Physiological aspects of a high affinity binding site for pancreatic-type phospholipase A2.
We characterized a specific binding site for pancreatic-type phospholipase A2 (PLA2-I) in several tissues and cells. The PLA2-I binding protein was purified from bovine corpus luteum membranes, which had a mass of 190 kDa. The purified protein, which possessed a binding capacity with high affinity and specificity for a mammalian mature type of PLA2-I, was a glycoprotein having a core protein of approx. 150 kDa and its carbohydrate moieties might be required for ligand recognition. PLA2-I elicited several biological responses in tissues and cells; i.e., cell proliferation and eicosanoid production, possibly through its specific binding site.
Arita
H
H
Shionogi Research Laboratories, Shionogi and Co., Ltd., Osaka, Japan.
Hanasaki
K
K
D000818:Animals; D001665:Binding Sites; D002352:Carrier Proteins / Q000378:metabolism; D002417:Cattle; D003338:Corpus Luteum / Q000201:enzymology; D005260:Female; D006023:Glycoproteins / Q000378:metabolism; D051379:Mice; D008954:Models, Biological; D010179:Pancreas / Q000201:enzymology*; D010741:Phospholipases A / Q000302:isolation & purification / Q000378:metabolism*; D054467:Phospholipases A2; D051381:Rats; D011956:Receptors, Cell Surface; D054507:Receptors, Phospholipase A2; D014018:Tissue Distribution
D002352:Carrier Proteins; D006023:Glycoproteins; C516357:Pla2r1 protein, mouse; D011956:Receptors, Cell Surface; D054507:Receptors, Phospholipase A2; D010741:Phospholipases A; D054467:Phospholipases A2