Send to

Choose Destination
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

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


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.

[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Georg Thieme Verlag Stuttgart, New York
Loading ...
Support Center