Stimulation of glucose transport in skeletal muscle by hypoxia

Cartee, Gregory D.; Douen, Andre G.; Ramlal, Toolsie; Klip, Amira; Holloszy, John O.

doi:10.1152/jappl.1991.70.4.1593

Cited by 271 publications

(266 citation statements)

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“…Insulin, hypoxia and contraction stimulate glucose transport into skeletal muscle through the recruitment of glucose transporters to the cell surface [21][22][23]. The mechanism of stimulation of glucose transport by hypoxia has been postulated to be the same as that triggered by muscle contraction and different from that triggered by insulin, since the effects ofmaximum contraction and hypoxia are not additive, whereas those of contraction and insulin are [23][24][25].…”

Section: Resultsmentioning

confidence: 99%

“…The mechanism of stimulation of glucose transport by hypoxia has been postulated to be the same as that triggered by muscle contraction and different from that triggered by insulin, since the effects ofmaximum contraction and hypoxia are not additive, whereas those of contraction and insulin are [23][24][25]. However, the differences or similarities in the mechanisms of action of insulin, hypoxia or contraction have been difficult to dissect, since until now there were no approaches available to prevent specifically one of the responses.…”

Section: Resultsmentioning

confidence: 99%

“…The averaged basal glucose transport rate of untreated cells was 6. 23 The role of P13k in the stimulation of glucose transport by DNP was subsequently assessed by using wortmannin, a specific inhibitor of the enzyme. Table l(a) shows the effects of 100 nM wortmannin on the basal rate of glucose transport and its stimulation by insulin or DNP.…”

Section: Resultsmentioning

confidence: 99%

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Phosphatidylinositol 3-kinase and the actin network are not required for the stimulation of glucose transport caused by mitochondrial uncoupling: comparison with insulin action

Tsakiridis

Vranić

Klip

1995

Biochemical Journal

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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. Insulin, but not dinitrophenol, caused tyrosine phosphorylation of several polypeptides, including the insulin-receptor substrate-1 and mitogen-activated protein kinase. Similarly, insulin, but not dinitrophenol, caused actin reorganization, which was inhibited by wortmannin. We conclude that insulin and dinitrophenol stimulate glucose transport by different mechanisms.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Phosphatidylinositol 3-kinase and the actin network are not required for the stimulation of glucose transport caused by mitochondrial uncoupling: comparison with insulin action

Tsakiridis

Vranić

Klip

1995

Biochemical Journal

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“…The rise in muscle glucose uptake provoked by hypoxia is brought about by translocation of GLUT4 to the plasma membrane [56]. This response is curbed in muscles expressing a dominant-negative AMPKα K45R mutant transgene [54], establishing that in response to hypoxia AMPK elicits GLUT4 mobilisation.…”

Section: Discussionmentioning

confidence: 99%

Troglitazone causes acute mitochondrial membrane depolarisation and an AMPK-mediated increase in glucose phosphorylation in muscle cells

et al. 2005

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Aims/hypothesis: Troglitazone was the first thiazolidinedione (TZD) approved for clinical use, exerting hypoglycaemic effects related to its action as a ligand of the peroxisome proliferator-activated receptor γ receptor in adipocytes. However, emerging evidence suggests that mitochondrial function may be affected by troglitazone, and that skeletal muscle cells acutely respond to troglitazone by enhancing glucose uptake. The aim of the present study was to determine the cellular mechanisms by which troglitazone acutely stimulates glucose utilisation in skeletal muscle cells. Methods: L6 cells overexpressing GLUT4myc were incubated with troglitazone. Glucose uptake, transport and phosphorylation as well as AMP-activated protein kinase (AMPK) signalling and insulin signalling were examined. Changes in mitochondrial membrane potential were measured using the J-aggregate-forming dye JC-1. AMPK signalling was interfered with using AMPK α1/α2 siRNA. Results: Troglitazone acutely (in 10 min) reduced the mitochondrial membrane potential in L6GLUT4myc myotubes and robustly stimulated AMPK activity. Following 30 min of incubation with troglitazone or insulin, 2-deoxyglucose uptake was stimulated 1.5-and 2.1-fold respectively, and in cells treated with troglitazone, a 1.8-fold increase in the 2-deoxyglucose-6-phosphate:2-deoxyglucose ratio was observed. Moreover, contrary to insulin, troglitazone did not significantly stimulate 3-O-methylglucose uptake. Unlike insulin, troglitazone did not increase surface GLUT4myc content and did not increase IRS1-associated phosphatidylinositol 3-kinase activity or Akt phosphorylation on T308 and S473. Interestingly, interfering with troglitazone-induced activation of AMPK by decreasing the expression of the enzyme using siRNA inhibited the stimulation of 2-deoxyglucose uptake by the TZD. Conclusions/interpretation: We propose that troglitazone acutely increases glucose flux in muscle via an AMPK-mediated increase in glucose phosphorylation.

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“…[1][2][3][4]. Peripheral insulin-sensitive tissues, such as fat, skeletal muscles, and heart, express a unique transporter isoform (GLUT4), 1 which is largely confined to an intracellular storage site in the basal, nonstimulated state and becomes recruited to the cell surface under the influence of insulin (5,6) but also other stimuli, such as contraction (7)(8)(9) and hypoxia or anoxia (10,11). This recruitment process is likely to account for a large part of the increase in the rate of glucose uptake observed on stimulation with these agents (12)(13)(14)(15)(16).…”

mentioning

confidence: 99%

Insulin-induced Recruitment of Glucose Transporter 4 (GLUT4) and GLUT1 in Isolated Rat Cardiac Myocytes

Fischer

Thomas

Sevilla

et al. 1997

Journal of Biological Chemistry

151

111

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Using isolated rat cardiomyocytes we have examined: 1) the effect of insulin on the cellular distribution of glucose transporter 4 (GLUT4) and GLUT1, 2) the total amount of these transporters, and 3) the co-localization of GLUT4, GLUT1, and secretory carrier membrane proteins (SCAMPs) in intracellular membranes. Insulin induced 5.7-and 2.7-fold increases in GLUT4 and GLUT1 at the cell surface, respectively, as determined by the nonpermeant photoaffinity label [ 3 H]2-N-[4(1-azi-2,2,2-trifluoroethyl)benzoyl]-1,3-bis-(D-mannos-4-yloxy)propyl-2-amine. The total amount of GLUT1, as determined by quantitative Western blot analysis of cell homogenates, was found to represent a substantial fraction (ϳ30%) of the total glucose transporter content. Intracellular GLUT4-containing vesicles were immunoisolated from low density microsomes by using monoclonal anti-GLUT4 (1F8) or anti-SCAMP antibodies (3F8) coupled to either agarose or acrylamide. With these different immunoisolation conditions two GLUT4 membrane pools were found in nonstimulated cells: one pool with a high proportion of GLUT4 and a low content in GLUT1 and SCAMP 39 (pool 1) and a second GLUT4 pool with a high content of GLUT1 and SCAMP 39 (pool 2). The existence of pool 1 was confirmed by immunotitration of intracellular GLUT4 membranes with 1F8-acrylamide. Acute insulin treatment caused the depletion of GLUT4 in both pools and of GLUT1 and SCAMP 39 in pool 2. In conclusion: 1) GLUT4 is the major glucose transporter to be recruited to the surface of cardiomyocytes in response to insulin; 2) these cells express a high level of GLUT1; and 3) intracellular GLUT4-containing vesicles consist of at least two populations, which is compatible with recently proposed models of GLUT4 trafficking in adipocytes.

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Stimulation of glucose transport in skeletal muscle by hypoxia

Cited by 271 publications

References 0 publications

Phosphatidylinositol 3-kinase and the actin network are not required for the stimulation of glucose transport caused by mitochondrial uncoupling: comparison with insulin action

Phosphatidylinositol 3-kinase and the actin network are not required for the stimulation of glucose transport caused by mitochondrial uncoupling: comparison with insulin action

Troglitazone causes acute mitochondrial membrane depolarisation and an AMPK-mediated increase in glucose phosphorylation in muscle cells

Insulin-induced Recruitment of Glucose Transporter 4 (GLUT4) and GLUT1 in Isolated Rat Cardiac Myocytes

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