Linked Life Data

9240967

Source:http://linkedlifedata.com/resource/pubmed/id/9240967

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1997-8-19
pubmed:abstractText
Protein kinase C (PKC) is a phospholipid-dependent serine/threonine kinase family consisting of at least 11 closely related isoenzymes. The different PKC isoenzymes play important roles in signal transduction pathways. The exact significance of each isoenzyme is not known at present; therefore, the elucidation of the roles of the various PKC isoenzymes is important. To explain the function of distinct PKC isoenzymes, the availability of isoenzyme-specific inhibibitors or activators would be an advantage. PKC inhibitors have been known for some time, but these compounds are not isoenzyme-specific and also inhibit other kinases. Recently, an inhibitor selective for PKC alpha and another one selective for PKCbetaI and betaII were described. Both compounds compete with the ATP binding sites that exhibit high homologies among the different PKC isoenzymes. Among others, the phosporyl transfer region, the pseudosubstrate domain, the phorbolester binding sequences, and the phosphorylation sites may also be targets for modulation of isoenzyme-specific PKC activity. The question is whether the differences in these domains and the substrate specificity of the PKC isoenzymes will allow isoenzyme-specific inhibition. In this review the human sequences of these sites, isoenzyme-specific substrates, inhibitory compounds, and inhibitory peptides are summarized.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0892-6638
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
649-69
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
The potential for isoenzyme-selective modulation of protein kinase C.
pubmed:affiliation
Institute of Medical Chemistry and Biochemistry, University of Innsbruck, Austria.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't