Substrates for protein kinase C in a cell free preparation of rat aorta smooth muscles
Protein phosphorylation has been studied in a cell free system of rat aorta smooth muscles. Addition of Ca/sup 2 +/ caused phosphorylation of several proteins. The addition of phosphatidylserine or calmodulin together with Ca/sup 2 +/ further increased the phosphorylation of proteins with apparent molecular weights of 20 and 92.5 kilodaltons. The activators of protein kinase C, 12-0-tetradecanoylphorbol-13-acetate and 1,2-diolein, increased phosphorylation of the protein bands of similar molecular weight to those increased by phosphatidylserine in the presence of Ca/sup 2 +/, whereas the biologically inactive phorbol ester, 4 ..cap alpha..-phorbol-12,13 didecanoate (4 ..cap alpha.. PDD) failed to change the pattern of protein phosphorylation. These results show that proteins present in smooth muscle of rat aorta with molecular weights of 20 and 92.5 kilodaltons are substrates for protein kinase C.
- Research Organization:
- National Institute of Mental Health, Washington, DC (USA)
- OSTI ID:
- 5238450
- Journal Information:
- Life Sci.; (United States), Journal Name: Life Sci.; (United States) Vol. 42:13; ISSN LIFSA
- Country of Publication:
- United States
- Language:
- English
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ALKALINE EARTH METAL COMPOUNDS
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