Journal of Proteomics & Bioinformatics

Journal of Proteomics & Bioinformatics
Open Access

ISSN: 0974-276X

Structural modification of histone by glyoxal: Recognition by autoantibodies in type 1 diabetes and cancer


International Conference & Exhibition on Proteomics & Bioinformatics

2011

Nadeem A. Ansari, D. Dash

Scientific Tracks Abstracts: J Proteomics Bioinform

Abstract :

Reactive carbonyl species (RCS) reacts non-enzymatically with amino groups of lysine and arginine to form advanced glycation end products (AGEs). In the present study glyoxal mediated glycoxidation of histone was undertaken and the modified peptide was characterized by spectral studies involving IR and Mass Spectrometry together with polyacrylamide gel electrophoresis. RCS-induced modification was confirmed by quenching study involving penicillamine and aminoguanidine as carbonyl scavengers. Presence of antibodies against glycoxidated histone in sera of type 1 diabetes and breast cancer patients was evaluated by solid phase enzyme immunoassay. The findings indicate that as a result of structural perturbation in the histone by glyoxal, the modified histone plays a major role in production of autoantibodies in diabetes and cancer patients.

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