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PMID: 2121134 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Purification of a high-molecular-mass form of phospholipase A2 from rat kidney activated at physiological calcium concentrations.

The Biochemical journal ·Vol. 271 ·No. 1 ·1990-10-01 ·Pages 37-43

Gronich JH, Bonventre JV, Nemenoff RA

Abstract

Rat kidney contains a soluble phospholipase A2 (PLA2), which is chromatographically identical with a previously identified hormonally regulated form of the enzyme in rat renal mesangial cells. This kidney enzyme has been purified by sequential column fractionation. The purified enzyme is a 110 kDa polypeptide which can hydrolyse arachidonoyl phosphatidylcholine and arachidonoyl phosphatidylethanolamine, but has low activity towards arachidonoyl phosphatidylinositol. The enzyme is considerably larger than most previously isolated forms of secretory or intracellular PLA2, and is stimulated by physiological concentrations of Ca2+, with half-maximal activation occurring at 500 nM-Ca2+. The hormonal regulation and Ca2(+)-dependency of this enzyme strongly suggest that it plays a role in hormonally regulated arachidonic acid release and prostaglandin production in the kidney.

MeSH Terms
Animals Arachidonic Acid Arachidonic Acids/metabolism Calcium/pharmacology Cations, Divalent Chromatography, Gel Chromatography, Ion Exchange Electrophoresis, Polyacrylamide Gel Enzyme Activation/drug effects Kidney/enzymology Male Molecular Weight Phosphatidylcholines/metabolism Phospholipases A/isolation & purification,metabolism Phospholipases A2 Phospholipids/metabolism Rats Rats, Inbred Strains Substrate Specificity
Chemicals
Arachidonic Acids Cations, Divalent Phosphatidylcholines Phospholipids Arachidonic Acid Phospholipases A Phospholipases A2 Calcium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Gronich J H
Medical Services, Massachusetts General Hospital, Boston.
Bonventre J V
Nemenoff R A
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2710037
Published
1990-10-01
Pages
37-43
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1149511
Subset
IM
Grants
NIDDK NIH HHS · DK 38452 · United States
NIDDK NIH HHS · DK 39773 · United States
NIDDK NIH HHS · DK 39902 · United States
External Links
PubMed source DOI: 10.1042/bj2710037 PMC Full Text View journal details
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