PROTEIN MODIFICATION BY OXIDANTS AND THE ROLE OF PROTEOLYTIC-ENZYMES
PROTEIN MODIFICATION BY OXIDANTS AND THE ROLE OF PROTEOLYTIC-ENZYMES
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DOI:
10.1042/bst0210346
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发表时间:
1993-05-01
影响因子:
3.9
通讯作者:
DAVIES, KJA
中科院分区:
文献类型:
--
作者:
DAVIES, KJA
J act as water-soluble radical scavengers in the cytoplasm. Finally, various transition metal-chelating proteins (eg transferrin, ferritin, ceruloplasmin) and compounds (eg uric acid) diminish or prevent the involvement of free iron or copper in radical reactions (such as the ferrous iron-catalysed reduction of hydrogen peroxide to form the hydroxyl radical). Although the antioxidant enzymes and compounds comprise an impressive array of defences, it is clear that intracellular, cellular and organismal damage by radicaWoxidants still occurs at a significant rate. In other words, the defenses are not 100% effective. It is also clear, however, that intracellular components, and even long-lived cells, rarely exhibit signs of the overt accumulation of oxidative damage. On the basis of these observations, I proposed originally that cells must also possess enzymes/systems to remove (degrade) and/or repair the products of oxidative damage [2-51. Such ‘Damage RemovaVRepair Systems’ are also depicted in Figure 1. It should be noted that Figure 1 is a natural evolution of previously proposed (and similar) schemes in which antioxidant defences were referred to as ‘Primary Defenses’, and damage removal/repair systems were referred to as ‘Secondary Defences’[2, 31. In Figure 1, I allude to enzymes that can catalyse the removal (degradation) and/or repair of oxidatively damaged proteins, lipids and DNA. These ‘Repair Systems’ form the background for the present communication. This particular paper will focus on the role (s) of proteolytic enzymes in removing oxidatively modified proteins, preventing further protein oxidation or aggregation, and pro-