UV B-irradiation enhances the racemization and isomerizaiton of aspartyl residues and production of N-epsilon-carboxymethyl lysine (CML) in keratin of skin

作者：Mori Yuhei; Aki Kenzo; Kuge Katsunori; Tajima Shingo; Yamanaka Natsuko; Kaji Yuichi; Yamamoto Naoki; Nagai Ryoji; Yoshii Hanako; Fujii Norihiko; Watanabe Masami; Kinouchi Tadatoshi; Fujii Noriko

来源：Journal of Chromatography B-Analytical Technologies in the Biomedical and Life Sciences, 2011, 879(29): 3303-3309.

DOI：10.1016/j.jchromb.2011.05.010

• UV B irradiation
• Racemization
• D-Aspartic acid
• Skin
• Advanced glycation end products (AGEs)
• Keratin

UV-B irradiation is one of the risk factors in age-related diseases. We have reported that biologically uncommon D-beta-Asp residues accumulate in proteins from sun-exposed elderly human skin. A previous study also reported that carboxymethyl lysine (CML; one of the advanced glycation end products (AGES)) which is produced by the oxidation of glucose and peroxidation of lipid, also increases upon UV B irradiation. The formation of D-beta-Asp and CML were reported as the alteration of proteins in UV B irradiated skin, independently. In this study, in order to clarify the relationship between the formation of D-beta-Asp and CML, immunohistochemical analysis using anti-D-beta-Asp containing peptide antibodies and anti-CML antibodies was performed in UV B irradiated mice. Immunohistochemical analyses clearly indicated that an anti-D-beta-Asp containing peptide antibody and anti-CML antibody reacted at a common area in UV B irradiated skin. Western blot analyses of the proteins isolated from UV B irradiated skin demonstrated that proteins of 50-70 kDa were immunoreactive towards antibodies for both D-beta-Asp containing peptide and CML. These proteins were identified by proteomic analysis as members of the keratin families including keratin-1, keratin-6B, keratin-10, and keratin-14.

• 出版日期2011-11-1