Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1990-12-4
pubmed:abstractText
Phospholipase A2 (PLA2) is an important enzyme in the regulation of cell behavior. The hydrolysis of phosphatidylcholine in vitro catalyzed by porcine pancreatic PLA2 was inhibited by heparin. Other glycosaminoglycans inhibited PLA2 activity to a significantly lesser extent, with a pattern of inhibition: heparin much greater than chondroitin sulfate (CS)-C greater than CS-A greater than CS-B greater than keratan sulfate. Hyaluronic acid and heparan sulfate caused no inhibition. Heparin's ability to inhibit PLA2 activity did not depend on substrate concentration, but did depend on ionic strength, with inhibition decreasing with increasing ionic strength. Heparin inhibition also varied with pH, being more effective at pH 5-8 than at pH 10. As a consequence, heparin induced a shift of the pH optimum of PLA2 from 7 to 8. Histone IIA and protamine sulfate, heparin-binding proteins, reversed heparin-induced PLA2 inhibition. The concentration of heparin which inhibited PLA2 activity by 50% increased with increasing enzyme concentration. Furthermore, PLA2 bound to heparin-Affigel. The data indicate that the catalytic potential of PLA2 can be regulated by heparin or heparin-like molecules and that inhibition is contingent on the formation of a heparin-PLA2 complex.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
1046
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
242-8
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Inhibition of phospholipase A2 by heparin.
pubmed:affiliation
Department of Pharmacology and Cell Biophysics, University of Cincinnati, College of Medicine, OH 45267-0575.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.