GLUT-3 expression in human skeletal muscle

Stuart, Charles Alexander; Wen, Gary; Peng, Bi Hung; Popov, Vsevolod L.; Hudnall, S. David; Campbell, Gerald A.

doi:10.1152/ajpendo.2000.279.4.e855

Cited by 19 publications

(27 citation statements)

References 35 publications

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“…Consistent with previous studies in human skeletal muscles, we could not detect GLUT3 immunoreactivity in adult skeletal muscle fibres [37], nor could we confirm the fibre-type dependency of GLUT3 [32] when using two different polyclonal antibodies with optimised antibody concentrations. High concentrations of anti-GLUT3 antibodies stained muscle fibres, but at these concentrations liver cells, which do not express GLUT3, also stained.…”

Section: Discussionsupporting

confidence: 91%

“…Despite GLUT3 being cloned originally from a fetal human skeletal muscle library [21], GLUT3 mRNA is nearly undetectable in adult human muscle [4,18,29,30,36] and only two studies have reported concomitant GLUT3 protein expression [30,32].…”

Section: Discussionmentioning

confidence: 99%

“…A study on muscle from human autopsies suggested that the lack of detectable GLUT3 protein might be due to degradation of GLUT3 protein prior to investigation [30]. A recent study by the same group, using in situ hybridisation, electron microscopy, immunohistochemistry and immunofluorescence, showed GLUT3 mRNA and protein to be expressed throughout normal human skeletal muscle and predominantly in the triads of slow twitch muscle fibres [32]. In contrast, other groups [18,29] have shown that the expression of GLUT3 protein in adult human skeletal muscles in vivo is below the detection limit.…”

Section: Introductionmentioning

confidence: 99%

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Regenerating human muscle fibres express GLUT3 protein

Gaster

Beck‐Nielsen

2002

Pfl�gers Archiv European Journal of Physiology

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The presence of the GLUT3 glucose transporter protein in human muscle cells is a matter of debate. The present study was designed to establish whether GLUT3 is expressed in mature human skeletal muscle fibres and, if so, whether its expression changes under different conditions, such as metabolic stress (obesity, obese non-insulin-dependent diabetes mellitus), hypertrophy (training), de- and reinnervation (amyotrophic lateral sclerosis) or regeneration (polymyositis). We used an immunohistochemical approach to detect and localise GLUT3. GLUT3 immunoreactivity was not detectable in adult skeletal muscle fibres, nor did metabolic stress, training or de- and re-innervation induce GLUT3 expression, while a few GLUT3 expressing fibres were seen in some cases of polymyositis. In contrast, GLUT4 was expressed in all investigated muscle fibres. GLUT3 immunoreactivity was found in perineural and endoneural cells, indicating that GLUT3 is important for glucose transport into nerves through the perineurium. Taken together, these data suggest that GLUT3 expression is restricted to regenerating muscle fibres and nerves in adult human muscle. Although the significance of GLUT3 in adult human muscle fibres appears limited, GLUT3 may be of importance for the glucose supply in fetal muscle fibres and regenerating adult muscle fibres.

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Section: Discussionsupporting

confidence: 91%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Regenerating human muscle fibres express GLUT3 protein

Gaster

Beck‐Nielsen

2002

Pfl�gers Archiv European Journal of Physiology

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“…Additionally, higher rates of insulin infusion and higher plasma insulin concentrations might increase production of and/or translocation of other glucose transporter isoforms, including GLUT1, which our previous studies did show was responsive to insulin with increased expression and abundance, and GLUT3, which has been found in fetal skeletal muscle (6,14,29,(33)(34)(35)(37)(38)(39).…”

Section: Discussionmentioning

confidence: 91%

Effects of acute hyperinsulinemia on insulin signal transduction and glucose transporters in ovine fetal skeletal muscle

Anderson

Thamotharan²,

Kao³

et al. 2005

American Journal of Physiology-Regulatory, Integrative and Comp

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. Effects of acute hyperinsulinemia on insulin signal transduction and glucose transporters in ovine fetal skeletal muscle. Am J Physiol Regul Integr Comp Physiol 288: R473-R481, 2005. First published November 11, 2004; doi:10.1152/ajpregu.00405.2004.-To test the effects of acute fetal hyperinsulinemia on the pattern and time course of insulin signaling in ovine fetal skeletal muscle, we measured selected signal transduction proteins in the mitogenic, protein synthetic, and metabolic pathways in the skeletal muscle of normally growing fetal sheep in utero. In experiment 1, 4-h hyperinsulinemiceuglycemic clamps were conducted in anesthetized twin fetuses to produce selective fetal hyperinsulinemia-euglycemia in one twin and euinsulinemia-euglycemia in the other. Serial skeletal muscle biopsies were taken from each fetus during the clamp and assayed by Western blot for selected insulin signal transduction proteins. Tyrosine phosphorylation of the insulin receptor, insulin receptor substrate-1, and the p85 subunit of phosphatidylinositol 3-kinase doubled at 30 min and gradually returned to control values by 240 min. Phosphorylation of extracellular signal-regulated kinase 1,2 was increased fivefold through 120 min of insulin infusion and decreased to control concentration by 240 min. Protein kinase B phosphorylation doubled at 30 min and remained elevated throughout the study. Phosphorylation of p70 S6K increased fourfold at 30, 60, and 120 min. In the second experiment, a separate group of nonanesthetized singleton fetuses was clamped to intermediate and high hyperinsulinemic-euglycemic conditions for 1 h. GLUT4 increased fourfold in the plasma membrane at 1 h, and hindlimb glucose uptake increased significantly at the higher insulin concentration. These data demonstrate that an acute increase in fetal plasma insulin concentration stimulates a unique pattern of insulin signal transduction proteins in intact skeletal muscle, thereby increasing pathways for mRNA translation, glucose transport, and cell growth. insulin signaling; fetal growth; glucose transporter 4 IN ADULT ANIMALS and humans, insulin has primarily a metabolic role to regulate skeletal muscle glucose uptake with less effect on skeletal muscle protein synthesis than in rapidly growing tissues. Although increased serum insulin concentration in the fetal sheep has been shown to increase fetal skeletal muscle glucose uptake, especially at pharmacological doses (17,18,20,21), insulin in the rapidly growing fetus seems to act largely as an anabolic hormone, promoting skeletal muscle protein synthesis and growth. In human fetuses, abnormal insulin concentrations contribute to variations in fetal growth; excessive insulin promotes fetal overgrowth, whereas insufficient insulin leads to fetal growth restriction. Animal studies have produced experimental deficiencies in insulin secretion in fetal lambs, resulting in fetal growth restriction and limited carcass protein accretion (27). Also, it has been shown in the neonatal pig that insulin action to promote s...

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“…However, immunofluorescence and immunohistochemical localization of GLUT3 in normal human skeletal muscle demonstrated that GLUT3 protein is distributed throughout the muscle. GLUT3 was shown to be expressed predominantly in slow twitch fibers although at a low level [46] and was mainly localized to the plasma membrane-enriched fractions [47]. The presence of GLUT3 together with GLUT1 and GLUT4 at the plasma membrane could contribute to basal glucose uptake.…”

Section: Glut3mentioning

confidence: 98%

What we know about facilitative glucose transporters: Lessons from cultured cells, animal models, and human studies

Gorovits

Charron

2003

Biochem Molecular Bio Educ

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Glucose uptake by all cells in the organism by glucose transport proteins is among the most essential processes in life. The process of glucose uptake into tissues is performed by glucose transporters. This review focuses on the biology of facilitative glucose transporters (GLUTs). The knowledge that has accumulated for more than a decade with respect to the regulation of GLUT expression and function in various experimental conditions points to the great potential for GLUTs to be utilized as targets for designing therapies for treatment of diseases related to impaired regulation of glucose homeostasis including type 2 diabetes.Keywords: Glucose uptake, GLUT, insulin action, diabetes.The entry of glucose into cells is a crucial step in lifesupporting processes since glucose is the main monosaccharide in nature that provides carbon and energy for almost all cells. The passage of glucose into cells depends on different parameters, including expression of the appropriate glucose transporters in the target tissues and hormonal regulation of their function. Single cell eucaryotes such as Saccharomyces cerevisiae possess 20 genes encoding glucose or glucose-like transporters and express the glucose transporters most appropriate for the amount of glucose available [1]. In mammalian cells a tight regulation of blood glucose levels is needed to meet the energetic demands of the brain, a tissue that uses glucose as its primary energy source [2,3]. Adequate glucose flux into tissues provides maintenance of glucose homeostasis that is critical in well being. Transport of glucose across the plasma membrane is accomplished by two families of glucose transporters: sodium-glucose co-transporters (SGLT 1 1-3), mainly expressed in the apical membrane of renal and intestinal absorptive epithelial cells that transport glucose against its concentration gradient and utilize ATP (for a review, see Ref. 4), and facilitative glucose transporters (GLUTs) that are expressed in all cells that transport glucose down a concentration gradient [5][6][7]. Until now the search for the mammalian facilitative glucose transporters has yielded 12 carriers including GLUT1-5 and the recently discovered GLUT6 -12. GLUT1-4 share greater than 40% homology [8], and GLUT5, which is a fructose transporter, exhibits 42, 40, 38, and 41.6% identity with GLUT1, GLUT2, GLUT3, and GLUT4, respectively [9]. All GLUTs have been predicted to have 12 membrane-spanning domains (helices) connected by hydrophilic loops, the first of which is exofacial and contains an N-glycosylation site in GLUT1-5 (Fig. 1) [8,10]. Both the amino and carboxyl termini of GLUTs reside on the cytoplasmic side of the cell membrane [11]. The carboxyl termini of all GLUTs have unique amino acid sequences that have been utilized for development of reagents. The common sensitivity of the GLUT family to the inhibitory action of the fungal metabolite cytochalasin B has been reported widely and is utilized in studies of hexose transporters [12]. Substrate selectivity of GLUTs is dictated by conserve...

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GLUT-3 expression in human skeletal muscle

Cited by 19 publications

References 35 publications

Regenerating human muscle fibres express GLUT3 protein

Regenerating human muscle fibres express GLUT3 protein

Effects of acute hyperinsulinemia on insulin signal transduction and glucose transporters in ovine fetal skeletal muscle

What we know about facilitative glucose transporters: Lessons from cultured cells, animal models, and human studies

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