Trafficking of platelet-activating factor acetylhydrolase type II in response to oxidative stress.

ABSTRACT: Platelet-activating factor acetylhydrolase type II (PAFAH-II) is an intracellular phospholipase A(2) enzyme that hydrolyzes platelet-activating factor and oxidatively fragmented phospholipids. This N-terminally myristoylated protein becomes associated with cytoplasm-facing cell membranes under oxidative stress. The structural requirements for binding of PAFAH-II to membranes in response to oxidative stress are unknown. To begin elucidating the mechanism of trafficking and stress response, we constructed a homology model of PAFAH-II. From the predicted membrane orientation of PAFAH-II, the N-terminal myristoyl group and a hydrophobic patch are hypothesized to be involved in membrane binding. Localization studies of human PAFAH-II in HEK293 cells indicated that an unmyristoylated mutant rema

SUBMITTER: Thevenin AF 

PROVIDER: S-EPMC3183284 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature