albumin - publications

1. Arch Biochem Biophys. 2012 Apr 10. [Epub ahead of print]

Structural and immunological characterization of Amadori-rich human serum
albumin: Role in diabetes mellitus.

Arif B, Ashraf JM, Moinuddin, Ahmad J, Arif Z, Alam K.

Department of Biochemistry, Faculty of Medicine, A.M.U., Aligarh 202002, UP,
India.

Proteins modifications in diabetes may lead to early glycation products (EGPs) as
well as advanced glycation end products (AGEs). Whereas no extensive studies have
been carried out to assess the role of EGPs in secondary complications of
diabetes, numerous investigators have demonstrated the role of AGEs. Early
glycation involves attachment of glucose on ε-NH(2) of lysine residues of
proteins leading to generation of the Amadori product (an early glycation
species). This study reports the structural and immunological characterization of
EGPs of HSA because we believe that during persistent hyperglycemia the HSA, one
of the major blood proteins, can undergo fast glycation. Glucose mediated
generation of EGPs of HSA was quantitated as Amadori products by NBT assay and
authenticated by boronate affinity chromatography and LC/MS. Compared to native
HSA changes in glycated-HSA were characterized by hyperchromicity, loss in
fluorescence intensity and a new peak in the FTIR profile. Immunogenicity of
native- and glycated-HSA was evaluated by inducing antibodies in rabbits. Results
suggest generation of neo-epitopes on glycated-HSA rendering it highly
immunogenic compared to native HSA. Quantization of EGPs of HSA by authentic
antibodies against HSA-EGPs can be used as marker for early detection of the
initiation/progression of secondary complications of diabetes.

Copyright © 2012. Published by Elsevier Inc.

PMID: 22516656 [PubMed - as supplied by publisher]