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

Ansari, Nadeem A.; Moinuddin, Mohammed; Alam, Khursheed; Ali, Asif

doi:10.1016/j.humimm.2009.03.015

Cited by 63 publications

(36 citation statements)

References 40 publications

(26 reference statements)

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“…Reactive carbonyl species, such as glyoxal, modify lysine and arginine residues of proteins but their reaction products (AGEs) were detected by antibodies specific for sugar-derived AGEs [58]. In our study, antigenicity of glycated lysine residues in proteins was probed by immunization of rabbits with glycated poly-L-lysine [5]. Glycated poly-L-lysine was found to be highly antigenic and the antigen exhibited a high degree of specificity for the induced antibodies.…”

Section: Antigenicity Of Glycated Lysine Residues In Proteinsmentioning

confidence: 87%

“…Sera of diabetic patients were probed for the presence of antibodies against glycated lysine residues with the use of glycated poly-L-lysine. Amadori-rich glycated poly-L-lysine was recognized by 64% of serum antibodies from diabetic patients (both type 1 & 2) [5]. The higher binding to glycated poly-L-lysine by the antibodies in diabetic patients suggests the involvement of glycated lysine residues in the production of autoantibodies in these patients.…”

Section: Serum Autoantibodies Against Oxidized and Glycated Proteins mentioning

confidence: 95%

“…Previous reports on poly-L-lysine, a homopolymer of lysine residues with a large number of free ε-amino groups, were restricted to characterization of their browning products or AGEs [37,38]. In our investigation, the polypeptide was used to elaborate the role of Amadori lysine adducts in diabetes mellitus [5,6].…”

Section: Glycated Lysine-rich Proteins and Their Involvement In Age-rmentioning

confidence: 99%

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Glycated Lysine Residues: A Marker for Non-Enzymatic Protein Glycation in Age-Related Diseases

2011

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Abstract.Nonenzymatic glycosylation or glycation of macromolecules, especially proteins leading to their oxidation, play an important role in diseases. Glycation of proteins primarily results in the formation of an early stage and stable Amadori-lysine product which undergo further irreversible chemical reactions to form advanced glycation endproducts (AGEs). This review focuses these products in lysine rich proteins such as collagen and human serum albumin for their role in aging and age-related diseases. Antigenic characteristics of glycated lysine residues in proteins together with the presence of serum autoantibodies to the glycated lysine products and lysine-rich proteins in diabetes and arthritis patients indicates that these modified lysine residues may be a novel biomarker for protein glycation in aging and age-related diseases.

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Section: Antigenicity Of Glycated Lysine Residues In Proteinsmentioning

confidence: 87%

Section: Serum Autoantibodies Against Oxidized and Glycated Proteins mentioning

confidence: 95%

Section: Glycated Lysine-rich Proteins and Their Involvement In Age-rmentioning

confidence: 99%

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Glycated Lysine Residues: A Marker for Non-Enzymatic Protein Glycation in Age-Related Diseases

2011

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“…A constant amount of antigen (native IgG or AGE-IgG) was mixed with varying amounts of IgG from RA patients and the interaction was allowed for 2 h at 37°C and then overnight at 4°C [16]. At the end of incubation, one-tenth volume of sample buffer (10% glycerol, 2% SDS, 0.5 M Tris pH 6.8 and 0.002% bromophenol blue) was added to antigen-antibody complex and the non-reducing SDS-PAGE was carried out on 10% SDS-polyacrylamide for 3-5 h at 80 volts.…”

Section: Band Shift Assaymentioning

confidence: 99%

Preferential recognition of epitopes on AGE–IgG by the autoantibodies in rheumatoid arthritis patients

Ahmad¹,

Habib²,

Moinuddin³

et al. 2013

Human Immunology

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“…Random bred, New Zealand White female rabbits were immunized as described previously (18). Briefly, rabbits (n 5 4; two each for native and modified DNA) were immunized intramuscularly at multiple sites with 50 lg of respective antigens complexed with methylated bovine serum albumin (mBSA) (Sigma, St. Louis, MO) in 1:1 ratio (w/w) and emulsified with an equal volume of Freund's adjuvant (Sigma, St. Louis, MO).…”

Section: Immunization Schedulementioning

confidence: 99%

Acquired immunogenicity of human DNA damaged by N‐hydroxy‐N‐acetyl‐4‐aminobiphenyl

Shahab¹,

Moinuddin²,

Ahmad³

et al. 2012

IUBMB Life

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Summary4-Aminobiphenyl, a known carcinogen, has many environmental sources like cigarette smoke, industrial waste, and so forth. It can be metabolized to form a potent mutagen, N-hydroxy-N-acetyl-4-aminobiphenyl (N-OH-AABP) that undergoes further processing to form electrophilic nitrenium ions which interact with DNA-forming covalent adducts, thereby exerting genotoxic effects. While the mutagenicity of N-OH-AABP has been amply reported, no extensive studies have been performed to assess the immunogenicity of N-OH-AABP-modified DNA. In this study, human placental DNA was modified with N-OH-AABP, and the structural perturbations in the DNA molecule were evaluated by ultraviolet spectroscopy and nuclease S1 digestion. Native and N-OH-AABP-modified DNA were used as antigens for immunizing female rabbits. The modified DNA was found to be highly immunogenic, eliciting high titer immunogen-specific antibodies, while the native form was almost nonimmunogenic. The induced antibodies exhibited wide range of heterogeneity in recognizing various nucleic acid conformers and DNA bases. We also detected deposits of immune complex in glomerular basement membrane in rabbits immunized with N-OH-AABP-DNA. Possible role of N-OH-AABP-DNA in the induction of antibodies in cancer patients and the related consequences have been discussed.

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

Cited by 63 publications

References 40 publications

Glycated Lysine Residues: A Marker for Non-Enzymatic Protein Glycation in Age-Related Diseases

Glycated Lysine Residues: A Marker for Non-Enzymatic Protein Glycation in Age-Related Diseases

Preferential recognition of epitopes on AGE–IgG by the autoantibodies in rheumatoid arthritis patients

Acquired immunogenicity of human DNA damaged by N‐hydroxy‐N‐acetyl‐4‐aminobiphenyl

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