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Translocation of phospholipase A2 from cytosol to membranes induced by 1-oleoyl-2-acetyl-glycerol in serum-free cultured macrophages.

作者信息

Schonhardt T, Ferber E

机构信息

Max-Planck-Institut für Immunbiologie, Freiburg, FRG.

出版信息

Biochem Biophys Res Commun. 1987 Dec 16;149(2):769-75. doi: 10.1016/0006-291x(87)90434-7.

DOI:10.1016/0006-291x(87)90434-7
PMID:3426599
Abstract

Macrophages exhibit high activities of a phospholipase A2 which preferentially cleaves arachidonic acid (I. Flesch, B. Schmidt, and E. Ferber, Z. Naturforsch. 40c, 356-363, 1985). In unstimulated cells more than 90% of the total activity of this enzyme is localized in the cytosol. Treatment of these cells with 100 microM 1-oleoyl-2-acetyl-glycerol (OAG) for 30 min induced a translocation of phospholipase A2 to cellular membranes. The amount of translocated phospholipase A2 was about 30% of the total activity and correlated with a similar translocation of protein kinase C to membranes. These data suggest that the translocation of phospholipase A2 to membranes is related to the activation process of this enzyme.

摘要

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