Characterization of Cytosolic Phospholipase A_2 in Rat Mastocytoma RBL-2H3

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We previously reported that cultured mast cells expressed three discrete phospholipases A_2 (PLA_2s), one of which showed a remarkable preference for phospholipids bearing an arachidonoyl residue at the sn-2 position [M. Murakami, et al., J. Biochem., 111,175 (1992)]. In the present study, we have purified and characterized this enzyme using rat mastocytoma RBL-2H3 as an enzyme source. The elution profiles of the arachidonoyl-preferential PLA_2 activity of rat mastocytoma RBL-2H3 cells on several column chromatographies were indistinguishable from those of 85-kDa cytosolic PLA_2 (cPLA_2) characterized so far. The molecular mass of the partially purified PLA_2 was estimated to be about 90 kDa by gel filtration and it hydrolyzed arachidonate-containing phospholipids preferentially in the presence of submicromolar Ca^<2+> concentrations. Furthermore, it was immunoprecipitated with an anti-rabbit cPLA_2 antibody almost completely. From these observations, we have concluded that the arachidonoyl-preferential PLA_2 in mast cells belongs to the "cPLA_2" family.
社団法人日本薬学会の論文
1994-01-15