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Antibody-based detection of advanced glycation end-products: promises vs. limitations

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Abstract

Advanced glycation end-products (AGEs) of the Maillard reaction were originally measured according to their fluorescent and browning properties. A subsequent study with instrumental analyses such as high-performance liquid chromatography and gas chromatography mass spectrometry more clearly demonstrated the involvement of each AGE structure in pathological conditions. Furthermore, immunochemical methods have also been developed to clarify the localization of AGEs in tissues and measurement of AGEs in multiple clinical samples. Although the involvement of AGEs in age-related diseases has progressed due to immunochemical techniques, the relationship between AGE structure and diseases has not been clear because little was known about the epitope structure of each anti-AGE antibody. However, the development of epitope-identified antibodies against AGEs has made it possible to clarify AGE structures involved in diseases. This review discusses not only the usability of anti-AGE antibodies to evaluate AGEs and disease pathology and screen AGE inhibitors, but also describes their usage.

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Acknowledgments

This work was supported by JSPS KAKENHI Grant No. 15H02902 and 15 K12364 to Ryoji Nagai.

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Authors and Affiliations

  1. Laboratory of Food and Regulation Biology, Graduate School of Agriculture, Tokai University, Kawayou, Minamiaso, Aso-gun, Kumamoto, 869-1404, Japan

    Ryoji Nagai, Jun-ichi Shirakawa, Rei-ichi Ohno, Kota Hatano, Hikari Sugawa, Shoutaro Arakawa, Kenta Ichimaru, Shoh Kinoshita & Mime Nagai

  2. Department of Orthopaedic Surgery, Jikei University School of Medicine, Minato, Tokyo, Japan

    Shoutaro Arakawa

  3. Department of Pathology, Faculty of Medicine, Fukuoka University, Fukuoka, Japan

    Noriyuki Sakata

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  1. Ryoji Nagai
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  2. Jun-ichi Shirakawa
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Correspondence to Ryoji Nagai.

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Nagai, R., Shirakawa, Ji., Ohno, Ri. et al. Antibody-based detection of advanced glycation end-products: promises vs. limitations. Glycoconj J 33, 545–552 (2016). https://doi.org/10.1007/s10719-016-9708-9

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  • DOI: https://doi.org/10.1007/s10719-016-9708-9

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