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Volume 17, Number 14, Issue of July 15, 1997 pp. 5357-5365
Copyright ©1997 Society for NeurosciencePostsynaptic Inhibitors of Calcium/Calmodulin-Dependent Protein Kinase Type II Block Induction But Not Maintenance of Pairing-Induced Long-Term Potentiation
Received Feb. 12, 1997; revised May 5, 1997; accepted May 7, 1997.
Nikolai Otmakhov, Leslie C. Griffith, and John E. Lisman Volen Center for Complex Systems and Biology Department, Brandeis University, Waltham, Massachusetts 02254
The role of postsynaptic kinases in the induction and maintenance of long-term potentiation (LTP) was studied in the CA1 region of the rat hippocampal slice. A peptide inhibitor for the catalytic domain of calcium/calmodulin-dependent protein kinase type II (CaM-kinase) was applied through a perfused patch pipette. The inhibitor completely blocked both the short-term potentiation and LTP induced by a pairing protocol. This indicates that the kinase or kinases affected by the peptide are downstream from depolarization in the LTP cascade. The ability to block LTP required that measures be taken to interfere with degradation of the peptide kinase inhibitor by endogenous proteases; either addition of protease inhibitors or modifications of the peptide itself greatly enhanced the effectiveness of the peptide. Protease inhibitors by themselves or control peptide did not block LTP induction. To study the effect of kinase inhibitor on LTP maintenance, we induced LTP in one pathway. Subsequent introduction of the kinase inhibitor blocked the induction of LTP in a second pathway, but it did not affect maintenance of LTP in the first. The implications for the role of kinases in LTP maintenance are discussed.
Key words: long-term potentiation; calcium/calmodulin-dependent kinase; peptide inhibitors; hippocampal slices; whole-cell recording; intracellular perfusion; protease inhibitors; fluorescent imaging
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