Journal
MAILLARD REACTION: RECENT ADVANCES IN FOOD AND BIOMEDICAL SCIENCES
Volume 1126, Issue -, Pages 205-209Publisher
WILEY-BLACKWELL
DOI: 10.1196/annals.1433.065
Keywords
maillard reaction; glycation; lysine; redox-active metals; oxidation; dicarbonyls; methylgloxal; glyoxal; sugars; lipids
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Funding
- NATIONAL INSTITUTE ON AGING [R01AG018629] Funding Source: NIH RePORTER
- NIA NIH HHS [AG18629, R01 AG018629] Funding Source: Medline
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The epsilon-amino group of lysyl residues oxidatively deaminates in the presence of alpha-dicarbonyl sugars and redox-active metals forming alpha-aminoadipic acid-delta-semialdehyde (allysine; Suyarna'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 alpha-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).
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