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Journal of Clinical Endocrinology & Metabolism, Vol 57, 872-874, Copyright © 1983 by Endocrine Society


ARTICLES

Calcium- and lipid-dependent protein phosphorylation in the human ovary

MR Clark, JS Davis and WJ Lemaire

The cytosol of human ovarian tissues was observed to promote protein phosphorylation in the combined presence of Ca2+, 1,2-diolein, and phosphatidylserine. Ca2+ alone or lipid alone did not produce full activation of this protein kinase(s). The addition of human erythrocyte calmodulin to the assay mixture, in the presence or absence of Ca2+, had no effect on protein kinase activity. Phosphorylation of cytosol proteins ranging in mol wt from 10,000 to 200,000 was selectively increased by Ca2+ plus lipid. This protein kinase activity may play a crucial role in the intracellular transmission of the action of hormones affecting cellular Ca2+ flux and/or phospholipid metabolism.


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M. Liao, Y. Zhang, and M. L. Dufau
Protein Kinase C{alpha}-Induced Derepression of the Human Luteinizing Hormone Receptor Gene Transcription through ERK-Mediated Release of HDAC1/Sin3A Repressor Complex from Sp1 Sites
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[Abstract] [Full Text] [PDF]




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