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

Abstract:

:Abstract Type V adenylyl cyclase (AC) was stably over-expressed 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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Kawabe Ji,Ebina T,Toya Y,Oka N,Schwencke C,Duzic E,Ishikawa Y

doi

10.1016/0014-5793(96)00331-6

subject

Has Abstract

pub_date

1996-04-22 00:00:00

pages

273-6

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014579396003316

journal_volume

384

pub_type

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