Linked Life Data

2226814

Source:http://linkedlifedata.com/resource/pubmed/id/2226814

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1990-12-4
pubmed:abstractText
The activation of type I (gamma), II (beta) and III (alpha) protein kinase C (PKC) subspecies by phosphatidylserine (PS) and diacylglycerol (DAG) is inhibited by micromolar concentrations of triphenylacrylonitrile (TPE) antiestrogens. TPE A (with p-hydroxy and p-diethylaminoethoxy groups on the 3- and 3'-phenyl rings, respectively) interacts with PS-vesicles as well as with the regulatory domain of PKC, probably at a site different from the Ca2+ and DAG binding sites. The interaction of TPE A with the regulatory domain of enzyme is very slow. Apparently, TPE A does not interact with the catalytic domain of PKC. In contrast, another TPE derivative, TPE B (with a p-hydroxy group on each of the three phenyl rings) inhibits the enzyme activity in a competitive manner with respect to ATP, suggesting that this TPE interacts with the catalytically active site of the enzyme. It seems likely that various TPE antiestrogen derivatives may exert their inhibitory action on PKC by multiple different mechanisms.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
54-8
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Multiple mechanisms of protein kinase C inhibition by triphenylacrylonitrile antiestrogens.
pubmed:affiliation
Department of Biochemistry, Kobe University School of Medicine, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't