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Annexin II inhibits calcium‐dependent phospholipase A 1 and lysophospholipase but not triacyl glycerol lipase activities of rat liver hepatic lipase
Author(s) -
Bohn Ernst,
Gerke Volker,
Kresse Hans,
Löffler Bernd-Michael,
Kunze Hans
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80294-q
Subject(s) - lysophospholipase , lipase , phospholipase , annexin , phospholipase a2 , enzyme , biochemistry , chemistry , calcium , phospholipase a1 , annexin a1 , endocrinology , biology , in vitro , organic chemistry
A member of the annexin family (the heterotetrameric annexin II 2 pl 1 2 complex purified from porcine intestinal epithelium) was tested for its ability to affect different calcium‐dependent intrinsic lipolytic activities of rat liver hepatic lipase (HL). Whereas annexin II in the presence of calcium failed to interfere with HL triacyl glycerol lipase (EC 3.1.1.3) activity, it inhibited HL phospholipase A 1 (EC 3.1.1.32) and lysophospholipase (EC 3.1.1.5) activities. Inhibition could be overcome by increasing the substrate concentration. Under phospholipase A 1 assay conditions, annexin II did not bind to the purified HL enzyme. These results therefore suggest that only inhibitor/substrate interactions lead to inhibition of HL phospholipase A 1 and lysophospholipase activities, an obviously general mechanism of phospholipase inhibition by annexins. Possible implications of HL inhibition in vivo by annexins are discussed.