Linked Life Data

2629774

Source:http://linkedlifedata.com/resource/pubmed/id/2629774

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1990-5-10
pubmed:abstractText
Protein kinase C, which plays a significant role in the polyphosphoinositide pathway of transmembrane signaling, is activated by a large class of extracellular ligands including neurotransmitters, hormones and growth factors. Diacylglycerols are the intracellular mediators of protein kinase C activation. Tumor promoting phorbol esters mimic the diacylglycerol action in binding to the same site. Active diacylglycerols have the 1.2 sn configuration and saturated short chain or unsaturated long chain fatty acids. Alkyl analogs of diacylglycerols were devoid of activity when an ether bond was present in position 1, whereas activity of the alkyl analog in position 2 was retained. Protein kinase C activation and 3H-TPA binding to the enzyme occurred in the presence of 0.5 mM EGTA. Moreover it has been shown in vivo that full activation of the enzyme was obtained in the intact platelets loaded with an excess of Quin 2, prior to stimulation by phorbol esters. A peptide (residues 499-513) was synthesized which enhanced the affinity of protein kinase C for histone. It is suggested that it may be the receptor site for another peptide of the enzyme (residues 19 to 36) which behaves as a pseudosubstrate.
pubmed:language
fre
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0926-5287
pubmed:author
pubmed:issnType
Print
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
669-75
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
[The role of calcium, diglyceride ester bindings and a synthetic polypeptide in protein kinase C activation].
pubmed:affiliation
Groupe de laboratoires de l'IRSC, Villejuif, France.
pubmed:publicationType
Journal Article, English Abstract