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Wiley InterScience | ||||||||||||||
  Journal of NeurochemistryVolume 68 Issue 5, Pages 1960 - 1967 Published Online: 18 Nov 2002 Journal compilation © 2010 International Society for Neurochemistry Published for the International Society for Neurochemistry
Abstract | Full Text: PDF (Size: 989K) | Related Articles | Citation Tracking  Increased Phosphorylation of Myelin Basic Protein During Hippocampal Long-Term Potentiation The present address of Dr. S.-J. Chen is Department of Physiology, SUNY, Buffalo, NY 14051, U.S.A. The present address of Dr. E. Klann is Department of Neuroscience, University of Pittsburgh, Pittsburgh, PA 15260, U.S.A. Copyright Blackwell Science Inc KEYWORDS Long-term potentiation • Myelin basic protein • Protein kinase C • Phosphorylation • Back-phosphorylation ABSTRACTAbstract: Hippocampal long-term potentiation (LTP) is a long-lasting and rapidly induced increase in synaptic strength. Previous experiments have determined that persistent activation of protein kinase C (PKC) contributes to the early maintenance phase of LTP (E-LTP). Using the back-phosphorylation method, we observed an increase in the phosphorylation of a 21-kDa PKC substrate, termed p21, 45 min after LTP was induced in the CA1 region of the hippocampus. p21 was found to have the same apparent molecular weight as the 18.5-kDa isoform of myelin basic protein (MBP) and was recognized by an antibody to MBP in western blotting and immunoprecipitation. Furthermore, p21 from control and potentiated hippocampal slices and purified MBP have identical phosphopeptide maps when back-phosphorylated and then digested with either endoproteinase Lys-C or endoproteinase Asp-N, suggesting that p21 and MBP are identical proteins. As there was no observed change in the amount of MBP in LTP, the increase in MBP phosphorylation during LTP cannot be explained by a change in the amount of protein. From these experiments, we conclude that the phosphorylation of the 18.5-kDa isoform of MBP is increased during E-LTP. Received October 24, 1996; revised manuscript received December 26, 1996; accepted December 31, 1996. | 
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