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M109678200v1
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Papers In Press, published online ahead of print November 19, 2001
J. Biol. Chem, 10.1074/jbc.M109678200
Submitted on October 5, 2001
Revised on November 14, 2001
Accepted on November 19, 2001

Membrane association of glutathione S-transferase mGSTA4-4, an enzyme that metabolizes lipid peroxidation products

Sharda P. Singh, Andrzej J. Janecki, Sanjay K. Srivastava, Sanjay Awasthi, Yogesh C. Awasthi, Shujuan J. Xia, and Piotr Zimniak

Int. Medicine and Bioch. Mol. Biol., Univ. of Arkansas for Med. Sci. and McClellan VA Med. Ctr., Little Rock, AR 72205

Corresponding Author: zimniakpiotr{at}uams.edu

Lipid peroxidation products have signaling functions and, at higher concentrations, are toxic and may trigger cell death. The compounds are metabolized predominantly by glutathione S-transferases exemplified by mGSTA4-4, an enzyme highly efficient in glutathione conjugation of 4-hydroxyalkenals, and possessing glutathione peroxidase activity toward phospholipid hydroperoxides. mGSTA4-4 belongs to the predominant group of "canonical" glutathione S-transferases which are soluble and generally localized in the cytoplasm. The intracellular localization of mGSTA4-4 was examined in hepatocytes of normal mouse liver and in transfected HepG2 cells by fluorescence microscopy and digital deconvolution. mGSTA4-4 was found to be predominantly localized at or near the plasma membrane in transfected HepG2 cells, as well as in hepatocytes endogenously expressing the protein. In vitro, mGSTA4-4 associated with liposomes, and this interaction was potentiated when the liposomes contained negatively charged phospholipids. Mutating lysine-115 to glutamic acid resulted in a loss of the plasma membrane targeting of mGSTA4-4 as well as in a significant reduction of its binding to liposomes in vitro. These data suggest preferential targeting of mGSTA4-4 to the plasma membrane which may contain the major substrate(s) for this enzyme. Lysine-115 is critically important for the membrane association of mGSTA4-4, most likely by entering into an electrostatic interaction with negatively charged phospholipid headgroups.


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