We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Modification and Inactivation of Human Cu,Zn-Superoxide Dismutase by Methylglyoxal.
- Authors
Jung Hoon Kang
- Abstract
Methylglyoxal (MG) has been identified as an intermediate in non-enzymatic glycation, and increased levels have been reported in patients with diabetes. In this study, the effect of MG on the structure and function of human Cu,Zn-superoxide dismutase (SOD) was investigated. MG modifies Cu,Zn-SOD, as indicated by the formation of fluorescent products. When Cu, Zn-SOD was incubated with MG, covalent crosslinking of the protein increased progressively. MG-mediated modification of Cu,Zn-SOD led to loss of enzymatic activity and release of copper ions from the protein. Radical scavengers inhibited the crosslinking of Cu,Zn-SOD. When Cu,Zn-SOD that had been exposed to MG was analyzed, glycine, histidine, lysine, and valine residues were found to be particularly sensitive. It is suggested that oxidative damage to Cu,Zn-SOD by MG may perturb cellular antioxidant defense systems and damage cells. This effect may account, in part, for organ deterioration in diabetes.
- Subjects
DIABETES; SUPEROXIDE dismutase; CROSSLINKING (Polymerization); COPPER; ZINC
- Publication
Molecules & Cells (Springer Nature), 2003, Vol 15, Issue 2, p194
- ISSN
1016-8478
- Publication type
Article
- DOI
10.1016/s1016-8478(23)13727-7