Expression and mechanistic study on a novel group V phospholipase A2

Yijun Chen

Appointment Period: 1997-1998 / Grant Year: [13]

Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 fatty acyl bond of phospholipids to liberate free fatty acids and lysophospholipids. A novel human secreted calcium dependent form of PLA2 was recently discovered at the genomic level and is referred to as the Group V PLA2 (GV-PLA2). Group V PLA2 has been shown to be involved in signal transduction and inflammatory processes in cellular studies, but the physical and biochemical properties of this important enzyme have not been clear. To understand the biochemical characteristics, the structure-function relationships and the ultimate design of specific inhibitors, the expression of this human enzyme to obtain a substantial amount of the active enzyme is necessary. Further kinetic characterization of the GV-PLA2 and studies with macrophage cells to investigate its roles in cellular function are underway.

PUBLICATIONS (resulting from this training)

Chen Y, Dennis EA. (1998) Expression and characterization of human group V phospholipase A2. Biochim Biophys Acta. 1394:57-64.

Yang HC, Mosior M, Johnson CA, Chen Y, Dennis EA. (1999) Group-specific assays that distinguish between the four major types of mammalian phospholipase A2. Anal Biochem. 269:278-88.