title: Selective inhibition of phospholipase A2 by different lipocortins.
abstract: Different lipocortins, purified from pig lung and from cultured bone marrow-derived macrophages showed a high degree of specificity for distinct phospholipids, when assayed for anti-phospholipase A2 activity. The 34-kDa fraction from lung inhibited pancreas phospholipase A2 only if phosphatidylethanolamine was used as substrate, whereas the 68-kDa lung fraction was inhibitory only when phosphatidylcholine was the substrate. A comparison of phospholipases A2 from different sources (pancreas and macrophages) revealed different inhibitory properties of lipocortins when assayed with the same substrate. Using phosphatidylcholine as substrate, the 68-kDa lung fraction only inhibited the pancreas enzyme. On the other hand with phosphatidylethanolamine as substrate, the 34-kDa macrophage lipocortin exerted inhibition on phospholipase A2, purified from macrophages, but did not affect the pancreas enzyme. These data suggest a complex interaction consisting of specific binding of individual lipocortins to distinct phospholipids but also suggest that lipocortins interact with the enzyme as well.
authors: Max-Planck-Institut für Immunobiologie, Freiburg.
authors: G
authors: G
authors: Weber
authors: E
authors: E
authors: Ferber
mesh_terms: D000818:Animals; D017302:Annexins; D002135:Calcium-Binding Proteins / Q000302:isolation & purification / Q000494:pharmacology*; D008168:Lung / Q000737:chemistry; D008264:Macrophages / Q000737:chemistry / Q000201:enzymology; D051379:Mice; D010179:Pancreas / Q000201:enzymology; D010713:Phosphatidylcholines / Q000378:metabolism; D010714:Phosphatidylethanolamines / Q000378:metabolism; D010741:Phospholipases A / Q000037:antagonists & inhibitors*; D054467:Phospholipases A2; D013552:Swine
chemical_list: D017302:Annexins; D002135:Calcium-Binding Proteins; D010713:Phosphatidylcholines; D010714:Phosphatidylethanolamines; D010741:Phospholipases A; D054467:Phospholipases A2