A novel intracellular membrane-bound calcium-independent phospholipase A2

Haruki Tanaka, Ryu Takeya, Hideki Sumimoto

Research output: Contribution to journalArticlepeer-review

81 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)320-326
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - Jun 7 2000

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'A novel intracellular membrane-bound calcium-independent phospholipase A2'. Together they form a unique fingerprint.

Cite this