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Complexity of cyclic AMP‐dependent phosphoproteins in membranes from brain tissue containing synapses
Author(s) -
Reddington M.,
Mehl E.
Publication year - 1977
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(77)80053-7
Subject(s) - physics , citation , combinatorics , mathematics , computer science , library science
There is now considerable evidence that some of the effects of neurotransmitter substances on their receptor cells are mediated through the synthesis of adenosine 3’5’-monophosphate (cyclic AMP) (see [ 11). A number of studies have further suggested that such effects might occur through modification of the state of phosphorylation of synaptic membrane proteins. In intact cell-containing preparations of nervous tissue, for example, protein phosphorylation is stimulated by various putative neurotransmitters [2-51. This may be related to the phosphorylation of endogenous proteins in synaptic membrane fragments by intrinsic cyclic AMP-stimulated protein kinase activity [6-l 11. Cyclic AMP-stimulated phosphorylation of at least four protein components was found in such preparations [9] . If any of these proteins were specifically involved in synaptic transmission it would be expected that they would only occur in tissue containing synapses. We have therefore investigated the distribution of phosphorylated proteins in crude membrane fractions from two regions of bovine cerbral cortex: grey matter, which contains neurons with synaptic contacts as well as other cells and white matter, which lacks synaptic contacts and consists predominantly of oligodendroglial cells.