Studies on the acyl-chain selectivity of cellular phospholipases A2.
The selective release of arachidonate, as opposed to monoenoic and dienoic fatty acids, after stimulation of cells has suggested the involvement of arachidonate-selective phospholipases A2. Supportive evidence for the existence of such enzymes has also come from in vitro experiments. We have studied the acyl-chain selectivity of phospholipase A2 preparations obtained from human polymorphonuclear leukocytes, human platelets and rat platelets using sn-2-[14C]oleoylphosphatidylcholine and sn-2-[3H]arachidonoylphosphatidylcholine either as single substrates or in doubly labeled mixtures. In either case, no evidence for acyl-chain selectivity was observed for human PMN and rat platelet phospholipase A2. Additional experiments with human PMN homogenates and derived extracts yielded no indication for the selective loss of an arachidonate-selective phospholipase A2. Results with human platelet cytosol were highly suggestive for the presence of an arachidonoyl-selective phospholipase A2 when separate phosphatidylcholine species were assayed. This apparent selectivity was progressively lost when the substrates were mixed or embedded in a membrane of 1-palmitoyl-2-linoleoylphosphatidylcholine. The implications for occurrence of arachidonate-selective phospholipase A2 are discussed.
Schalkwijk
C G
CG
Centre for Biomembranes and Lipid Enzymology, Utrecht, The Netherlands.
Märki
F
F
Van den Bosch
H
H
D000818:Animals; D001665:Binding Sites; D001792:Blood Platelets / Q000201:enzymology*; D006801:Humans; D008051:Lipid Bilayers / Q000378:metabolism; D009504:Neutrophils / Q000201:enzymology*; D010740:Phospholipases / Q000378:metabolism*; D010741:Phospholipases A / Q000378:metabolism*; D054467:Phospholipases A2; D051381:Rats; D013379:Substrate Specificity
D008051:Lipid Bilayers; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2