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Aging, Diabetes, and Renal Failure Catalyze the Oxidation of Lysyl Residues to 2‐Aminoadipic Acid in Human Skin Collagen
Author(s) -
Sell David R.,
Strauch Christopher M.,
Shen Wei,
Monnier Vincent M.
Publication year - 2008
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1433.065
Subject(s) - chemistry , biochemistry , stereochemistry , oxidative phosphorylation , amino acid , redox , organic chemistry
The ɛ‐amino group of lysyl residues oxidatively deaminates in the presence of α‐dicarbonyl sugars and redox‐active metals forming α‐aminoadipic acid‐δ‐semialdehyde (allysine; Suyama's hypothesis), which can further oxidize into 2‐aminoadipic acid. Here we show that 2‐aminoadipic acid is significantly ( P < 0.05) correlated with 6‐hydroxynorleucine, carboxyethyllysine (CEL), and carboxymethyllysine (CML) in human skin collagen. Since CEL and CML can originate from carbohydrate and lipid by oxidative decomposition and α‐dicarbonyl formation, these results provide support for Suyama's hypothesis. Allysine, in turn, is readily converted by oxidation into 2‐aminoadipic acid, which accumulates to high levels in skin (i.e., > 2 nmol/mg collagen).