DECREASED INSULIN RESPONSIVENESS IN FAT CELLS RENDERED PROTEIN KINASE C-DEFICIENT BY A TREATMENT WITH A PHORBOL ESTER.
- 1 May 1987
- journal article
- research article
- Published by The Endocrine Society in Endocrinology
- Vol. 120 (5) , 2192-2194
- https://doi.org/10.1210/endo-120-5-2192
Abstract
Insulin stimulation of 2-deoxyglucose transport and lipogenesis from glucose was examined in fat cells in which protein kinase C had been down-modulated by a 3 h pretreatment with 5 .times. 10-7 M 4.beta.-phorbol 12.beta.-myristate, 13.alpha.-acetate (PMA). As compared to control fat cells, the down-modulated cells exhibited a 55-65% decrease in insulin responsiveness with no change in either the hormone sensitivity or the insulin receptor affinity. The present study shows that fat cells made protein kinase C-deficient by chronic treatment with PMA exhibit an insulin-resistant state, distal to the initial step of hormone binding.This publication has 5 references indexed in Scilit:
- Insulin provokes a transient activation of phospholipase C in the rat epididymal fat pad.Journal of Biological Chemistry, 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
- Phorbol esters, but not insulin, promote depletion of cytosolic protein kinase C in rat adipocytesBiochemical and Biophysical Research Communications, 1986
- Growth factor-stimulated protein phosphorylation in 3T3-L1 cells. Evidence for protein kinase C-dependent and -independent pathways.Journal of Biological Chemistry, 1985
- Insulin-stimulated phosphoinositide metabolism in isolated fat cells.Journal of Biological Chemistry, 1985