Increased Phosphorylation of a 17‐kDa Protein Kinase C Substrate (P17) in Long‐Term Potentiation

Eric Klann, Shu‐Jen ‐J Chen, J. David Sweatt

Research output: Contribution to journalArticlepeer-review


Abstract: Hippocampal long‐term potentiation (LTP) is a persistent increase in the efficacy of synaptic transmission, which is widely thought to be a cellular mechanism that could contribute to learning and memory. Studies on the biochemical mechanisms underlying LTP suggest the involvement of protein kinases in both LTP induction and maintenance. In this report we describe an LTP‐associated increase in the phosphorylation in vitro of a 17‐kDa protein kinase C (PKC) substrate protein, which we have termed P17, in homogenates from the CA1 region of rat hippocampal slices. This LTP‐associated increase in phosphorylation was expressed independent of significant levels of free Ca2+, as phosphorylation reactions were performed in the presence of 500 μM EGTA. The increased phosphorylation of P17 was substantially inhibited by PKC19–36, a selective inhibitor of PKC. These data support the model that persistent PKC activation contributes to the maintenance of LTP and implicate P17 as a potential target for PKC in the CA1 region of the hippocampus.

Original languageEnglish (US)
Pages (from-to)1576-1579
Number of pages4
JournalJournal of Neurochemistry
Issue number4
StatePublished - Apr 1992


  • Calcium
  • Long‐term potentiation
  • Protein kinase C
  • Synaptic plasticity

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience


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