Cytosolic Phospholipase A2 (pla2G4A)
The phospholipase A2 was the first of the phopsholipases to be identified when, in 1877, Bokay observed that the lecithin was degraded by a ferment obtained from pancreatic juice. Subsequently, in 1902, this enzyme, known as lecithinase, was detected also in cobra venom where it was observed to induce hemolytic activity through the lysis of erythrocytes membrane. The enzyme was then isolated from human pancreatic tissue by Gronchi and colleagues in 1936 (Glaser and Vadas 1995; Vance and Vance 2002). Since then, an increasing number of PLA2 have now been identified and grouped according to their biochemical features. However, the first evidence that mammalian cells contain a cytosolic calcium-dependent PLA2 able to specifically cleave arachidonic acid was reported only 50 years later by Flesch in 1985 (Flesch et al. 1985 ) and Alonso in 1986 (Alonso et al. 1986). Subsequently, important information regarding the role of...
- Glaser KB, Vadas P. Phospholipase A2 in clinical inflammation. Molecular approaches to pathophysiology. Boca Raton, FL: CRC Press, p. 5; 1995.Google Scholar
- Rydel TJ, Williams JM, Krieger E, Moshiri F, Stallings WC, Brown SM, Pershing JC, Purcell JP, Alibhai MF. The crystal structure, mutagenesis, and activity studies reveal that patatin is a lipid acyl hydrolase with a Ser-Asp catalytic dyad. Biochemistry. 2003;42(22):6696–708.PubMedCrossRefGoogle Scholar
- Vance DE, Vance JF. Biochemistry of lipids, lipoproteins and membranes. 4th ed. Amsterdam: Elsevier Science B.V; 2002.Google Scholar