Two distinct 4-hydroxynonenal metabolizing glutathione S-transferase isozymes are differentially expressed in human tissues

被引:51
作者
Cheng, JZ
Yang, YS
Singh, SP
Singhal, SS
Awasthi, S
Pan, SS
Singh, SV
Zimniak, P
Awasthi, YC
机构
[1] Univ Texas, Med Branch, Dept Human Biol Chem & Genet, Galveston, TX 77555 USA
[2] Univ Arkansas Med Sci, Dept Internal Med, Little Rock, AR 72205 USA
[3] Univ Arkansas Med Sci, Dept Biochem & Mol Biol, Little Rock, AR 72205 USA
[4] Cent Arkansas Vet Healthcare Syst, Little Rock, AR USA
[5] Univ Texas, Dept Chem & Biochem, Arlington, TX 76019 USA
[6] Univ Pittsburgh, Sch Med, Pittsburgh Canc Inst, Pittsburgh, PA 15261 USA
关键词
glutathione; human glutathione S-transferase; 4-hydroxynonenal;
D O I
10.1006/bbrc.2001.4707
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
The two previously reported human glutathione S-transferase isszymes, hGST5.8 and hGSTA4-4, hare been suggested to be similar because of their comparable activities toward 4-hydroxynonenal-GSH conjugation, Here, we demonstrate that hGST5.8 and hGSTA4-4 are distinct, Antibodies raised against hGSTA4-4 did not recognize hGST5.8, and antibodies raised against mouse GSTA4-4 that cross-react with hGST5.8 did not recognize hGSTA4-4 The pi value of hGSTA4-4 was found to be 8.4, as opposed to the pi value of 5.8 for hGST5.6. The two isozymes are differentially expressed in human tissues and there are significant differences in their kinetic properties, While both isozymes showed a strong expression in liver and testis, hGSTA4-4 was not detected in brain where EGST5.8 was present. In the pancreas, a strong expression of hGST5.8 was observed while hGSTA4-4 was barely detectable in this tissue, (C) 2001 Academir Press.
引用
收藏
页码:1268 / 1274
页数:7
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