d-Ribose contributes to the glycation of serum protein

Autor: Lexiang Yu, Yong Xu, Yan Wei, Yao Chen, Tao He, Rongqiao He, Yujing Wang
Rok vydání: 2019
Předmět:
Zdroj: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1865:2285-2292
ISSN: 0925-4439
Popis: 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 with GSP than the level of d -glucose in streptozotocin-treated rats. In diabetic patients, the levels of both d -ribose and d -glucose were closely related to the level of GSP. Together, these in vitro and in vivo findings indicated that d -ribose is an important contributor to the glycation of serum protein, compared to d -glucose. To assess GSP levels in diabetes mellitus, we should consider the contribution from d -ribose, which plays a nonnegligible role.
Databáze: OpenAIRE