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Mutual interaction between glycation and oxidation during non-enzymatic protein modification
N Traverso1, S Menini, D Cottalasso
1Institute of General Pathology, Genova, Italy. patgen@unige.it
Biochimica Et Biophysica Acta
|November 21, 1997
Summary
Protein oxidation and glycation, key aging processes, mutually enhance each other. These non-enzymatic modifications, involving oxidative mechanisms, damage proteins through shared pathways.
Area of Science:
- Biochemistry
- Aging Research
- Protein Chemistry
Background:
- Aging involves non-enzymatic protein modifications like oxidation and glycation.
- Interactions between these processes are of significant interest in understanding aging pathogenesis.
Purpose of the Study:
- To investigate the interrelations between protein oxidation and glycation in vitro.
- To explore potential molecular mechanisms underlying their mutual enhancement.
Main Methods:
- Bovine serum albumin (BSA) was subjected to gamma-irradiation for oxidation.
- Oxidized BSA was then exposed to in vitro glycation.
- Fluorescence spectroscopy, free sulfhydryl group assays, and protein carbonyl content measurements were used.
- SDS-PAGE was employed to assess structural damage.
Main Results:
- Both oxidation and glycation induced similar fluorescence modifications, which were additive.
- Both processes led to a loss of free sulfhydryl groups and increased protein carbonyl content.
- Glycation appeared to proceed via oxidative mechanisms, with potential predisposition by irradiation-induced amino group rearrangement.
- Protein peroxides from oxidation may drive further modifications and interact with monosaccharides, promoting glycation.
Conclusions:
- Data support a hypothesis of mutual enhancement between protein oxidation and glycation.
- Glycation can exacerbate oxidation-mediated structural damage.
- Potential molecular mechanisms for the interaction and mutual enhancement of these processes were suggested.