Identification of a novel $Ca^{2+}$-independent Phospholipase $A_2$ in Bovine Brain

  • Jeong, Eui-Man (Department of Environmental & Health Chemistry, College of Pharmacy, Chung-Ang University) ;
  • Jun, Hyung-Jin (Department of Environmental & Health Chemistry, College of Pharmacy, Chung-Ang University) ;
  • Kim, Ha-Dong (Department of Environmental & Health Chemistry, College of Pharmacy, Chung-Ang University) ;
  • Lee, Ho-Sup (Department of Environmental & Health Chemistry, College of Pharmacy, Chung-Ang University) ;
  • Min, Pil-Gi (Department of Environmental & Health Chemistry, College of Pharmacy, Chung-Ang University) ;
  • Jo, Dong-Hwan (Department of Environmental & Health Chemistry, College of Pharmacy, Chung-Ang University) ;
  • Jung, Sung-Yun (Department of Environmental & Health Chemistry, College of Pharmacy, Chung-Ang University) ;
  • Kim, Dea-Kyong (Department of Environmental & Health Chemistry, College of Pharmacy, Chung-Ang University)
  • Published : 2003.10.01

Abstract

Phospholipase A$_2$(PLA$_2$) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid(AA), a precursor of eicosanoids including prostaglandins(PGs) and leukotrienes (LTs). The same reaction also produces lyso-phospholipids. So far, at least 19 enzymes that possess PLA2 activity have been identified, consists of low-molecular-weight, Ca$\^$2+/-requiring, secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, host defense, and atherosclerosis. (omitted)

Keywords