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The upregulating effect of insulin and vanadate on cell surface insulin receptors in rat adipocytes is modulated by glucose and energy availability.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences, Endocrinology, Diabetes and Metabolism.
2000 (English)In: Hormone and Metabolic Research, ISSN 0018-5043, E-ISSN 1439-4286, Vol. 32, no 8, 310-5 p.Article in journal (Refereed) Published
Abstract [en]

The aim of this study was to further characterize the rapid effects of insulin and the tyrosine phosphatase inhibitor vanadate to amplify cell surface insulin binding capacity in isolated rat adipocytes. The effect of 20 min insulin treatment (1000 microU/ml) was 2- to 3-fold (p < 0.01) when cells were treated in medium containing 5.6 mM D-glucose, but it was totally absent in glucose-free medium. Other carbon energy sources, such as fructose and pyruvate, could only partly substitute for D-glucose, with an approximately 1.5-fold insulin effect. Moreover, inhibiting transmembrane glucose transport with cytochalasin B completely blocked the effect of insulin to enhance cell surface binding. The effect of vanadate was only partly glucose-dependent, since a submaximal effect (1.5- to 2-fold, p<0.05) was seen also in the absence of glucose. The tyrosine kinase inhibitor genistein markedly blunted the effect of vanadate (from 3- to 4-fold to approximately 2-fold, p < 0.05) also indicating the importance of tyrosine phosphorylation-related mechanisms in the upregulation of cell surface insulin binding. Glycosylation of insulin receptors as a mechanism for this effect appears unlikely since neither the effect of insulin nor that of vanadate was altered by the glycosylation inhibitor tunicamycin. The time course for the insulin effect displayed a long duration (at least 6 h), suggesting a maintenance role of insulin keeping its receptors accessible for ligand binding at the cell surface. In conclusion, the effect of insulin and vanadate to upregulate cell-surface insulin receptors is energy-dependent and to some extent specifically glucose-dependent.

Place, publisher, year, edition, pages
2000. Vol. 32, no 8, 310-5 p.
National Category
Medical and Health Sciences
URN: urn:nbn:se:uu:diva-211316DOI: 10.1055/s-2007-978642PubMedID: 10983626OAI: oai:DiVA.org:uu-211316DiVA: diva2:681547
Available from: 2013-12-20 Created: 2013-11-21 Last updated: 2013-12-20

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