.doi.org/10.1590/s0004-27301998000600003.

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A glicose, principal fonte de energia celular, é transportada na maioria das células por difusão facilitada, através de proteínas transportadoras presentes na membrana plasmática. Está caracterizada a existencia de urna familia de transportadores (GLUT1-GLUT7), com características funcionáis e distribuição tecidual distintas. Por outro lado, em epitelios intestinal e tubular renal, o transporte é contra gradiente e acoplado ao Na+ na membrana apical das células através de cotransportadores (SGLT1-SGLT2), com posterior difusão para o intersticio através de GLUTs presentes na membrana basolatera

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12

Vasileuskaya, Zinaida, Ulrike Oster, and Christoph F. Beck. "Mg-Protoporphyrin IX and Heme Control HEMA, the Gene Encoding the First Specific Step of Tetrapyrrole Biosynthesis, in Chlamydomonas reinhardtii." Eukaryotic Cell 4, no. 10 (2005): 1620–28. http://dx.doi.org/10.1128/ec.4.10.1620-1628.2005.

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ABSTRACT HEMA encodes glutamyl-tRNA reductase (GluTR), which catalyzes the first step specific for tetrapyrrole biosynthesis in plants, archaea, and most eubacteria. In higher plants, GluTR is feedback inhibited by heme and intermediates of chlorophyll biosynthesis. It plays a key role in controlling flux through the tetrapyrrole biosynthetic pathway. This enzyme, which in Chlamydomonas reinhardtii is encoded by a single gene (HEMA), exhibits homology to GluTRs of higher plants and cyanobacteria. HEMA mRNA accumulation was inducible not only by light but also by treatment of dark-adapted cells

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13

Medina, RA, AM Meneses, JC Vera, et al. "Differential regulation of glucose transporter expression by estrogen and progesterone in Ishikawa endometrial cancer cells." Journal of Endocrinology 182, no. 3 (2004): 467–78. http://dx.doi.org/10.1677/joe.0.1820467.

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Estrogen replacement therapy and other unopposed estrogen treatments increase the incidence of endometrial abnormalities, including cancer. However, this effect is counteracted by the co-administration of progesterone. In the endometrium, glucose transporter (GLUT) expression and glucose transport are known to fluctuate throughout the menstrual cycle. Here, we determined the effect of estrogen and progesterone on the expression of GLUT1-4 and on the transport of deoxyglucose in Ishikawa endometrial cancer cells. Cells were incubated with estrogen, progesterone or combined estrogen and progeste

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14

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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15

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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Wang, Peng, Fu-Cheng Liang, Daniel Wittmann, Alex Siegel, Shu-ou Shan, and Bernhard Grimm. "Chloroplast SRP43 acts as a chaperone for glutamyl-tRNA reductase, the rate-limiting enzyme in tetrapyrrole biosynthesis." Proceedings of the National Academy of Sciences 115, no. 15 (2018): E3588—E3596. http://dx.doi.org/10.1073/pnas.1719645115.

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Assembly of light-harvesting complexes requires synchronization of chlorophyll (Chl) biosynthesis with biogenesis of light-harvesting Chl a/b-binding proteins (LHCPs). The chloroplast signal recognition particle (cpSRP) pathway is responsible for transport of nucleus-encoded LHCPs in the stroma of the plastid and their integration into the thylakoid membranes. Correct folding and assembly of LHCPs require the incorporation of Chls, whose biosynthesis must therefore be precisely coordinated with membrane insertion of LHCPs. How the spatiotemporal coordination between the cpSRP machinery and Chl

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17

Medina, Rodolfo A., Ana Maria Meneses, Juan Carlos Vera, et al. "Estrogen and Progesterone Up-Regulate Glucose Transporter Expression in ZR-75-1 Human Breast Cancer Cells." Endocrinology 144, no. 10 (2003): 4527–35. http://dx.doi.org/10.1210/en.2003-0294.

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Breast cancer incidence increases in women receiving combined estrogen and progesterone therapy. Breast tumors show increased expression of the glucose transporter GLUT1. We determined the effect of these hormones on GLUT1–4 expression and deoxyglucose transport in ZR-75-1 breast cancer cells. Immunoblotting, immunocytochemistry, flow cytometry, and RT-PCR showed that GLUT1 expression is up-regulated by progesterone and, to a greater degree, combined therapy. GLUT2 expression is unaffected by hormonal treatment. GLUT3 protein and RNA is up-regulated by progesterone and combined therapy, and GL

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18

Custódio, Tânia Filipa, Peter Aasted Paulsen, Kelly May Frain, and Bjørn Panyella Pedersen. "Structural comparison of GLUT1 to GLUT3 reveal transport regulation mechanism in sugar porter family." Life Science Alliance 4, no. 4 (2021): e202000858. http://dx.doi.org/10.26508/lsa.202000858.

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The human glucose transporters GLUT1 and GLUT3 have a central role in glucose uptake as canonical members of the Sugar Porter (SP) family. GLUT1 and GLUT3 share a fully conserved substrate-binding site with identical substrate coordination, but differ significantly in transport affinity in line with their physiological function. Here, we present a 2.4 Å crystal structure of GLUT1 in an inward open conformation and compare it with GLUT3 using both structural and functional data. Our work shows that interactions between a cytosolic “SP motif” and a conserved “A motif” stabilize the outward confo

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Grabauskas, Gintautas, Shi-Yi Zhou, Yuanxu Lu, Il Song, and Chung Owyang. "Essential Elements for Glucosensing by Gastric Vagal Afferents: Immunocytochemistry and Electrophysiology Studies in the Rat." Endocrinology 154, no. 1 (2013): 296–307. http://dx.doi.org/10.1210/en.2012-1382.

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Glucosensing nodose ganglia neurons mediate the effects of hyperglycemia on gastrointestinal motility. We hypothesized that the glucose-sensing mechanisms in the nodose ganglia are similar to those of hypothalamic glucose excited neurons, which sense glucose through glycolysis. Glucose metabolism leads to ATP-sensitive potassium channel (KATP) channel closure and membrane depolarization. We identified glucosensing elements in the form of glucose transporters (GLUTs), glucokinase (GK), and KATP channels in rat nodose ganglia and evaluated their physiological significance. In vitro stomach-vagus

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Koehler-Stec, Ellen M., Kang Li, Fran Maher, Susan J. Vannucci, Carolyn B. Smith, and Ian A. Simpson. "Cerebral Glucose Utilization and Glucose Transporter Expression: Response to Water Deprivation and Restoration." Journal of Cerebral Blood Flow & Metabolism 20, no. 1 (2000): 192–200. http://dx.doi.org/10.1097/00004647-200001000-00024.

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The relationship between local rates of cerebral glucose utilization (lCMRglc) and glucose transporter expression was examined during physiologic activation of the hypothalamoneurohypophysial system. Three days of water deprivation, which is known to activate the hypothalamoneurohypophysial system, resulted in increased lCMRglc and increased concentrations of GLUT1 and GLUT3 in the neurohypophysis; mRNA levels of GLUT1 and GLUT3 were decreased and increased, respectively. Water deprivation also increased lCMRglc in the hypothalamic supraoptic and paraventricular nuclei; mRNA levels of GLUT1 an

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Gao, Lu, Chunmei Lv, Chen Xu, et al. "Differential Regulation of Glucose Transporters Mediated by CRH Receptor Type 1 and Type 2 in Human Placental Trophoblasts." Endocrinology 153, no. 3 (2012): 1464–71. http://dx.doi.org/10.1210/en.2011-1673.

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Glucose transport across the placenta is mediated by glucose transporters (GLUT), which is critical for normal development and survival of the fetus. Regulatory mechanisms of GLUT in placenta have not been elucidated. Placental CRH has been implicated to play a key role in the control of fetal growth and development. We hypothesized that CRH, produced locally in placenta, could act to modulate GLUT in placenta. To investigate this, we obtained human placentas from uncomplicated term pregnancies and isolated and cultured trophoblast cells. GLUT1 and GLUT3 expressions in placenta were determined

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22

Gonzalez-Menendez, Pedro, David Hevia, Aida Rodriguez-Garcia, Juan C. Mayo, and Rosa M. Sainz. "Regulation of GLUT Transporters by Flavonoids in Androgen-Sensitive and -Insensitive Prostate Cancer Cells." Endocrinology 155, no. 9 (2014): 3238–50. http://dx.doi.org/10.1210/en.2014-1260.

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Abstract Cancer cells show different metabolic requirements from normal cells. In prostate cancer, particularly, glycolytic metabolism differs in androgen-responsive and nonresponsive cells. In addition, some natural compounds with antiproliferative activities are able to modify glucose entry into cells by either modulating glucose transporter (GLUT) expression or by altering glucose binding. The aim of this work was to study the regulation of some GLUTs (GLUT1 and GLUT4) in both androgen-sensitive (LNCaP) and -insensitive (PC-3) prostate cancer cells by 4 structurally different flavonoids (ie

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23

Zhang, Wei, Lindsay H. Sumners, Paul B. Siegel, Mark A. Cline, and Elizabeth R. Gilbert. "Quantity of glucose transporter and appetite-associated factor mRNA in various tissues after insulin injection in chickens selected for low or high body weight." Physiological Genomics 45, no. 22 (2013): 1084–94. http://dx.doi.org/10.1152/physiolgenomics.00102.2013.

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Chickens from lines selected for low (LWS) or high (HWS) body weight differ by 10-fold in body weight at 56 days old with differences in food intake, glucose regulation, and body composition. To evaluate if there are differences in appetite-regulatory factor and glucose transporter ( GLUT) mRNA that are accentuated by hypoglycemia, blood glucose was measured, and hypothalamus, liver, pectoralis major, and abdominal fat collected at 90 days of age from female HWS and LWS chickens, and reciprocal crosses, HL and LH, at 60 min after intraperitoneal injection of insulin. Neuropeptide Y ( NPY) and

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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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Chen, Y., ML Nagpal, and T. Lin. "Expression and regulation of glucose transporter 8 in rat Leydig cells." Journal of Endocrinology 179, no. 1 (2003): 63–72. http://dx.doi.org/10.1677/joe.0.1790063.

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Basal and LH/human chorionic gonadotropin (hCG)-stimulated testosterone formation by Leydig cells is dependent on ambient glucose levels. Inhibition of glucose uptake is associated with decreased testosterone formation. Recently, glucose transporter 8 (GLUT8) has been shown to be highly expressed in the testis. In the present study, we have investigated the expression and regulation of the GLUT8 gene in rat Leydig cells. Primers were designed by using sequences that are not conserved in GLUT1 to GLUT5 and that contain the glycosylation region of GLUT8. This yielded an amplicon of 186 bp. The t

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Apitz, Janina, Kenji Nishimura, Judith Schmied, et al. "Posttranslational Control of ALA Synthesis Includes GluTR Degradation by Clp Protease and Stabilization by GluTR-Binding Protein." Plant Physiology 170, no. 4 (2016): 2040–51. http://dx.doi.org/10.1104/pp.15.01945.

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Baumann, Marc U., Stacy Zamudio, and Nicholas P. Illsley. "Hypoxic upregulation of glucose transporters in BeWo choriocarcinoma cells is mediated by hypoxia-inducible factor-1." American Journal of Physiology-Cell Physiology 293, no. 1 (2007): C477—C485. http://dx.doi.org/10.1152/ajpcell.00075.2007.

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Placental hypoxia has been implicated in pregnancy pathologies, including fetal growth restriction and preeclampsia; however, the mechanism by which the trophoblast cell responds to hypoxia has not been adequately explored. Glucose transport, a process crucial to fetoplacental growth, is upregulated by hypoxia in a number of cell types. We investigated the effects of hypoxia on the regulation of trophoblast glucose transporter (GLUT) expression and activity in BeWo choriocarcinoma cells, a trophoblast cell model, and human placental villous tissue explants. GLUT1 expression in BeWo cells was u

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Dimitriadis, George, Eirini Maratou, Eleni Boutati, et al. "IGF-I increases the recruitment of GLUT4 and GLUT3 glucose transporters on cell surface in hyperthyroidism." European Journal of Endocrinology 158, no. 3 (2008): 361–66. http://dx.doi.org/10.1530/eje-07-0532.

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ObjectiveIn hyperthyroidism, tissue glucose disposal is increased to adapt to high energy demand. Our aim was to examine the regulation of glucose transporter (GLUT) isoforms by IGF-I in monocytes from patients with hyperthyroidism.Design and methodsBlood (20 ml) was drawn from 21 healthy and 10 hyperthyroid subjects. The abundance of GLUT isoforms on the monocyte plasma membrane was determined in the absence and presence of IGF-I (0.07, 0.14, and 0.7 nM) using flow cytometry. Anti-CD14-phycoerythrin monocional antibody was used for monocyte gating. GLUT isoforms were determined after staining

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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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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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Mahraoui, L., A. Rodolosse, A. Barbat, et al. "Presence and differential expression of SGLT1, GLUT1, GLUT2, GLUT3 and GLUT5 hexose-transporter mRNAs in Caco-2 cell clones in relation to cell growth and glucose consumption." Biochemical Journal 298, no. 3 (1994): 629–33. http://dx.doi.org/10.1042/bj2980629.

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Seven clones from the Caco-2 cell line, three isolated from passage 29 (PD7, PD10, PF11) and four from passage 198 (TB10, TC7, TF3, TG6), all of them selected on the basis of differences in the levels of expression of sucrase-isomaltase and rates of glucose consumption, were analysed for the expression of hexose-transporter mRNAs (SGLT1, GLUT1-GLUT5) in relation to the phases of cell growth and the associated variations of the rates of glucose consumption. All clones showed a similar pattern of evolution of the rates of glucose consumption, which decreased from the exponential to the late-stat

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RYDER, Jeffrey W., Yuichi KAWANO, Alexander V. CHIBALIN, et al. "In vitro analysis of the glucose-transport system in GLUT4-null skeletal muscle." Biochemical Journal 342, no. 2 (1999): 321–28. http://dx.doi.org/10.1042/bj3420321.

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We have characterized the glucose-transport system in soleus muscle from female GLUT4-null mice to determine whether GLUT1, 3 or 5 account for insulin-stimulated glucose-transport activity. Insulin increased 2-deoxyglucose uptake 2.8- and 2.1-fold in soleus muscle from wild-type and GLUT4-null mice, respectively. Cytochalasin B, an inhibitor of GLUT1- and GLUT4-mediated glucose transport, inhibited insulin-stimulated 2-deoxyglucose uptake by > 95% in wild-type and GLUT4-null soleus muscle. Addition of 35 mM fructose to the incubation media was without effect on insulin-stimulated 3-O-methyl

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Li, Qiang, Andrei Manolescu, Mabel Ritzel, et al. "Cloning and functional characterization of the human GLUT7 isoform SLC2A7 from the small intestine." American Journal of Physiology-Gastrointestinal and Liver Physiology 287, no. 1 (2004): G236—G242. http://dx.doi.org/10.1152/ajpgi.00396.2003.

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Facilitated glucose transporters (GLUTs) mediate transport of sugars across cell membranes by using the chemical gradient of sugars as the driving force. Improved cloning techniques and database analyses have expanded this family of proteins to a total of 14 putative members. In this work a novel hexose transporter isoform, GLUT7, has been cloned from a human intestinal cDNA library by using a PCR-based strategy (GenBank accession no. AY571960 ). The encoded protein is comprised of 524 amino acid residues and shares 68% similarity and 53% identity with GLUT5, its most closely related isoform.

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Concha, Ilona I., Fernando V. Velásquez, Juan M. Martı́nez, et al. "Human Erythrocytes Express GLUT5 and Transport Fructose." Blood 89, no. 11 (1997): 4190–95. http://dx.doi.org/10.1182/blood.v89.11.4190.

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Abstract Although erythrocytes readily metabolize fructose, it has not been known how this sugar gains entry to the red blood cell. We present evidence indicating that human erythrocytes express the fructose transporter GLUT5, which is the major means for transporting fructose into the cell. Immunoblotting and immunolocalization experiments identified the presence of GLUT1 and GLUT5 as the main facilitative hexose transporters expressed in human erythrocytes, with GLUT2 present in lower amounts. Functional studies allowed the identification of two transporters with different kinetic properties

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Gutiérrez-Torres, Daniela Sarahí, Carmen González-Horta, Luz María Del Razo, et al. "Prenatal Exposure to Sodium Arsenite Alters Placental Glucose 1, 3, and 4 Transporters in Balb/c Mice." BioMed Research International 2015 (2015): 1–9. http://dx.doi.org/10.1155/2015/175025.

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Inorganic arsenic (iAs) exposure induces a decrease in glucose type 4 transporter (GLUT4) expression on the adipocyte membrane, which may be related to premature births and low birth weight infants in women exposed to iAs at reproductive age. The aim of this study was to analyze the effect of sodium arsenite (NaAsO2) exposure on GLUT1, GLUT3, and GLUT4 protein expression and on placental morphology. Female Balb/c mice (n=15) were exposed to 0, 12, and 20 ppm of NaAsO2in drinking water from 8th to 18th day of gestation. Morphological changes and GLUT1, GLUT3, and GLUT4 expression were evaluated

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Ermini, Leonardo, Anna Maria Nuzzo, Francesca Ietta, et al. "Placental Glucose Transporters and Response to Bisphenol A in Pregnancies from of Normal and Overweight Mothers." International Journal of Molecular Sciences 22, no. 12 (2021): 6625. http://dx.doi.org/10.3390/ijms22126625.

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Bisphenol A (BPA) is a synthetic phenol extensively used in the manufacture of polycarbonate plastics and epoxy resins and a component of liquid and food storages. Among health disorders potentially attributed to BPA, the effects on metabolism have been especially studied. BPA represents a hazard in prenatal life because of its presence in tissues and fluids during pregnancy. Our recent study in rats fed with BPA showed a placental increase in glucose type 1 transporter (GLUT-1), suggesting a higher uptake of glucose. However, the role of BPA on GLUT transporters in pregnant women with metabol

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Evans, Sarah A., Manuel Doblado, Maggie M. Chi, John A. Corbett та Kelle H. Moley. "Facilitative Glucose Transporter 9 Expression Affects Glucose Sensing in Pancreatic β-Cells". Endocrinology 150, № 12 (2009): 5302–10. http://dx.doi.org/10.1210/en.2009-0747.

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Abstract Facilitative glucose transporters (GLUTs) including GLUT9, accelerate the facilitative diffusion of glucose across the plasma membrane. Studies in GLUT2-deficient mice suggested the existence of another GLUT in the mammalian β-cell responsible for glucose sensing. The objective of this study was to determine the expression and function of GLUT9 in murine and human β-cells. mRNA and protein expression levels were determined for both isoforms of GLUT9 in murine and human isolated islets as well as insulinoma cell lines (MIN6). Immunohistochemistry and subcellular localization were perfo

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Lesage, J., D. Hahn, M. Leonhardt, B. Blondeau, B. Breant, and JP Dupouy. "Maternal undernutrition during late gestation-induced intrauterine growth restriction in the rat is associated with impaired placental GLUT3 expression, but does not correlate with endogenous corticosterone levels." Journal of Endocrinology 174, no. 1 (2002): 37–43. http://dx.doi.org/10.1677/joe.0.1740037.

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Fetal intrauterine growth restriction (IUGR) is a frequently occurring and serious complication of pregnancy. Infants exposed to IUGR are at risk for numerous perinatal morbidities, including hypoglycemia in the neonatal period, as well as increased risk of later physical and/or mental impairments, cardiovascular disease and non-insulin-dependent diabetes mellitus. Fetal growth restriction most often results from uteroplacental dysfunction during the later stage of pregnancy. As glucose, which is the most abundant nutrient crossing the placenta, fulfills a large portion of the fetal energy req

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McKinnon, Brett, Dominic Bertschi, Carlos Wotzkow, Nick A. Bersinger, Jakob Evers, and Michael D. Mueller. "Glucose transporter expression in eutopic endometrial tissue and ectopic endometriotic lesions." Journal of Molecular Endocrinology 52, no. 2 (2014): 169–79. http://dx.doi.org/10.1530/jme-13-0194.

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Endometriosis is an extremely prevalent disorder characterized by the growth of endometrial tissue at ectopic locations. Glycolysis is an energy-producing mechanism that occurs in almost all cells and requires an adequate uptake of glucose mediated by glucose transporter (GLUT) proteins. At present, however, very little is known about their expression in either the endometrium or the endometriotic lesions. The objective of this study was to examine the expression ofSLC2Agenes in the endometrium of women with and without endometriosis and in the matching ectopic tissue, and to confirm the prese

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Burant, C. F., and N. O. Davidson. "GLUT3 glucose transporter isoform in rat testis: localization, effect of diabetes mellitus, and comparison to human testis." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 267, no. 6 (1994): R1488—R1495. http://dx.doi.org/10.1152/ajpregu.1994.267.6.r1488.

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Facilitative hexose transporter expression was compared in rat and human testes. In rat testis, only GLUT1 and GLUT3 proteins were expressed. By contrast, human testis expressed GLUT1 and GLUT3 in addition to GLUT5. Immunocytochemical studies showed that GLUT3 was expressed in all cells of the seminiferous epithelium of rat testis, including sperm. In human testis, GLUT3 was expressed exclusively in cells juxtaposed to the lumen of the seminiferous tubule and ejaculate sperm, a pattern of expression that was identical to that of GLUT5. Induction of insulinopenic diabetes mellitus in the rat di

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Aerni-Flessner, Lauren, Melissa Abi-Jaoude, Amanda Koenig, Maria Payne, and Paul W. Hruz. "GLUT4, GLUT1, and GLUT8 are the dominant GLUT transcripts expressed in the murine left ventricle." Cardiovascular Diabetology 11, no. 1 (2012): 63. http://dx.doi.org/10.1186/1475-2840-11-63.

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STROBEL, Pablo, Claudio ALLARD, Tomás PEREZ-ACLE, Rosario CALDERON, Rebeca ALDUNATE, and Federico LEIGHTON. "Myricetin, quercetin and catechin-gallate inhibit glucose uptake in isolated rat adipocytes." Biochemical Journal 386, no. 3 (2005): 471–78. http://dx.doi.org/10.1042/bj20040703.

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The facilitative glucose transporter, GLUT4, mediates insulin-stimulated glucose uptake in adipocytes and muscles, and the participation of GLUT4 in the pathogenesis of various clinical conditions associated with obesity, visceral fat accumulation and insulin resistance has been proposed. Glucose uptake by some members of the GLUT family, mainly GLUT1, is inhibited by flavonoids, the natural polyphenols present in fruits, vegetables and wine. Therefore it is of interest to establish if these polyphenolic compounds present in the diet, known to be effective antioxidants but also endowed with se

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Ennis, Kathleen, Barbara Felt, Michael K. Georgieff, and Raghavendra Rao. "Early-Life Iron Deficiency Alters Glucose Transporter-1 Expression in the Adult Rodent Hippocampus." Journal of Nutrition 149, no. 9 (2019): 1660–66. http://dx.doi.org/10.1093/jn/nxz100.

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ABSTRACT Background Early-life iron deficiency (ID) impairs hippocampal energy production. Whether there are changes in glucose transporter (GLUT) expression is not known. Objective The aim of this study was to investigate whether early-life ID and the treatment iron dose alter brain regional GLUT expression in adult rats and mice. Methods In Study 1, ID was induced in male and female Sprague Dawley rat pups by feeding dams a 3-mg/kg iron diet during gestation and the first postnatal week, followed by treatment using low-iron [3–10 mg/kg; formerly iron-deficient (FID)-10 group], standard-iron

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Hresko, Richard C., Thomas E. Kraft, Andrew Quigley, Elisabeth P. Carpenter, and Paul W. Hruz. "Mammalian Glucose Transporter Activity Is Dependent upon Anionic and Conical Phospholipids." Journal of Biological Chemistry 291, no. 33 (2016): 17271–82. http://dx.doi.org/10.1074/jbc.m116.730168.

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The regulated movement of glucose across mammalian cell membranes is mediated by facilitative glucose transporters (GLUTs) embedded in lipid bilayers. Despite the known importance of phospholipids in regulating protein structure and activity, the lipid-induced effects on the GLUTs remain poorly understood. We systematically examined the effects of physiologically relevant phospholipids on glucose transport in liposomes containing purified GLUT4 and GLUT3. The anionic phospholipids, phosphatidic acid, phosphatidylserine, phosphatidylglycerol, and phosphatidylinositol, were found to be essential

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Vannucci, Susan J., Lisa B. Seaman, and Robert C. Vannucci. "Effects of Hypoxia-Ischemia on GLUT1 and GLUT3 Glucose Transporters in Immature Rat Brain." Journal of Cerebral Blood Flow & Metabolism 16, no. 1 (1996): 77–81. http://dx.doi.org/10.1097/00004647-199601000-00009.

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Cerebral hypoxia-ischemia produces major alterations in energy metabolism and glucose utilization in brain. The facilitative glucose transporter proteins mediate the transport of glucose across the blood–brain barrier (BBB) (55 kDa GLUT1) and into the neurons and glia (GLUT3 and 45 kDa GLUT1). Glucose uptake and utilization are low in the immature rat brain, as are the levels of the glucose transporter proteins. This study investigated the effect of cerebral hypoxia-ischemia in a model of unilateral brain damage on the expression of GLUT 1 and GLUT3 in the ipsilateral (damaged, hypoxic-ischemi

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Suwabe, Yoko, Rei Nakano, Shinichi Namba, et al. "Involvement of GLUT1 and GLUT3 in the growth of canine melanoma cells." PLOS ONE 16, no. 2 (2021): e0243859. http://dx.doi.org/10.1371/journal.pone.0243859.

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The rate of glucose uptake dramatically increases in cancer cells even in the presence of oxygen and fully functioning mitochondria. Cancer cells produce ATP by glycolysis rather than oxidative phosphorylation under aerobic conditions, a process termed as the “Warburg effect.” In the present study, we treated canine melanoma cells with the glucose analog 2-deoxy-D-glucose (2-DG) and investigated its effect on cell growth. 2-DG attenuated cell growth in a time- and dose-dependent manner. Cell growth was also inhibited following treatment with the glucose transporter (GLUT) inhibitor WZB-117. Th

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Tsakiridis, T., M. Vranic, and A. Klip. "Phosphatidylinositol 3-kinase and the actin network are not required for the stimulation of glucose transport caused by mitochondrial uncoupling: comparison with insulin action." Biochemical Journal 309, no. 1 (1995): 1–5. http://dx.doi.org/10.1042/bj3090001.

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In L6 myotubes insulin stimulates glucose transport through the translocation of glucose transporters GLUT1, GLUT3 and GLUT4 from intracellular stores to the plasma membrane. An intact actin network and phosphatidylinositol 3-kinase activity are required for this process. Glucose transport is also stimulated by the mitochondrial ATP-production uncoupler dinitrophenol. We show here that, in serum-depleted myotubes, dinitrophenol induced translocation of GLUT1 and GLUT4, but not GLUT3. This response was not affected by inhibiting phosphatidylinositol 3-kinase or disassembling the actin network.

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KHAYAT, Zayna A., Anthony L. McCALL, and Amira KLIP. "Unique mechanism of GLUT3 glucose transporter regulation by prolonged energy demand: increased protein half-life." Biochemical Journal 333, no. 3 (1998): 713–18. http://dx.doi.org/10.1042/bj3330713.

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L6 muscle cells survive long-term (18 h) disruption of oxidative phosphorylation by the mitochondrial uncoupler 2,4-dinitrophenol (DNP) because, in response to this metabolic stress, they increase their rate of glucose transport. This response is associated with an elevation of the protein content of glucose transporter isoforms GLUT3 and GLUT1, but not GLUT4. Previously we have reported that the rise in GLUT1 expression is likely to be a result of de novo biosynthesis of the transporter, since the uncoupler increases GLUT1 mRNA levels. Unlike GLUT1, very little is known about how interfering

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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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Wagstaff, P., H. Y. Kang, D. Mylott, P. J. Robbins, and M. K. White. "Characterization of the avian GLUT1 glucose transporter: differential regulation of GLUT1 and GLUT3 in chicken embryo fibroblasts." Molecular Biology of the Cell 6, no. 11 (1995): 1575–89. http://dx.doi.org/10.1091/mbc.6.11.1575.

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Vertebrate cells that are transformed by oncogenes such as v-src or are stimulated by mitogens have increased rates of glucose uptake. In rodent cells, the mechanisms whereby glucose transport is up-regulated are well understood. Stimulation of glucose transport involves an elevation in mRNA encoding the GLUT1 glucose transporter that is controlled at the levels of both transcription and mRNA stability. Cloning and sequencing of chicken GLUT1 cDNA showed that it shares 95% amino acid sequence similarity to mammalian GLUT1s. Nevertheless, unlike mammalian GLUT1 mRNA, it was not induced by v-src

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