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Ca 2+ ‐independent cytosolic phospholipase A in HL‐60 cells differentiating to granulocytes
Author(s) -
Hullin-Matsuda Françoise,
Tsujishita Yosuke,
Nishizuka Yasutomi
Publication year - 1997
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/s0014-5793(97)01444-0
Subject(s) - phosphatidylethanolamine , phosphatidic acid , arachidonic acid , phospholipase d , enzyme , biochemistry , phospholipase , cytosol , phosphatidylcholine , phospholipase c , phosphatidylinositol , chemistry , oleic acid , phospholipase a2 , phosphatidylethanol , gtp' , biology , phospholipid , signal transduction , membrane
The release of various fatty acids (FAs) from permeabilized HL‐60 cells, predominantly oleic acid (OA) rather than arachidonic acid, was greatly enhanced by GTP‐γ‐S and vanadate [Tsujishita, Y., Asaoka, Y. and Nishizuka, Y., Proc. Natl. Acad. Sci. USA 91 (1994) 6274–6278]. The present study shows that phospholipase A (A 2 /A 1 ) activity which cleaves the acyl group from both sn ‐2 and sn ‐1 positions of phosphatidylethanolamine (PtdEtn) is increased in HL‐60 cells during differentiation to granulocyte‐like cells. This enzyme does not require Ca 2+ and releases various FAs, preferentially OA from PtdEtn and, to lesser extent, from lysoPtdEtn. Other phospholipids including phosphatidylcholine and phosphatidic acid serve as very poor substrates. Although further studies are necessary to show the direct link of this enzyme activation to receptor stimulation, the results described here imply that this enzyme is responsible for the release of various FAs, particularly OA, from permeabilized HL‐60 cells.