A Perspective on the Maillard Reaction and the Analysis of Protein Glycation by Mass Spectrometry: Probing the Pathogenesis of Chronic Disease

被引：307

作者：

Zhang, Qibin ^{[1
]}

Ames, Jennifer M. ^{[2
]}

Smith, Richard D. ^{[1
]}

Baynes, John W. ^{[3
]}

Metz, Thomas O. ^{[1
]}

机构：

[1] Pacific NW Natl Lab, Div Biol Sci, Richland, WA 99352 USA

[2] Queens Univ Belfast, Sch Biol Sci, Human Nutr & Hlth Grp, Belfast BT9 5AG, Antrim, North Ireland

[3] Univ S Carolina, Sch Publ Hlth, Dept Exercise Sci, Columbia, SC 29208 USA

来源：

JOURNAL OF PROTEOME RESEARCH | 2009年 / 8卷 / 02期

关键词：

Maillard reaction; protein glycation; advanced glycation end-products (AGEs); diabetes mellitus; mass spectrometry; ELECTRON-TRANSFER DISSOCIATION; HUMAN-SERUM-ALBUMIN; NON-ENZYMATIC GLYCOSYLATION; AMINO-CARBONYL REACTION; HUMANIZED MONOCLONAL-ANTIBODY; HUMAN ADULT HEMOGLOBIN; END-PRODUCTS; MITOCHONDRIAL PROTEINS; DIABETIC-NEPHROPATHY; PLASMA-PROTEINS;

D O I：

10.1021/pr800858h

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The Maillard reaction, starting from the glycation of protein and progressing to the formation of advanced glycation end-products (AGEs), is implicated in the development of complications of diabetes mellitus, as well as in the pathogenesis of cardiovascular, renal, and neurodegenerative diseases. In this perspective review, we provide an overview on the relevance of the Maillard reaction in the pathogenesis of chronic disease and discuss traditional approaches and recent developments in the analysis of glycated proteins by mass spectrometry. We propose that proteomics approaches, particularly bottom-up proteomics, will play a significant role in analyses of clinical samples leading to the identification of new markers of disease development and progression.

引用

页码：754 / 769

页数：16

共 147 条

[1] Analysis of glycated insulin by MALDI-TOF mass spectrometry [J].

Abul Farah, M ;

Bose, S ;

Lee, JH ;

Jung, HC ;

Kim, Y .

BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 2005, 1725 (03) :269-282

[2] Advanced glycation endproducts: what is their relevance to diabetic complications? [J].

Ahmed, N. ;

Thornalley, P. J. .

DIABETES OBESITY & METABOLISM, 2007, 9 (03) :233-245

[3] Peptide mapping identifies hotspot site of modification in human serum albumin by methylglyoxal involved in ligand binding and esterase activity [J].

Ahmed, N ;

Dobler, D ;

Dean, M ;

Thornalley, PJ .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (07) :5724-5732

[4] The AGE inhibitor pyridoxamine inhibits lipemia and development of renal and vascular disease in Zucker obese rats [J].

Alderson, NL ;

Chachich, ME ;

Youssef, NN ;

Beattie, RJ ;

Nachtigal, M ;

Thorpe, SR ;

Baynes, JW .

KIDNEY INTERNATIONAL, 2003, 63 (06) :2123-2133

[5] Chemical modification of muscle protein in diabetes [J].

Alt, N ;

Carson, JA ;

Alderson, NL ;

Wang, YP ;

Nagai, R ;

Henle, T ;

Thorpe, SR ;

Baynes, JW .

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2004, 425 (02) :200-206

[6]

Amadori M., 1925, ATTI ACCAD NAZ LIN, V2, P337

[7]

Ames J. M., 1990, Trends in Food Science & Technology, V1, P150, DOI 10.1016/0924-2244(90)90113-D

[8]

Ames J.M., 2003, ENCY FOOD SCI NUTR, VSecond, P665, DOI 10.1016/130-12-227055-X/00128-0

[9] Application of semiquantitative proteomics techniques to the Maillard reaction [J].

Ames, JM .

MAILLARD REACTION: CHEMISTRY AT THE INTERFACE OF NUTRITION, AGING, AND DISEASE, 2005, 1043 :225-235

[10] Production of Nε-(carboxymethyl)lysine is impaired in mice deficient in NADPH oxidase -: A role for phagocyte-derived oxidants in the formation of advanced glycation end products during inflammation [J].

Anderson, MM ;

Heinecke, JW .

DIABETES, 2003, 52 (08) :2137-2143

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