Regulation of type V adenylyl cyclase by PMA-sensitive and -insensitive protein kinase C isoenzymes in intact cells

被引：46

作者：

Kawabe, J ^{[1
]}

Ebina, T ^{[1
]}

Toya, Y ^{[1
]}

Oka, N ^{[1
]}

Schwencke, C ^{[1
]}

Duzic, E ^{[1
]}

Ishikawa, Y ^{[1
]}

机构：

[1] CADUS PHARMACEUT CO,TARRYTOWN,NY 10571

来源：

FEBS LETTERS | 1996年 / 384卷 / 03期

关键词：

adenylylcyclase; protein kinase C; phorbol ester; insulin; cyclic AMP;

D O I：

10.1016/0014-5793(96)00331-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Type V adenylyl cyclase (AC) was stably overexpressed in HEK293 cells (293AC-V). Forskolin-stimulated cAMP accumulation in 293AC-V was 5 times as great as that in control cells. PMA, a protein kinase C (PKC) activator, enhanced cAMP accumulation in 293AC-V cells dose-and time-dependently and this enhancement was abolished by staurosporine. Insulin also enhanced cAMP accumulation in 293AC-V cells. Co-transfection of PKC-zeta, but not PKC-alpha, potentiated the effects of insulin. These data suggest that type V AC activity is regulated in cells by PKC isoenzymes through different extracellular stimuli.

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页码：273 / 276

页数：4

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