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Horm Metab Res 1990; 22(1): 29-32
DOI: 10.1055/s-2007-1004842
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Involvement of Protein Kinase C in the Regulation of Cortisol Production by Guinea Pig Adrenocortical Cells

T. Nishikawa, Akiko Yoshida, Y. Tamura, S. Yoshida
  • Department of Internal Medicine (II), School of Medicine, Chiba University, Chiba City, Chiba, Japan
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Publication History

1988

1989

Publication Date:
14 March 2008 (online)

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Summary

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-Tetradecanoyl-phorbol-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.

Key words

TPA - Protein Kinase C - Adrenocortical Cells - Steroidogenesis - Guinea Pig

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