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Cited by 434

The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.

Nε-(Carboxymethyl)lysine Protein Adduct Is a Major Immunological Epitope in Proteins Modified with Advanced Glycation End Products of the Maillard Reaction

Ikeda, Kazuyoshi, Higashi, Takayuki, Sano, Hiroyuki, Jinnouchi, Yoshiteru, Yoshida, Masaki, Araki, Tomohiro, Ueda, Shoichi, Horiuchi, Seikoh·1996·Biochemistry
DOI 10.1021/bi9530550
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Abstract

Long-term incubation of proteins with glucose leads to the formation of advanced glycation end products (AGE). Recent immunological studies have suggested the potential role of AGE in atherosclerosis, aging, and diabetic complications. We previously prepared a monoclonal (6D12) as well as a polyclonal anti-AGE antibody and proposed the presence of a common AGE structure(s) that may act as a major immunochemical epitope [Horiuchi, S., Araki, N., & Morino, Y. (1991) J. Biol. Chem. 266, 7329-7332]. The purpose of the present study was to determine the major epitope. Amino acid analysis of AGE-proteins indicated that N(epsilon)-(carboxymethyl)lysine (CML) was a major modified lysine residue. Immunologic studies demonstrated the positive reaction of 6D12 not only to all CML-modified proteins tested, but also to BSA modified with several aldehydes known to generate a CML-protein adduct, and a linear correlation between the CML contents of CML-BSA and their immunoreactivity to 6D12 up to approximately 8 mol/mol of protein. Further experiments with CML analogs revealed that the epitope of 6D12 is a CML-protein adduct with an important carbonyl group. In contrast to 6D12, our polyclonal anti-AGE antibody showed a significant but much weaker immunoreactivity to CML-BSA, suggesting that the polyclonal antibody contains two populations, one reactive to CML (CML-PA) and the other unreactive to CML (Non-CML-PA). Non-CML-PA separated from CML-PA by CML-BSA affinity chromatography did not react with all CML-modified preparations, but retained its property to react commonly with AGE preparations obtained from proteins, lysine derivatives, and monoaminocarboxylic acids. Therefore, it is clear that a CML-protein adduct is a major immunological epitope in AGE structures, but there still exist other major epitope(s) expressed commonly in AGE-proteins.

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Metadata

Authors
Ikeda, K., Higashi, T., Sano, H., Jinnouchi, Y., Yoshida, M., Araki, T., Ueda, S., & Horiuchi, S.
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
1996-01-01
Volume
35
Issue
24
Pages
8075-8083
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi9530550
OpenAlex
W2025016154
Cited by
434
References
10
FWCI
15.85
Type
journal article
Language
en
Open access
closed

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