2-acyl-sn-glycero-3-phosphoethanolamine lysophospholipase A2 activity in guinea-pig heart microsomes.
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Key Findings
Abstract
We have recently described a lysophospholipase A2 activity in guinea-pig heart microsomes that hydrolyses 2-acyl-sn-glycero-3-phosphocholine (2-acyl-GPC). The presence of a similar activity that hydrolyses 2-acyl-sn-glycero-3-phosphoethanolamine (2-acyl-GPE) was not known. In this study, a lysophospholipase A2 activity in guinea-pig heart microsomes that hydrolyses 2-acyl-GPE has been characterized. The enzyme did not require Ca2+ for activity and exhibited a high specificity for 2-arachidonoyl-GPE and 2-linoleoyl-GPE over 2-oleoyl-GPE and 2-palmitoyl-GPE. The specificity for these unsaturated substrates was observed in the presence and absence of detergents. Selective hydrolysis of 2-arachidonoyl-GPE over 2-palmitoyl-GPE was observed when equimolar quantities of the two substrates were incubated with the enzyme. There was no preferential hydrolysis of either 2-linoleoyl- or 2-arachidonoyl-GPE when presented individually or as a mixture. Significant differences in the characteristics of 2-acyl-GPE-hydrolysing and 2-acyl-GPC-hydrolysing activities included differences in their optimum pH, the effect of Ca2+ and their acyl specificities. Taken together, these results suggest that the two activities are catalysed by different enzymes. 2-Acyl-GPE lysophospholipase activity with a preference for 2-arachidonoyl-GPE over 2-oleoyl-GPE was observed in guinea-pig brain, liver, kidney and lung microsomes. Lysophospholipase A1 activity that catalyses the hydrolysis of 1-acyl-GPE was also present in guinea-pig heart microsomes and had different characteristics from the 2-acyl-GPE-hydrolysing activity, including a preference for saturated over unsaturated substrates. The 2-acyl-GPE lysophospholipase A2 activity appeared to be distinct from Ca(2+)-independent phospholipase A2. The characteristics of the 2-acyl-GPE lysophospholipase A2 suggest it could play a role in the selective release of arachidonic and linoleic acids for further metabolism in cells.
Affiliation
Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of Manitoba, Winnipeg, Canada.
External References
- PubMed ID:
- 2025224
- DOI:
- 10.1042/bj2750393
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