Insulin stimulation of glucose uptake can be mediated by diacylglycerol in adipocytes
- 1 October 1988
- journal article
- Published by Springer Nature in Nature
- Vol. 335 (6190), 554-556
- https://doi.org/10.1038/335554a0
Abstract
An early effect of insulin in adipocytes is to stimulate glucose uptake. The increased uptake appears to be due to mobilization of glucose transporters from an intracellular location to the plasma membrane and to enhanced intrinsic activity of the transporters. Little is known about the insulin-generated signals causing these changes. Phorbol esters have been shown to mimic the insulin effect, but phosphorylation of the transporter does not seem to be involved. A phospho-oligosaccharide was recently shown to mimic the effects of insulin on protein phosphorylation, suggesting that it could be a mediator for some intracellular metabolic effects of the hormone, but it did not affect glucose uptake. A diacyglycerol is produced in the plasma membrane in conjunction with the generation of the phospho-oligosaccharide. Here I show that added 1,2-diacylglycerols potently increase glucose transporter-mediated uptake of glucose in rat adipocytes, but without activation of protein kinase C.Keywords
This publication has 18 references indexed in Scilit:
- Effects of insulin on glucose transport and glucose transporters in rat heartBiochemical Journal, 1988
- Phorbol esters imitate in rat fat-cells the full effect of insulin on glucose-carrier translocation, but not on 3-O-methylglucose-transport activityBiochemical Journal, 1988
- Qualitative and quantitative comparison of glucose transport activity and glucose transporter concentration in plasma membranes from basal and insulin-stimulated rat adipose cellsBiochemical Journal, 1987
- Phospho-dephospho-control by insulin is mimicked by a phospho-oligosaccharide in adipocytesNature, 1987
- Glucose transport and antilipolysis are differentially regulated by the polar head group of an insulin-sensitive glycophospholipid.Proceedings of the National Academy of Sciences, 1987
- Purification of a phosphatidylinositol-glycan-specific phospholipase C from liver plasma membranes: a possible target of insulin action.Proceedings of the National Academy of Sciences, 1987
- Insulin-Stimulated Hydrolysis of a Novel Glycolipid Generates Modulators of cAMP PhosphodiesteraseScience, 1986
- Low concentrations of bile salts increase the rate of spontaneous phospholipid transfer between vesiclesBiochemistry, 1986
- Effect of protein kinase C activation and Ca2+ mobilization on hexose transport in Swiss 3T3 cellsBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1986
- Evidence that insulin causes translocation of glucose transport activity to the plasma membrane from an intracellular storage site.Proceedings of the National Academy of Sciences, 1980