Stimulation of Protein Phosphatase-1 Activity by Phorbol Esters. Evaluation of the regulatory role of protein kinase C in insulin action.
作者： M. Srinivasan , N. Begum
DOI: 10.1016/S0021-9258(19)89441-3
关键词:
摘要: In this study, we examined the role of insulin, protein kinase C (PKC) and mitogen-activated (MAPK) cascade in activation phosphatase-1 (PP-1) by using three complementary approaches. First, differentiated L6 cells were acutely exposed to 12-O-tetradecanoylphorbol-13-acetate (TPA, 400 nM) activate PKC. these cells, TPA caused 32% stimulation PP-1 activity. The was comparable insulin (t1/2 = 1 min EC50 5 with a maximum effect min. effects not additive. Insulin also stimulated MAPK (> 2-fold increase over basal, myelin basic as substrate). ML-9, myosin light chain inhibitor, blocked on both activation. second approach, PKC down-regulated chronic treatment TPA. subsequent blocked, without an basal enzyme levels. third two selective inhibitors PKC, calphostin chelerythrine chloride, used inhibit These completely prevented insulin-induced translocation plasma membranes. We conclude that plays important via cascade.
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