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Phosphorylation of Chromatin Proteins in Cerebral Anoxia and Ischemia
Author(s) -
Yanagihara T.
Publication year - 1980
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.1471-4159.1980.tb07877.x
Subject(s) - gerbil , biochemistry , phosphorylation , chemistry , gel electrophoresis , in vitro , ischemia , fraction (chemistry) , polyacrylamide gel electrophoresis , chromatography , enzyme , medicine
Phosphorylation of nuclear protein was investigated in cerebral anoxia up to 30 min with rabbit brain and in cerebral ischemia up to 6 h with gerbil brain in vitro. Isolated nuclei were incubated in the presence of [γ‐ 32 P]ATP and were then fractionated into the NaCl‐soluble, HCl‐soluble, and phenol‐soluble protein fraction. Each protein fraction was further separated by gel electrophoresis, and profiles of 32 P incorporation were evaluated in these pathophysiological conditions. 32 P incorporation of the acidic phenol‐soluble nonhistone chromatin protein became significantly suppressed in cerebral anoxia after 15 min, and there were decreases of 32 P incorporation in protein with high molecular weight and increase in protein with low molecular weight on gel electrophoresis. With gerbil brain nuclei, 32 P incorporation into the NaCl‐soluble and HCl‐soluble fraction was increased without significant de‐crease in the phenol‐soluble fraction after an ischemic period of 3 h. However, further separation of the phenol‐soluble fraction demonstrated decrease of 32 P incorporation in protein with high molecular weight and increase in protein with low molecular weight. At present, the significance of these findings, particularly in relation to chromatin template activity or irreversibility of these pathophysiological conditions, is not clear.