Cleavage of glycated protein cross-linking and cleavage of AGEs cross-linking of substances contained in vegetables and herbs.

Kim Yurim, Yokota Saki, Yagi Masayuki, Sakiyama Chieko, Yonei Yoshikazu

doi:10.24659/gsr.9.2_106

Glycative stress-induced production and accumulation of advanced glycation end products (AGEs) in the body contribute to aging and the development of various diseases. N-phenacylthiazolium bromide (PTB) cleaves the α-diketone bond, which is the most common glycation end product in the body. PTB cleaves α-diketone bonds and cleaves cross-links associated with the formation of AGEs in glycated proteins (cleavage of AGE cross-linking; CAC). However, since glucospan, α-diketone, and lysine-dihydropyridinium-lysine are involved in the formation of protein cross-links by glycation, the usefulness of the cross-link cleavage effect must be verified using glycated proteins. Whereas, measurement of cleavage of glycated-protein cross-linking (CGPC) using glycated lysozyme as a model has been reported. In this study, CGPC and CAC of 12 substances contained in vegetables and herbs were measured to examine the possibility of degradation of protein cross-links polymerized by glycation. 12 substances were measured for CGPC and CAC, and a high positive correlation was observed between CGPC and CAC in 6 substances (50%), indicating that α diketone bond cleavage may be involved in the degradation of glycated protein cross-links. In contrast, only CGPC was observed for the three substances, and it was possible that they cleaved cross-links different from the α-diketone structure; the CGPC measurement had the potential to evaluate glycated protein cross-link cleavage actions other than α-dicarbonyl bond cleavage.

Cleavage of glycated protein cross-linking and cleavage of AGEs cross-linking of substances contained in vegetables and herbs.

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