Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5824275 | Biochemical Pharmacology | 2007 | 11 Pages |
Phospholipase A2 (PLA2) are esterases that cleave glycerophospholipids to release fatty acids and lysophospholipids. Inhibition of PLA2 alters cancer cell growth and death in vitro and PLA2 expression is increased in breast, lung, and prostate cancers compared to control tissues. Thus, PLA2 may be novel targets for chemotherapeutics. However, PLA2 are a diverse family of enzymes, encompassing 19 members. The selectivity of these individual PLA2 for phospholipids varies, as does their location within the cell, and tissue expression. Thus, their role in cancer may also vary. This review summarizes the expression of individual PLA2 in cancers, focuses on the potential mechanisms by which these esterases mediate carcinogenesis, and suggests that select PLA2 isoforms may be targets for anti-cancer drugs.