Journal
FREE RADICAL BIOLOGY AND MEDICINE
Volume 36, Issue 11, Pages 1355-1365Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.freeradbiomed.2004.02.038
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Funding
- NINDS NIH HHS [NS40494] Funding Source: Medline
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In this review, we describe the free radical mechanism of covalent aggregation of human copper, zinc superoxide dismutase (hSOD1). Bicarbonate anion (HCO3-) enhances the covalent aggregation of hSOD1 mediated by the SOD1 peroxidase-dependent formation of carbonate radical anion (CO3.-), a potent and selective oxidant. This species presumably diffuses out the active site of hSOD1 and reacts with tryptophan residue located on the surface of hSOD1. The oxidative degradation of tryptophan to kynurenine and N-formyl kyrturenine results in the covalent crosslinking and aggregation of hSOD1. Implications of oxidant-mediated aggregation of hSOD1 in the increased cytotoxicity of motor neurons in amyotrophic lateral sclerosis are discussed. (C) 2004 Elsevier Inc. All rights reserved.
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