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Effect of Digestion with Phospholipase A 2 on Endogenous Protein Phosphorylation in Particulate Fractions from Rat Brain Synaptosomes
Author(s) -
Dosemeci Ayse,
Rodnight Richard
Publication year - 1987
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1987.tb05637.x
Subject(s) - phosphorylation , synaptic vesicle , synapsin i , phospholipase , endogeny , vesicle , protein phosphorylation , biochemistry , phospholipase c , calmodulin , biology , phospholipase a , chemistry , membrane , phospholipase d , phospholipase a2 , microbiology and biotechnology , enzyme , protein kinase a
The endogenous phosphorylation of synapsin 1 in cyclic AMP‐containing media was greatly decreased by digestion of synaptic vesicles and synaptosomal membranes with phospholipase A 2 , suggesting that the system is functionally dependent on the membrane structure. Treatment of the synaptic vesicle fraction with phospholipase A 2 also caused a small but significant inhibition of the Ca 2+ /calmo‐dulin‐dependent phosphorylation of the same protein. The Ca 2+ /calmodulin‐dependent phosphorylation of other major acceptors, and the basal phosphorylation of a 52‐kD acceptor enriched in the vesicle fraction, remained unchanged after cleavage of the membrane phospholipids with phospholipase A 2 . The significance of the selective effect of phospholipase A 2 treatment on endogenous membrane phosphorylation is discussed.