Physicochemical studies on glycation-induced structural changes in human igg

被引：51

作者：

Ahmad, Saman ^{[1
]}

Moinuddin ^{[1
]}

Khan, Rizwan Hasan ^{[2
,3
]}

Ali, Asif ^{[1
]}

机构：

[1] Aligarh Muslim Univ, Dept Biochem, Fac Med, JN Med Coll, Aligarh 202002, Uttar Pradesh, India

[2] UCL, Div Biosci, Dept Struct & Mol Biol, London, England

[3] Aligarh Muslim Univ, Interdisciplinary Biotechnol Unit, Aligarh 202002, Uttar Pradesh, India

来源：

IUBMB LIFE | 2012年 / 64卷 / 02期

关键词：

glycation; IgG; spectroscopy; AGEs; glucose; OPTICAL-ROTATORY DISPERSION; HUMAN-SERUM-ALBUMIN; POLY-L-LYSINE; RHEUMATOID-ARTHRITIS; NONENZYMATIC GLYCOSYLATION; CIRCULAR-DICHROISM; IMMUNOGLOBULIN-G; MASS-SPECTROMETRY; END-PRODUCT; PROTEINS;

D O I：

10.1002/iub.582

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Glycation of biomolecules leads to the formation of advanced glycation end products (AGEs). Glycation of immunoglobulin G (IgG) has been implicated in autoimmune diseases such as rheumatoid arthritis (RA). In this study, human IgG was glycated with physiological concentration of glucose. The changes induced in IgG were analyzed by UV, fluorescence, circular dichroism, and Fourier transform infrared (FTIR) spectroscopy; thermal denaturation studies, native, and Sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis. The ketoamine moieties and carbonyl content were also quantitated in glycated IgG. We report structural perturbations, increased carbonyl content, and ketoamine moieties in the glycated IgG. This may interfere with the normal function of IgG and may contribute to initiation of arthritic complications. AGEs damaged IgG may be used as a biomarker for early detection of RA and the associated secondary complications. (c) 2012 IUBMB Life, 2012

引用

页码：151 / 156

页数：6

共 36 条

[1]

Advanced glycation endproducts - role in pathology of diabetic complications [J].

Ahmed, N .

DIABETES RESEARCH AND CLINICAL PRACTICE, 2005, 67 (01) :3-21

[2]

Oxidative stress in systemic lupus erythematosus and allied conditions with vascular involvement [J].

Ames, PRJ ;

Alves, J ;

Inanc, M ;

Isenberg, DA ;

Nourooz-Zadeh, J .

RHEUMATOLOGY, 1999, 38 (06) :529-534

[3]

Preferential recognition of Amadori-rich lysine residues by serum antibodies in diabetes mellitus: Role of protein glycation in the disease process [J].

Ansari, Nadeem A. ;

Moinuddin ;

Alam, Khursheed ;

Ali, Asif .

HUMAN IMMUNOLOGY, 2009, 70 (06) :417-424

[4]

Physicochemical Analysis of Poly-L-lysine: An Insight into the Changes Induced in Lysine Residues of Proteins on Modification with Glucose [J].

Ansari, Nadeem Ahmad ;

Moinuddin ;

Ali, Rashid .

IUBMB LIFE, 2011, 63 (01) :26-29

[5]

AUSTIN GE, 1987, CLIN CHEM, V33, P2220

[6]

Brwonlee M., 1998, NEW ENGL J MED, V318, P1315

[7]

Bucala R, 1992, Adv Pharmacol, V23, P1

[8]

DETERMINATION OF SECONDARY STRUCTURES OF PROTEINS BY CIRCULAR-DICHROISM AND OPTICAL ROTATORY DISPERSION [J].

CHEN, YH ;

YANG, JT ;

MARTINEZ, HM .

BIOCHEMISTRY, 1972, 11 (22) :4120-+

[9]

Interaction of bovine serum albumin with anionic surfactants [J].

Deep, S ;

Ahluwalia, JC .

PHYSICAL CHEMISTRY CHEMICAL PHYSICS, 2001, 3 (20) :4583-4591

[10]

EFFECT OF NONENZYMATIC GLYCATION ON THE STRUCTURE OF IMMUNOGLOBULIN-G [J].

DOLHOFERBLIESENER, R ;

GERBITZ, KD .

BIOLOGICAL CHEMISTRY HOPPE-SEYLER, 1990, 371 (08) :693-697

← 1 2 3 4 →