The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
N ε-(Carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins
Open accessAbstract
Advanced glycation end-products and glycoxidation products, such as Nϵ-(carboxymethyl)lysine (CML) and pentosidine, accumulate in long-lived tissue proteins with age and are implicated in the aging of tissue proteins and in the development of pathology in diabetes, atherosclerosis and other diseases. In this paper we describe a new advanced glycation end-product, Nϵ-(carboxyethyl)lysine (CEL), which is formed during the reaction of methylglyoxal with lysine residues in model compounds and in the proteins RNase and collagen. CEL was also detected in human lens proteins at a concentration similar to that of CML, and increased with age in parallel with the concentration of CML. Although CEL was formed in highest yields during the reaction of methylglyoxal and triose phosphates with lysine and protein, it was also formed in reactions of pentoses, ascorbate and other sugars with lysine and RNase. We propose that levels of CML and CEL and their ratio to one another in tissue proteins and in urine will provide an index of glyoxal and methylglyoxal concentrations in tissues, alterations in glutathione homoeostasis and dicarbonyl metabolism in disease, and sources of advanced glycation end-products in tissue proteins in aging and disease.
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Cites
Glomb, M. A., & Monnier, V. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.17.10017 · Cited by 576
Cited by
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
Effect of Collagen Turnover on the Accumulation of Advanced Glycation End Products
Verzijl, N., DeGroot, J., Thorpe, S. R., Bank, R. A., Shaw, J. N., Lyons, T. J., Bijlsma, J. W. J., Lafeber, F. P. J. G., Baynes, J. W., & TeKoppele, J. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006700200 · Cited by 963
Self-citationRadicals and oxidative stress in diabetes
West, I. C. (2000) · Diabetic Medicine · doi:10.1046/j.1464-5491.2000.00259.x · Cited by 913
Ramasamy, R., Vannucci, S. J., Yan, S. S. D., Herold, K., Yan, S. F., & Schmidt, A. M. (2005) · Glycobiology · doi:10.1093/glycob/cwi053 · Cited by 834
Vistoli, G., De Maddis, D., Cipak, A., Zarkovic, N., Carini, M., & Aldini, G. (2013) · Free Radical Research · doi:10.3109/10715762.2013.815348 · Cited by 823
Metadata
- Authors
- AHMED, M. U., FRYE, E. B., DEGENHARDT, T. P., THORPE, S. R., & BAYNES, J. W.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1997-06-01
- Volume
- 324
- Issue
- 2
- Pages
- 565-570
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1896619220
- Cited by
- 604
- References
- 1
- FWCI
- 13.39
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: N ε-(Carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins. https://app.cochat.ai/papers/10.1042/bj3240565
- The paper
- AHMED, M. U., FRYE, E. B., DEGENHARDT, T. P., THORPE, S. R., & BAYNES, J. W. (1997). N ε-(Carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins. Biochemical Journal. https://doi.org/10.1042/bj3240565
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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