Review: Glycation of human serum albumin

被引：315

作者：

Anguizola, Jeanethe ^{[1
]}

Matsuda, Ryan ^{[1
]}

Barnaby, Omar S. ^{[1
]}

Hoy, K. S. ^{[1
]}

Wa, Chunling ^{[1
]}

DeBolt, Erin ^{[1
]}

Koke, Michelle ^{[1
]}

Hage, David S. ^{[1
]}

机构：

[1] Univ Nebraska, Dept Chem, Lincoln, NE 68588 USA

来源：

CLINICA CHIMICA ACTA | 2013年 / 425卷

基金：

美国国家科学基金会; 美国国家卫生研究院;

关键词：

Human serum albumin; Glycation; Glycated albumin; Diabetes; Protein modification; Drug-protein binding; PERFORMANCE AFFINITY-CHROMATOGRAPHY; DRUG BINDING-SITES; FATTY-ACID-BINDING; END-PRODUCTS AGES; PROTEIN-BINDING; IN-VITRO; NONENZYMATIC GLYCOSYLATION; MASS-SPECTROMETRY; QUANTITATIVE-ANALYSIS; LIGAND-BINDING;

D O I：

10.1016/j.cca.2013.07.013

中图分类号：

R446 [实验室诊断]; R-33 [实验医学、医学实验];

学科分类号：

1001 ;

摘要：

Glycation involves the non-enzymatic addition of reducing sugars and/or their reactive degradation products to amine groups on proteins. This process is promoted by the presence of elevated blood glucose concentrations in diabetes and occurs with various proteins that include human serum albumin (HSA). This review examines work that has been conducted in the study and analysis of glycated HSA. The general structure and properties of HSA are discussed, along with the reactions that can lead to modification of this protein during glycation. The use of glycated HSA as a short-to-intermediate term marker for glycemic control in diabetes is examined, and approaches that have been utilized for measuring glycated HSA are summarized. Structural studies of glycated HSA are reviewed, as acquired for both in vivo and in vitro glycated HSA, along with data that have been obtained on the rate and thermodynamics of HSA glycation. In addition, this review considers various studies that have investigated the effects of glycation on the binding of HSA with drugs, fatty acids and other solutes and the potential clinical significance of these effects. (C) 2013 Elsevier B.V. All rights reserved.

引用

页码：64 / 76

页数：13

共 145 条

[1] Chromatographic assay of glycation adducts in human serum albumin glycated in vitro by derivatization with 6-aminoquinolyl-N-hydroxysuccinimidyl-carbamate and intrinsic fluorescence [J].