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CYCLIC AMP‐DEPENDENT PROTEIN KINASE ACTIVITY AND SYNAPTOSOMAL PROTEIN PHOSPHORYLATION IN THE BRAINS OF AGED RATS
Author(s) -
Schmidt Michael J.,
Truex Lewis L.,
Conway Richard G.,
Routtenberg Aryeh
Publication year - 1979
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.1471-4159.1979.tb00356.x
Subject(s) - phosphorylation , protein kinase a , hippocampus , cerebral cortex , synaptosome , cerebellum , protein phosphorylation , stimulation , biology , medicine , endocrinology , kinase , endogeny , chemistry , biochemistry , in vitro
— The activity of soluble protein kinase and phosphorylation of endogenous synaptosomal proteins were studied in vitro , in the hippocampus and cerebral cortex of rats 3, 12, or 24 months of age. No between‐age differences in the activity of cyclic AMP‐dependent or independent protein kinase were detected in either brain region. The degree of stimulation by cyclic AMP and the apparent K a , for cyclic AMP were similar at all stages. Cyclic AMP stimulated the phosphorylation of synaptosomal proteins from the cerebral cortex, hippocampus, caudate nucleus, and cerebellum of rats at all ages. There were no significant differences across age in the extent of phosphorylation of any membrane proteins in any brain region. The number and staining density of synaptosornal proteins separated by polyacrylamide gel electrophoresis were also similar at all ages. These studies indicate that the cyclic AMP‐dependent phosphorylation system in the rat brain does not change during advanced aging.