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rdf:type |
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lifeskim:mentions |
umls-concept:C0021547,
umls-concept:C0030685,
umls-concept:C0248868,
umls-concept:C0391871,
umls-concept:C0596235,
umls-concept:C0597694,
umls-concept:C0680255,
umls-concept:C0851285,
umls-concept:C1283071,
umls-concept:C1314939,
umls-concept:C1879547,
umls-concept:C1963578
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pubmed:issue |
1
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pubmed:dateCreated |
1999-6-1
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pubmed:abstractText |
The effect of Ca2+ on inositol (1,4,5)-trisphosphate 3-kinase (3-kinase) activity was measured on Xenopus oocyte cytosolic extracts. The Ca2+-evoked elevation in 3-kinase activity appeared to be mediated by calmodulin (CaM) and the calmodulin-dependent protein kinase II (CaMKII). The results observed in vitro were totally retrieved in intact oocytes and tend to demonstrate the involvement of a CaMKII-mediated phosphorylation in the regulation of 3-kinase activity. Finally, electrophysiological recordings of InsP3-elicited chloride current transients in the presence of CaM/CaMKII inhibitors allowed to postulate an involvement of 3-kinase activity in the regulation of InsP3-mediated Ca2+ release.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
449
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
70-4
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:10225431-Animals,
pubmed-meshheading:10225431-Calcium,
pubmed-meshheading:10225431-Calcium-Calmodulin-Dependent Protein Kinase Type 2,
pubmed-meshheading:10225431-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:10225431-Enzyme Activation,
pubmed-meshheading:10225431-Inositol 1,4,5-Trisphosphate,
pubmed-meshheading:10225431-Oocytes,
pubmed-meshheading:10225431-Phosphotransferases (Alcohol Group Acceptor),
pubmed-meshheading:10225431-Xenopus laevis
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pubmed:year |
1999
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pubmed:articleTitle |
The inositol (1,4,5)-trisphosphate 3-kinase of Xenopus oocyte is activated by CaMKII and involved in the regulation of InsP3-mediated Ca2+ release.
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pubmed:affiliation |
Laboratoire de Neurobiologie Cellulaire, Université de Picardie Jules Verne, Faculté des Sciences, Amiens, France.
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pubmed:publicationType |
Journal Article
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