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

Martin R. Clark, John S. Davis, William J. Lemaire

Research output: Contribution to journalArticle

23 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)872-874
Number of pages3
JournalJournal of Clinical Endocrinology and Metabolism
Volume57
Issue number4
DOIs
StatePublished - Oct 1983

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Biochemistry
  • Endocrinology
  • Clinical Biochemistry
  • Biochemistry, medical

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