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PMID: 6732821 Published · ppublish English Journal Article

Calcium regulation of phospholipase A2 is independent of calmodulin.

Biochemical and biophysical research communications ·Vol. 121 ·No. 2 ·1984-06-15 ·Pages 507-13

Withnall MT, Brown TJ, Diocee BK

Abstract

There are conflicting data in the literature as to whether or not the Ca2+ activation of phospholipase A2 is mediated by the calcium binding protein calmodulin. In the present study the membrane-bound phospholipase A2 enzymes in rat and human platelets were shown to be absolutely Ca2+ dependent but were not stimulated by the addition of calmodulin. A partially purified phospholipase A2 from rat platelet membrane, which contained little endogenous calmodulin, also was not stimulated by calmodulin addition. Both isolated and membrane-bound phospholipase A2 were inhibited by the non-specific calmodulin antagonist trifluoperazine but the inhibition was not overcome by adding calmodulin. There was thus no evidence from these studies that phospholipase A2 is calmodulin regulated.

MeSH Terms
Animals Blood Platelets/enzymology Calcium/physiology Calmodulin/physiology Enzyme Activation/drug effects Humans In Vitro Techniques Phospholipases/blood Phospholipases A/antagonists & inhibitors,blood Phospholipases A2 Rats Trifluoperazine/pharmacology
Chemicals
Calmodulin Trifluoperazine Phospholipases Phospholipases A Phospholipases A2 Calcium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Withnall M T
Brown T J
Diocee B K
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1984-06-15
Pages
507-13
Language
English
Region
United States
NLM ID
0372516
Subset
IM
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