Daiber Andreas, Münzel Thomas
II. Medizinische Klinik - Labor für Molekulare Kadiologie, Johannes Gutenberg-Universität, Mainz, Germany.
Methods Mol Biol. 2010;594:43-55. doi: 10.1007/978-1-60761-411-1_3.
In 2002, mitochondrial aldehyde dehydrogenase (ALDH-2) was identified as an organic nitrate bioactivating enzyme. This so-called nitrate reductase activity denitrates nitroglycerin (glycerol trinitrate) to its 1,2-glycerol dinitrate metabolite and nitrite. This reaction relies on reduced thiols at the active site of the enzyme and on the presence of reduced dithiols as the electron source. During bioconversion of nitroglycerin, and also in the presence of reactive oxygen and nitrogen species, the active site thiols of ALDH-2 are oxidized and the enzyme looses its activity. We, therefore, speculated that ALDH-2 activity could be a useful marker for cardiovascular oxidative stress. Indeed, this hypothesis was supported by a number of studies, indicating that ALDH-2 activity is impaired in experimental animal models of increased oxidative stress and may be used for detection of an imbalance of mitochondrial and cellular redox state.
2002年，线粒体醛脱氢酶（ALDH-2）被鉴定为一种有机硝酸盐生物活化酶。这种所谓的硝酸还原酶活性将硝酸甘油（三硝酸甘油酯）脱硝为其1,2-二硝酸甘油酯代谢物和亚硝酸盐。该反应依赖于酶活性位点处的还原型硫醇以及作为电子源的还原型二硫醇的存在。在硝酸甘油的生物转化过程中，以及在活性氧和氮物种存在的情况下，ALDH-2的活性位点硫醇会被氧化，酶失去活性。因此，我们推测ALDH-2活性可能是心血管氧化应激的一个有用标志物。事实上，这一假设得到了多项研究的支持，表明在氧化应激增加的实验动物模型中ALDH-2活性受损，并且可用于检测线粒体和细胞氧化还原状态的失衡。
