Stimulation by phosphatidylserine and calmodulin of calcium-dependent phosphorylation of endogenous proteins from cerebral cortex

The Ca2+-dependent phosphorylation of a number of proteins in the cytosol of the rat or guinea pig cerebral cortex was profoundly stimulated by phosphatidylserine; calmodulin, on the other hand, had only a minimal effect. The Ca2+-dependent phosphorylation of different proteins from the total partic...

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Bibliographic Details
Published in:The Journal of biological chemistry 1980-12, Vol.255 (24), p.12042-12046
Main Authors: Wrenn, R W, Katoh, N, Wise, B C, Kuo, J F
Format: Article
Language:English
Subjects:
Animals
Calcium - pharmacology
Calcium-Binding Proteins - pharmacology
Calmodulin - pharmacology
Cerebral Cortex - metabolism
Cytosol - metabolism
Guinea Pigs
Male
Molecular Weight
Nerve Tissue Proteins - isolation & purification
Nerve Tissue Proteins - metabolism
Phosphatidylserines - pharmacology
Phosphorylation
Protein Kinases - isolation & purification
Protein Kinases - metabolism
Rats
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Summary:The Ca2+-dependent phosphorylation of a number of proteins in the cytosol of the rat or guinea pig cerebral cortex was profoundly stimulated by phosphatidylserine; calmodulin, on the other hand, had only a minimal effect. The Ca2+-dependent phosphorylation of different proteins from the total particulate fraction of the same tissue, in comparison, was specifically stimulated by either phosphatidylserine or calmodulin. The present findings, in line with the phospholipid-sensitive Ca2+-dependent protein kinase recently recognized, suggest an involvement of phospholipid in regulating Ca2+-dependent phosphorylation of endogenous substrate proteins. This new system presumably functions independent or in a complementary manner with the calmodulin-sensitive Ca2+-dependent protein phosphorylation system previously reported by others.
ISSN:0021-9258
1083-351X
DOI:10.1016/s0021-9258(19)70241-5