Genetic variations in human glutathione transferase enzymes: significance for pharmacology and toxicology.
Genetic variations in human glutathione transferase enzymes: significance for pharmacology and toxicology.
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DOI：
10.4061/2010/876940
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发表时间：
2010-06-13
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影响因子：
--
通讯作者：
Josephy PD
中科院分区：
文献类型：
--
作者：
Josephy PD
谷胱甘肽转移酶（GST）催化亲电试剂与三肽巯基谷胱甘肽结合的反应。虽然许多GST催化的转化导致异生物质的解毒，但一些底物（如二卤代烷）经历生物活化以形成活性中间体。许多分子流行病学研究已经检测了人类GST基因的多态性（特别是缺失）与疾病易感性或对治疗的反应之间的关联。本文综述了GST的生物化学，GST活性的个体间变异的遗传和环境的来源，以及它们对药理学和毒理学的影响进行了讨论;特别注意的是θ类GST。
Glutathione transferase enzymes (GSTs) catalyze reactions in which electrophiles are conjugated to the tripeptide thiol glutathione. While many GST-catalyzed transformations result in the detoxication of xenobiotics, a few substrates, such as dihaloalkanes, undergo bioactivation to reactive intermediates. Many molecular epidemiological studies have tested associations between polymorphisms (especially, deletions) of human GST genes and disease susceptibility or response to therapy. This review presents a discussion of the biochemistry of GSTs, the sources—both genetic and environmental—of interindividual variation in GST activities, and their implications for pharmaco- and toxicogenetics; particular attention is paid to the Theta class GSTs.