Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-2-23
pubmed:abstractText
With mixtures of phosphatidylethanolamine and phosphatidylserine, the activity of protein kinase C is highly dependent on the fatty acid composition of the phosphatidylethanolamine. This contrasts with phosphatidylcholine/phosphatidylserine mixtures which affect the activity of PKC in a manner independent of the fatty acid composition of the phosphatidylcholine. The results are in accord with those phospholipids having the lowest bilayer-hexagonal phase transition temperature being most effective in augmenting the activity of PKC in the presence of its cofactors. Although the activity of this enzyme is markedly sensitive to the presence of hexagonal phase forming lipids, the activity is insensitive to differences between gel and liquid crystalline state membranes. Membrane defects alone also do not explain the observed effects since vesicles with phase boundary defects do not activate PKC. Increased hexagonal phase propensity of the lipid does not alter the partitioning of PKC between aqueous and membrane phases, which remains calcium dependent. The results demonstrate that simply the formation of defects is not sufficient to promote PKC activity, but that changes in membrane bilayer properties related to hexagonal phase propensity are required.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:volume
300
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
378-83
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Role of membrane defects in the regulation of the activity of protein kinase C.
pubmed:affiliation
Department of Biochemistry, McMaster University, Hamilton, Ontario, Canada.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't