Translocation of phospholipase A2 from cytosol to membranes induced by 1-oleoyl-2-acetyl-glycerol in serum-free cultured macrophages.
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.
Schonhardt
T
T
Max-Planck-Institut für Immunbiologie, Freiburg, FRG.
Ferber
E
E
D000818:Animals; D002118:Calcium / Q000032:analysis; D002462:Cell Membrane / Q000201:enzymology; D002478:Cells, Cultured; D003600:Cytosol / Q000201:enzymology; D004075:Diglycerides / Q000494:pharmacology*; D004305:Dose-Response Relationship, Drug; D005989:Glycerides / Q000494:pharmacology*; D008264:Macrophages / Q000201:enzymology*; D051379:Mice; D008810:Mice, Inbred C57BL; D010740:Phospholipases / Q000378:metabolism*; D010741:Phospholipases A / Q000378:metabolism*; D054467:Phospholipases A2; D011493:Protein Kinase C / Q000378:metabolism; D013997:Time Factors
D004075:Diglycerides; D005989:Glycerides; C038237:1-oleoyl-2-acetylglycerol; D011493:Protein Kinase C; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2; D002118:Calcium