Purification and characterization of a 4-hydroxynonenal metabolizing glutathione S-transferase isozyme from bovine pulmonary microvessel endothelial cells

被引:24
|
作者
He, NG
Singhal, SS
Chaubey, M
Awasthi, S
Zimniak, P
Partridge, CA
Awasthi, YC
机构
[1] UNIV TEXAS,MED BRANCH,DEPT HUMAN BIOL CHEM & GENET,GALVESTON,TX 77555
[2] UNIV TEXAS,MED BRANCH,DEPT INTERNAL MED,GALVESTON,TX 77555
[3] UNIV ARKANSAS MED SCI HOSP,DEPT INTERNAL MED & BIOCHEM & MOL BIOL,LITTLE ROCK,AR 72205
[4] JOHN L MCCLELLAN MEM VET ADM MED CTR,LITTLE ROCK,AR 72205
[5] ALBANY MED COLL,DEPT BIOCHEM & MOL BIOL,ALBANY,NY 12208
来源
关键词
glutathione S-transferase; 4-hydroxynonenal; lipid peroxidation; microvessel endothelial cell; (bovine);
D O I
10.1016/S0304-4165(96)00064-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Previous studies have suggested that a group of structurally and immunologically related mammalian glutathione S-transferases (GSTs) which utilize 4-hydroxynonenal (4-HNE) as the preferred substrate and show glutathione peroxidase activity towards phospholipid hydroperoxides may be important for the defense of cells against lipid peroxidation. In present studies we have purified and characterized GST isozymes of bovine pulmonary microvessel endothelial (BPMVE) cells. The results of these studies indicate that BPMVE cells express relatively high amounts of a GST isozyme which utilizes 4-HNE as the preferred substrate. This GST isozyme purified to homogeneity from BPMVE cells showed remarkably high specific activity towards 4-HNE (48.3 units/mg protein) and had similar immunological, kinetic, and structural characteristics as reported for mouse enzyme mGSTA4-4 and other mammalian GSTs of this group. Since the endothelial cells are exposed to constant oxidative stress, we suggest that this GST isozyme may be important for the defense of these cells against lipid peroxidation.
引用
收藏
页码:182 / 188
页数:7
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