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Phorbol 12-myristate 13-acetate Inhibits the Antilipolytic Action of Insulin, Probably via the Activity of Protein Kinase Cε

Phorbol 12-myristate 13-acetate Inhibits the Antilipolytic Action of Insulin, Probably via the Activity of Protein Kinase Cε

Jiro Nakamura

Eur J Pharmacol. 2010 Dec 1;648(1-3):188-94.

PMID: 20826143

Abstract:

Protein kinase CβI (PKCβI) mediates insulin signaling and attenuates β1-adrenoceptor-stimulated lipolysis. In this work, the effect of the PKC activator phorbol 12-myristate 13-acetate (PMA) on the antilipolytic action of insulin was determined by analyzing lipolysis induced by a β3-adrenoceptor agonist CL 316243. PMA inhibited the insulin antilipolytic action. The pan-PKC inhibitors GF 109203X and chelerythrine inhibited the PMA effect, but the PKCα/β inhibitors Gö 6976 and CGP 53353 did not. Exposure of cells to PMA downregulated PKCs α, βI, and δ within 3 h and PKCε within 12 h. The effect of PMA on insulin action greatly diminished when PKCε was downregulated. Inhibitors of phosphatidylinositol 3-kinase (PI3-K), Akt, and phosphodiesterase 3B (PDE3B) diminished the PMA effect. PMA inhibited insulin-stimulated phosphorylation of Tyr in insulin receptor β subunit and Ser/Thr in Akt. These data suggest that PMA inhibits the antilipolytic signal mediated by the insulin receptor, PI3-K, Akt, and PDE3B. The most probable target of PMA is PKCε.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP145915602-A	CGP-53353		145915-60-2	Price

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