Molecular characterization of cytosolic phospholipase A2-beta

  • J Biol Chem. 1999 Jun 11;274(24):17063-7. doi: 10.1074/jbc.274.24.17063.
C Song  1 ,  X J Chang ,  K M Bean ,  M S Proia ,  J L Knopf ,  R W Kriz
Affiliations
  • 1. Small Molecule Drug Discovery Group, Genetics Institute, Cambridge, Massachusetts 02140, USA.
PMID: 10358058 DOI: 10.1074/jbc.274.24.17063
Abstract

We have isolated a cDNA encoding a 1012-amino acid polypeptide cPLA2-beta, that has significant homology with cPLA2-alpha in both the calcium-dependent lipid binding domain as well as in the catalytic domain. Transient expression of cPLA2-beta cDNA in COS cells results in an increase in calcium-dependent Phospholipase A1 (PLA1) and PLA2 activities compared with vector-transfected cells. cPLA2-beta is markedly less selective for cleavage at sn-2 as compared with cPLA2-alpha and cPLA2-gamma. Northern analysis reveals a cPLA2-beta transcript of 8 kilobase pairs that is expressed in all the human tissues examined. With the identification of cPLA2-beta, the newly defined cPLA2 family now comprises three members that may have dramatically different mechanisms for regulation of expression and enzymatic activation.