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Horm Metab Res. 1990 Jan;22(1):29-32.

Involvement of protein kinase C in the regulation of cortisol production by guinea pig adrenocortical cells.

Author information

1
Department of Internal Medicine (II), School of Medicine, Chiba University, Japan.

Abstract

Cytosol of the guinea pig adrenals was found to contain a protein kinase which was dependent on the presence of both calcium and phospholipids (phosphatidylserine and diolein), i.e., calcium/phospholipid-dependent protein kinase (protein kinase C). The peak of protein kinase C was separated from type II cAMP-dependent protein kinase by DE-52 chromatography. 12-0-Tetradecanoylphorbol-13-acetate (TPA) caused dose-dependent increments of cortisol formation without affecting cAMP formation by guinea pig adrenocortical cells as well as angiotensin II did. TPA-activated cortisol production was blocked by the addition of aminoglutethimide and cycloheximide, suggesting that the site of action of TPA might be located at a point before the production of pregnenolone in the mitochondria. Since TPA showed an increase in the cortisol production, protein kinase C may be involved in modulating steroidogenesis in the guinea pig adrenals in addition to the classical cAMP-dependent protein kinase pathway.

PMID:
1689688
DOI:
10.1055/s-2007-1004842
[Indexed for MEDLINE]

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