| Literature DB >> 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.Entities:
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Year: 1987 PMID: 3426599 DOI: 10.1016/0006-291x(87)90434-7
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575