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Identification of Glyoxal and Arabinose as Intermediates in the Autoxidative Modification of Proteins by Glucose
Abstract
Glycation and oxidation reactions contribute to protein modification in aging and diabetes. Formation of dicarbonyl sugars during autoxidation of glucose is the hypothetical first step in the autoxidative glycosylation and subsequent browning of proteins by glucose [Wolff, S. P., & Dean, R. T. (1987) Biochem. J. 245, 243-250]. In order to identify the dicarbonyl sugar(s) formed during autoxidation of glucose under physiological conditions, glucose was incubated in phosphate buffer (pH 7.4) at 37 degrees C under air (oxidative conditions) or nitrogen with transition metal chelators (antioxidative conditions). Dicarbonyl compounds were analyzed spectrophotometrically and by HPLC after reaction with Girard-T reagent. Carbohydrates were analyzed by gas chromatography-mass spectrometry. Both dicarbonyl sugar and arabinose concentrations increased with time and glucose concentration in incubations conducted under oxidative conditions; only trace amounts of these products were detected in glucose incubated under antioxidative conditions. HPLC analysis of adducts formed with Girard-T reagent indicated that glyoxal was the only alpha-dicarbonyl sugar formed on autoxidation of glucose. Glyoxal and arabinose accounted for > or = 50% of the glucose lost during a 21 day incubation. Neither glucosone nor its degradation product, ribulose, was detectable. Reaction of glyoxal with RNase yielded the glycoxidation product, N epsilon-(carboxymethyl)lysine, while arabinose is a source of pentosidine. Our results implicate glyoxal and arabinose as intermediates in the browning and crosslinking of proteins by glucose under oxidative conditions. They also provide a mechanism by which antioxidants and dicarbonyl trapping reagents, such as aminoguanidine, limit glycoxidation reactions and support further evaluation of these types of compounds for inhibition of chemical modification and crosslinking of proteins during aging and diabetes.
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Cited by
Biochemistry and molecular cell biology of diabetic complications
Brownlee, M. (2001) · Nature · doi:10.1038/414813a · Cited by 9,107
Incalza, M. A., D'Oria, R., Natalicchio, A., Perrini, S., Laviola, L., & Giorgino, F. (2018) · Vascular Pharmacology · doi:10.1016/j.vph.2017.05.005 · Cited by 1,356
Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose
Thornalley, P. J., LANGBORG, A., & Minhas, H. S. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3440109 · Cited by 1,243
Glucolipotoxicity: fuel excess and β-cell dysfunction
Poitout, V., & Robertson, R. P. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0023 · Cited by 1,092
Advanced Glycation End Products and Oxidative Stress in Type 2 Diabetes Mellitus
Nowotny, K., Jung, T., Höhn, A., Weber, D., & Grune, T. (2015) · Biomolecules · doi:10.3390/biom5010194 · Cited by 1,095
Metadata
- Authors
- Wells-Knecht, K. J., Zyzak, D. V., Litchfield, J. E., Thorpe, S. R., & Baynes, J. W.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1995-03-21
- Volume
- 34
- Issue
- 11
- Pages
- 3702-3709
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W820854987
- Cited by
- 595
- References
- 0
- FWCI
- 14.86
- Type
- journal article
- Language
- en
- Open access
- closed
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- Wells-Knecht, K. J., Zyzak, D. V., Litchfield, J. E., Thorpe, S. R., & Baynes, J. W. (1995). Identification of Glyoxal and Arabinose as Intermediates in the Autoxidative Modification of Proteins by Glucose. Biochemistry. https://doi.org/10.1021/bi00011a027
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