| pubmed-article:10844014 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10844014 | lifeskim:mentions | umls-concept:C0027882 | lld:lifeskim |
| pubmed-article:10844014 | lifeskim:mentions | umls-concept:C0019564 | lld:lifeskim |
| pubmed-article:10844014 | lifeskim:mentions | umls-concept:C0033634 | lld:lifeskim |
| pubmed-article:10844014 | lifeskim:mentions | umls-concept:C0080093 | lld:lifeskim |
| pubmed-article:10844014 | lifeskim:mentions | umls-concept:C1413038 | lld:lifeskim |
| pubmed-article:10844014 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:10844014 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:10844014 | pubmed:dateCreated | 2000-6-30 | lld:pubmed |
| pubmed-article:10844014 | pubmed:abstractText | The NMDA subtype of the glutamate-gated channel exhibits a high permeability to Ca(2+). The influx of Ca(2+) through NMDA channels is limited by a rapid and Ca(2+)/calmodulin (CaM)-dependent inactivation that results from a competitive displacement of cytoskeleton-binding proteins from the NR1 subunit of the receptor by Ca(2+)/CaM (Zhang et al., 1998; Krupp et al., 1999). The C terminal of this subunit can be phosphorylated by protein kinase C (PKC) (Tingley et al., 1993). The present study sought to investigate whether PKC regulates Ca(2+)-dependent inactivation of the NMDA channel in hippocampal neurons. Activation of endogenous PKC by 4beta-phorbol 12-myristate 13-acetate enhanced peak (I(p)) and depressed steady-state (I(ss)) NMDA-evoked currents, resulting in a reduction in the ratio of these currents (I(ss)/I(p)). We demonstrated previously that PKC activity enhances I(P) via a sequential activation of the focal adhesion kinase cell adhesion kinase beta/proline-rich tyrosine kinase 2 (CAKbeta/Pyk2) and the nonreceptor tyrosine kinase Src (Huang et al., 1999; Lu et al., 1999). Here, we report that the PKC-induced depression of I(ss) is unrelated to the PKC/CAKbeta/Src-signaling pathway but depends on the concentration of extracellular Ca(2+). Intracellular applications of CaM reduced I(ss)/I(p) and occluded the Ca(2+)-dependent effect of phorbol esters on I(ss.) Moreover, increasing the concentration of intracellular Ca(2+) buffer or intracellular application of the inhibitory CaM-binding peptide (KY9) greatly reduced the phorbol ester-induced depression of I(ss). Taken together, these results suggest that PKC enhances Ca(2+)/CaM-dependent inactivation of the NMDA channel, most likely because of a phosphorylation-dependent regulation of interactions between receptor subunits, CaM, and other postsynaptic density proteins. | lld:pubmed |
| pubmed-article:10844014 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10844014 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10844014 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10844014 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10844014 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10844014 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10844014 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:10844014 | pubmed:issn | 0270-6474 | lld:pubmed |
| pubmed-article:10844014 | pubmed:author | pubmed-author:MacDonaldJ... | lld:pubmed |
| pubmed-article:10844014 | pubmed:author | pubmed-author:BanAA | lld:pubmed |
| pubmed-article:10844014 | pubmed:author | pubmed-author:OrserB ABA | lld:pubmed |
| pubmed-article:10844014 | pubmed:author | pubmed-author:JacksonM FMF | lld:pubmed |
| pubmed-article:10844014 | pubmed:author | pubmed-author:LuW YWY | lld:pubmed |
| pubmed-article:10844014 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10844014 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:10844014 | pubmed:volume | 20 | lld:pubmed |
| pubmed-article:10844014 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10844014 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10844014 | pubmed:pagination | 4452-61 | lld:pubmed |
| pubmed-article:10844014 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:10844014 | pubmed:meshHeading | pubmed-meshheading:10844014... | lld:pubmed |
| pubmed-article:10844014 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10844014 | pubmed:articleTitle | In CA1 pyramidal neurons of the hippocampus protein kinase C regulates calcium-dependent inactivation of NMDA receptors. | lld:pubmed |
| pubmed-article:10844014 | pubmed:affiliation | Department of Physiology, University of Toronto, Toronto, Ontario M5S 1A8 Canada. w.lu@utoronto.ca | lld:pubmed |
| pubmed-article:10844014 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10844014 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:10844014 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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