Cinatrins, a novel family of phospholipase A2 inhibitors. II. Biological activities.
Cinatrins A, B and C3 inhibited phospholipase A2 purified from rat platelets in a dose-dependent manner. Cinatrin C3, the most potent component (IC50 70 microM), was noncompetitive with a Ki value of 36 microM. Cinatrins B and C3 also inhibited both porcine pancreas and Naja naja venom phospholipase A2. Inhibition of rat platelet phospholipase A2 by cinatrin C3 was independent of Ca2+ and substrate concentration. Comparison with duramycin, another phospholipase A2 inhibitor, displayed inhibition dependent on substrate concentration when phosphatidylethanolamine was the substrate. These results indicate that the inhibition of phospholipase A2 by cinatrin C3 may result from direct interaction with the enzyme.
Tanaka
K
K
Shionogi Research Laboratory, Shionogi & Co., Ltd., Osaka, Japan.
Itazaki
H
H
Yoshida
T
T
D000818:Animals; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D001430:Bacteriocins; D001792:Blood Platelets / Q000201:enzymology; D004546:Elapid Venoms / Q000737:chemistry; D007783:Lactones / Q000737:chemistry / Q000494:pharmacology*; D015394:Molecular Structure; D010179:Pancreas / Q000201:enzymology; D010455:Peptides / Q000494:pharmacology; D010741:Phospholipases A / Q000037:antagonists & inhibitors*; D054467:Phospholipases A2; D051381:Rats; D012044:Regression Analysis; D013552:Swine
D000900:Anti-Bacterial Agents; D001430:Bacteriocins; D004546:Elapid Venoms; D007783:Lactones; D010455:Peptides; C073567:cinatrin A; C073568:cinatrin B; C073569:cinatrin C1; C073570:cinatrin C2; C073571:cinatrin C3; C040522:duramycin; D010741:Phospholipases A; D054467:Phospholipases A2