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d-Ribose contributes to the glycation of serum protein by Yao Chen; Lexiang Yu; Yujing Wang; Yan Wei; Yong Xu; Tao He; Rongqiao He is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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d-Ribose is active in glycation and rapidly produces advanced glycation end products, leading to cell death and to cognitive impairment in mice. Glycated serum protein (GSP) is a relatively short-term biomarker for glycemic control in diabetes mellitus. However, whether d-ribose is related to GSP is unclear. The aim of this work was to identify the contribution of d-ribose to GSP compared to d-glucose. Here, we showed that the yield of glycated human serum albumin with d-ribose was at least two-fold higher than that with d-glucose in a 2-week incubation. The glycation of human serum albumin (HSA) with d-ribose was much faster than that with d-glucose, as determined by monitoring changes in the fluorescent intensity of glycation products with time. Liquid chromatography-mass spectrometry/mass spectrometry revealed that 17 and 7 lysine residues on HSA were glycated in the presence of d-ribose and d-glucose, respectively, even when the concentration ratio [d-ribose]/[d-glucose] was 1/50. The intraperitoneal injection of d-ribose significantly increased the GSP levels in Sprague Dawley rats, but the injection of d-glucose did not. The level of d-ribose was more positively associated wi

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Author

Yao Chen; Lexiang Yu; Yujing Wang; Yan Wei; Yong Xu; Tao He; Rongqiao He

Publisher

Elsevier BV

Published

2019

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)