Ouyang, Yannan and Kantor, David and Harris, Kristen M. and Schuman, Erin M. and Kennedy, Mary B. (1997) Visualization of the distribution of autophosphorylated calcium/calmodulin-dependent protein kinase II after tetanic stimulation in the CA1 area of the hippocampus. Journal of Neuroscience, 17 (14). pp. 5416-5427. ISSN 0270-6474 http://resolver.caltech.edu/CaltechAUTHORS:20120424-154221603
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Autophosphorylation of calcium/calmodulin-dependent protein kinase II (CaMKII) at threonine-286 produces Ca2+-independent kinase activity and has been proposed to be involved in induction of long-term potentiation by tetanic stimulation in the hippocampus. We have used an immunocytochemical method to visualize and quantify the pattern of autophosphorylation of CaMKII in hippocampal slices after tetanization of the Schaffer collateral pathway. Thirty minutes after tetanic stimulation, autophosphorylated CaM kinase II (P-CaMKII) is significantly increased in area CA1 both in apical dendrites and in pyramidal cell somas. In apical dendrites, this increase is accompanied by an equally significant increase in staining for nonphosphorylated CaM kinase II. Thus, the increase in P-CaMKII appears to be secondary to an increase in the total amount of CaMKII. In neuronal somas, however, the increase in P-CaMKII is not accompanied by an increase in the total amount of CaMKII. We suggest that tetanic stimulation of the Schaffer collateral pathway may induce new synthesis of CaMKII molecules in the apical dendrites, which contain mRNA encoding its alpha-subunit. In neuronal somas, however, tetanic stimulation appears to result in long-lasting increases in P-CaMKII independent of an increase in the total amount of CaMKII. Our findings are consistent with a role for autophosphorylation of CaMKII in the induction and/or maintenance of long-term potentiation, but they indicate that the effects of tetanus on the kinase and its activity are not confined to synapses and may involve induction of new synthesis of kinase in dendrites as well as increases in the level of autophosphorylated kinase.
|Additional Information:||© 1997 Society for Neuroscience. Received Feb. 26, 1997; revised May 6, 1997; accepted May 7, 1997. This work was supported by National Institutes of Health Grants MH49176 and NS17660 (M.B.K.), NS32792 (E.M.S.), NS21184 (K.M.H.); National Science Foundation Grant GER-9023446 (M.B.K.); and grants from the Alfred P. Sloan Foundation, Beckman Foundation, John Merck Fund, and PEW Charitable Trusts (E.M.S.). We thank Leslie Schenker for expert technical assistance, Mary Mosier and Kathryn Stofer for help with some of the experiments, Scott Fraser for valuable technical advice, and Kathleen Branson for help with preparation of this manuscript.|
|Subject Keywords:||long-term potentiation; protein phosphorylation; synapse; synaptic regulation; synaptic plasticity; immunocytochemistry; hippocampal slices|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Melanie Stefan|
|Deposited On:||25 Apr 2012 21:01|
|Last Modified:||26 Dec 2012 15:07|
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