Linked Life Data

3408497

Source:http://linkedlifedata.com/resource/pubmed/id/3408497

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1988-9-20
pubmed:abstractText
Staurosporine induced the association of purified protein kinase C (PKC) with inside-out vesicles from erythrocyte membranes. This effect was Ca2+ and concentration dependent, and maximum PKC translocation was observed at 50 nM staurosporine and 0.5 microM Ca2+, or higher. A significant effect of staurosporine was already obtained at free Ca2+ concentrations in the range found in resting cells. Under these conditions, the PKC activator 4-phorbol 12,13-dibutyrate was by itself inactive, but enhanced translocation by staurosporine. Protein phosphorylation by staurosporine-translocated PKC was inhibited in the presence or absence of phorbol esters. Translocation and inhibition of PKC occurred in the same staurosporine concentration range.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
154
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1273-9
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
The protein kinase inhibitor staurosporine, like phorbol esters, induces the association of protein kinase C with membranes.
pubmed:affiliation
Theodor-Kocher-Institut, University of Bern, Switzerland.
pubmed:publicationType
Journal Article