Endogenous Phosphorylation of a 61,000 Dalton Hippocampal Protein Increases Following Traumatic Brain Injury

Keyi Yang, William C. Taft, C. Edward Dixon, Robert K. yu, Ronald L. Hayes

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Acute biochemical consequences of moderate traumatic brain injury (TBI) include activation of kinases, including protein kinase C (PKC). To determine the possible consequences of PKC activation at the substrate level, we have examined protein phosphorylation patterns 1 h following injury. Although the phosphorylation of most proteins remained unchanged following injury, we observed a significant increase in the phosphorylation of a 61,000 dalton protein (TBI61) in injured rat hippocampus (121 % higher than sham control) in vitro. TBI61 phosphorylation could be enhanced by phosphatidyl serine and diacylglycerol or by addition of exogenous PKC. In addition, TBI61 phosphorylation was inhibited by the PKC inhibitor, staurosporine, suggesting further that this protein may be a PKC substrate. These data suggest that TBI increases the phosphorylation of a 61 kD hippocampal protein in vitro. Increases in the protein level and activity of PKC could contribute to this increased phosphorylation.

Original languageEnglish (US)
Pages (from-to)523-532
Number of pages10
JournalJournal of Neurotrauma
Issue number5
Publication statusPublished - Oct 1994
Externally publishedYes


ASJC Scopus subject areas

  • Clinical Neurology

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