Linked Life Data

2211681

Source:http://linkedlifedata.com/resource/pubmed/id/2211681

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
1990-11-15
pubmed:abstractText
Hormonal activation of the phosphatidylinositol (PI) signaling system initiates a biochemical pathway that bifurcates to increase cellular levels of diacylglycerol and of inositol trisphosphate/Ca2+. Both Diacylglycerol and Ca2+ are known to activate protein kinase C, a primary mediator of the PI signaling system. We now find that the two limbs of the PI pathway utilize distinct multifunctional protein kinases to mediate their cellular effects. An important consequence of Ca2+ elevated by the PI signaling system, when PC12 cells are treated with bradykinin, is the activation of multifunctional Ca2+/calmodulin-dependent protein kinase. This activation stimulates autophosphorylation of CaM kinase at its regulatory domain and converts it to an active, Ca2(+)-independent species that may be a basis for potentiation of Ca2+ transients.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18055-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Ca2+/calmodulin kinase is activated by the phosphatidylinositol signaling pathway and becomes Ca2(+)-independent in PC12 cells.
pubmed:affiliation
Department of Pharmacology, Stanford University School of Medicine, California 94305-5332.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.