Lipocortin-like anti-phospholipase A2 activity of endonexin.
Endonexin (protein II, 32.5 kDa) has been purified to homogeneity from bovine liver in the following steps: selective extraction by EGTA from membranes precipitated with Triton X-100/calcium; chromatography on DEAF-TSK 545 at pH 7.0, endonexin being eluted at 0.1 M NaCl; affinity chromatography on polyacrylamide-immobilized phosphatidylserine; gel filtration on TSK 3000. The amino acid composition was essentially similar to that previously reported. Using [3H]oleic acid-labelled Escherichia coli membranes as substrate, endonexin inhibited phospholipase A2 from pig pancreas. Maximal inhibition was 55 and 70%, whereas 50% inhibition occurred at 480 and 120 nM endonexin and lipocortin II, respectively. These data could be related to common features shared by both lipocortins/calpactins and endonexin, i.e. the presence of a consensus sequence and the ability to bind to anionic phospholipids in a calcium-dependent manner.
D000595:Amino Acid Sequence; D000818:Animals; D017304:Annexin A5; D017302:Annexins; D002135:Calcium-Binding Proteins / Q000302:isolation & purification / Q000494:pharmacology*; D002417:Cattle; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D006023:Glycoproteins / Q000494:pharmacology; D008099:Liver / Q000032:analysis; D010740:Phospholipases / Q000037:antagonists & inhibitors*; D010741:Phospholipases A / Q000037:antagonists & inhibitors*; D054467:Phospholipases A2
D017304:Annexin A5; D017302:Annexins; D002135:Calcium-Binding Proteins; D006023:Glycoproteins; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2