Collagen undergoes continuous non-enzymatic glycation during its long life period. The products resulting from the glycation reaction, so-called advanced glycation end products (AGEs), were regarded as potential pathogens of various diseases such as diabetic complications. Although several AGEs were identified from acid hydrolysates of glycated collagen, the major AGE(s) responsible for the diseases have not yet been fully characterized. Moreover, acid-labile constituents were decomposed during acid hydrolysis. To investigate these AGEs, we used the enzymatic hydrolysis method [Bensusan, Dixit and McKnight (1971) Biochim. Biophys. Acta 251, 100-108]. As a result, an acid-labile unknown compound was discovered from the digested glycated collagen. We identified this compound as NΩ-carboxymethylarginine (CMA) by matrix-assisted laster-desorption ionization-MS and NMR. CMA gradually increased in collagen during incubation with glucose and the yield reached about 8 mol/mol of collagen, which is 100 times higher than that of pentosidine. This result suggests that CMA is a major AGE in collagen.

This content is only available as a PDF.