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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1999-2-16
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pubmed:abstractText |
The phosphorylation state of three identified neural-specific protein kinase C substrates (RC3, GAP-43/B-50, and MARCKS) was monitored in hippocampal slices of mice lacking the gamma-subtype of protein kinase C and wild-type controls by quantitative immunoprecipitation following 32Pi labeling. Depolarization with potassium, activation of glutamate receptors with glutamate, or direct stimulation of protein kinase C with a phorbol ester increased RC3 phosphorylation in wild-type animals but failed to affect RC3 phosphorylation in mice lacking the gamma-subtype of protein kinase C. Our results suggests the following biochemical pathway: activation of a postsynaptic (metabotropic) glutamate receptor stimulates the gamma-subtype of protein kinase C, which in turn phosphorylates RC3. The inability to increase RC3 phosphorylation in mice lacking the gamma-subtype of protein kinase C by membrane depolarization or glutamate receptor activation may contribute to the spatial learning deficits and impaired hippocampal LTP observed in these mice.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GAP-43 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neurogranin,
http://linkedlifedata.com/resource/pubmed/chemical/Nrgn protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/myristoylated alanine-rich C...,
http://linkedlifedata.com/resource/pubmed/chemical/protein kinase C gamma
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1873-4
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:9890937-Animals,
pubmed-meshheading:9890937-Calmodulin-Binding Proteins,
pubmed-meshheading:9890937-GAP-43 Protein,
pubmed-meshheading:9890937-Hippocampus,
pubmed-meshheading:9890937-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:9890937-Isoenzymes,
pubmed-meshheading:9890937-Membrane Proteins,
pubmed-meshheading:9890937-Mice,
pubmed-meshheading:9890937-Mice, Knockout,
pubmed-meshheading:9890937-Nerve Tissue Proteins,
pubmed-meshheading:9890937-Neurogranin,
pubmed-meshheading:9890937-Phosphorylation,
pubmed-meshheading:9890937-Protein Kinase C,
pubmed-meshheading:9890937-Proteins,
pubmed-meshheading:9890937-Substrate Specificity
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pubmed:year |
1999
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pubmed:articleTitle |
Substrate phosphorylation in the protein kinase Cgamma knockout mouse.
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pubmed:affiliation |
Rudolf Magnus Institute for Neurosciences, Department of Medical Pharmacology, Unversiteitsweg 100, 3584 CG Utrecht, The Netherlands. geert.ramakers@basalmed.uio.no
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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