Johnson Felicity, Giulivi Cecilia
Department of Molecular Biosciences, University of California, 1311 Haring Hall, One Shields Ave, Davis, CA 95616, USA.
Mol Aspects Med. 2005 Aug-Oct;26(4-5):340-52. doi: 10.1016/j.mam.2005.07.006.
Superoxide dismutases (SOD), a group of metal-containing enzymes, have a vital anti-oxidant role in human health, conferred by their scavenging of one of the reactive oxygen species, superoxide anion. Three types of SODs are known in humans, with the most abundant being cytosolic SOD1, identified by its Cu, Zn-containing prosthetic group. The presence of these metals and the coordination to certain amino acids are essential for function. SODs are among the first line of defense in the detoxification of products resulting from oxidative stress. Here, we describe the importance of SOD function, and the need for coordination with other ROS-scavenging enzymes in this pathway of detoxification. The impact of metal-deficient diets (copper or zinc) or incorrect metal ion incorporation (copper chaperone for SOD) onto nascent SOD, are also examined. Finally, human pathologies associated with either SOD dysfunction or decreased activity are discussed with current progress on the development of novel therapies.
超氧化物歧化酶(SOD)是一类含金属的酶,通过清除活性氧之一超氧阴离子,在人类健康中发挥着至关重要的抗氧化作用。人类已知有三种类型的SOD,其中最丰富的是胞质SOD1,通过其含铜、锌的辅基得以鉴定。这些金属的存在以及与某些氨基酸的配位对其功能至关重要。SOD是氧化应激产生的产物解毒过程中的第一道防线之一。在此,我们描述了SOD功能的重要性,以及在该解毒途径中与其他活性氧清除酶协同作用的必要性。还研究了缺乏金属的饮食(铜或锌)或不正确的金属离子掺入(SOD的铜伴侣)对新生SOD的影响。最后,讨论了与SOD功能障碍或活性降低相关的人类病理学以及新型疗法开发的当前进展。