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ACTH 1–24 Releases a Protein from Synaptosomal Plasma Membranes
Author(s) -
Aloyo V. J.,
Zwiers H.,
Gispen W. H.
Publication year - 1982
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.1471-4159.1982.tb05323.x
Subject(s) - membrane , phosphorylation , endogeny , membrane protein , synaptosome , biochemistry , kinase , protein kinase a , microbiology and biotechnology , chemistry , biology
Brain membranes contain several protein kinases, all of which appear to play a role in the regulation of neuronal functioning. These membranes also contain numerous (phospho) proteins. It has been proposed that the degree of phosphorylation of some of these proteins may affect neuronal membrane properties. In a series of previous reports we showed that ACTH 1‐24 inhibits the endogenous phosphorylation of several synaptosomal plasmamembrane (SPM) proteins including the B‐50 protein. Although we have speculated that the degree of phosphorylation of B‐50 may be important in regulating the turnover of membrane (poly)‐phosphoinositides, the exact nature of the interaction between ACTH 1‐24 and B‐50/B‐50 protein kinase is unknown. The purpose of the present study was to determine whether treatment of SPM with ACTH 1‐24 will lead to a specific release of proteins from SPM. We found that ACTH 1‐24 specifically releases a 41,000 M r protein from rat brain SPM. Although we are not certain about the biological significance of the release of this polypeptide, it is of sufficient interest for further research in view of the lack of success of finding binding of labeled ACTH to brain membranes.