摘要
糖尿病是世界上最严重的疾病之一。糖尿病患者血液中的糖化蛋白水平高于非糖尿病者血液中的糖化蛋白水平。蛋白的糖化被认为与糖尿病并发症和相关疾病的发生有关。本文综述了人类血清白蛋白(HSA)的糖化对其结构和功能的影响。糖化导致HSA构象的改变,这将进一步影响其配体结合特性。高血糖条件下糖化HSA水平表明其与糖尿病严重并发症的产生有重要关系,尤其是通过影响多种细胞的功能。来自单个报道的结论彼此矛盾;因此,关于糖化对HSA结合小分子行为的影响很难给出一个明确评论。HSA的糖化对其亲和小分子的影响是由试验、小分子的结构和糖化程度决定的。然而,HSA的糖化被认为可减少其对多酚和酚酸等酸性药物的结合亲和力。
关键词: 糖尿病,糖化,血浆蛋白,蛋白结合,血清白蛋白,结构和功能。
Current Medicinal Chemistry
Title:Glycation of Human Serum Albumin in Diabetes: Impacts on the Structure and Function
Volume: 22 Issue: 1
Author(s): Hui Cao, Tingting Chen and Yujun Shi
Affiliation:
关键词: 糖尿病,糖化,血浆蛋白,蛋白结合,血清白蛋白,结构和功能。
摘要: Diabetes mellitus is one of the most serious diseases in the world. The levels of glycated proteins in the blood of diabetics are higher than that of non-diabetic subjects. The glycation of proteins is believed to link to the occurrence of diabetic complications and related diseases. This review focuses on the influence of glycation of human serum albumin (HSA) on its structure and function. The glycation leads to change the HSA conformation, which will further influence its ligand binding properties. The levels of glycated HSA in hyperglycemic conditions showed a significant relationship to the germination of serious complications for diabetics, especially by affecting various cells functions. The conclusion from individual report is contradictory to each other; therefore, it is very difficult to give an univocal comment on the impact of glycation on the binding behaviors of HSA for small molecules. The influence of glycation of HSA on the binding affinities for small molecules is decided by the assay, the structures of small molecules, as well as the degree of glycation. However, the glycation of HSA is believed to reduce the binding affinities for acidic drugs such as polyphenols and phenolic acids.
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Cite this article as:
Hui Cao, Tingting Chen and Shi Yujun, Glycation of Human Serum Albumin in Diabetes: Impacts on the Structure and Function, Current Medicinal Chemistry 2015; 22 (1) . https://dx.doi.org/10.2174/0929867321666140912155738
DOI https://dx.doi.org/10.2174/0929867321666140912155738 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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