We have cloned human cDNA encoding a novel protein of 782 amino acids that contains the lipase consensus sequence Gly-Xaa-Ser-Xaa-Gly and several stretches surrounding the motif, which are homologous to those of the catalytic domain of cytosolic calcium-independent phospholipase A2 (iPLA2). When expressed in COS-7 cells, the protein predominantly exists in the membrane fraction and exhibits a phospholipase A2 activity in a calcium-independent manner. The transcript of the membrane-bound iPLA2 gene is ubiquitously observed as a single band of approximately 3.3 kb on Northern blot, with the most abundant expression in the skeletal muscle and heart. By a search of the database, we have also identified its putative C. elegans homologue, which shows 47% identity with that of human in the iPLA2 catalytic region. Thus the novel type of iPLA2 is evolutionarily well conserved, suggestive of its biological significance. (C) 2000 Academic Press.
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - Jun 7 2000|
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology