Linked Life Data

3004131

Source:http://linkedlifedata.com/resource/pubmed/id/3004131

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1986-2-28
pubmed:abstractText
The activity of partially purified phospholipase C from human platelets was totally dependent on Ca2+, and approximately 800 microM Ca2+ was required for half-maximal activity. The enzyme hydrolyzed endogenous substrates in the order DPI greater than TPI greater than PI in a Ca2+-dependent manner. Hydrolysis of TPI in thrombin-stimulated platelets was dependent on the amount of the agonist, and it was not affected by the presence or absence of extracellular Ca2+. Hydrolysis was inhibited by preincubation with Quin-2AM in the absence of extracellular Ca2+. The intracellular Ca2+ concentration was significantly lowered below the basal level by such treatment. These observations suggested that TPI breakdown in thrombin-stimulated platelets is mediated by agonist-receptor coupling and requires at least the basal level of intracellular Ca2+.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0732-8141
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
131-4
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Ca2+ requirement in hydrolysis of phosphatidylinositol-4,5-bisphosphate in human platelets.
pubmed:publicationType
Journal Article