Kumari, N and Bandyopadhyay, D and Kumar, V and Venkatesh, DB and Prasad, S and Prakash, S and Krishnaswamy, PR and Balaram, P and Bhat, N (2021) Glycation of albumin and its implication in Diabetes: A comprehensive analysis using mass spectrometry. In: Clinica Chimica Acta, 520 . pp. 108-117.
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Abstract
Aim: To understand the mechanism of glycation of albumin and effects on cysteinylation and methionine oxidation. Methods: The in vitro glycation of HSA and BSA was studied with varying concentrations of glucose. Clinical blood samples of diabetic subjects with varying HbA1c values, were analyzed to assess in vivo glycation. All samples and their tryptic digests were analyzed using liquid chromatography/mass spectrometry. Glycation sites were mapped on to the three-dimensional structure of the HSA and BSA. Results: A total thirty-one sites for glycation and eight sites of Nε-carboxymethyl-lysine (CML) modification were identified on albumin. The site selectivity of glycation was correlated with the environment of the reactive residue in the three-dimensional structure. Conclusions: The maximum percentage glycation under extreme conditions was in the range of ~55 to 88 in four weeks. Two major glycation sites K-233 and K-525 were identified, which together accounted for 40�50 of total glycation. A correlation was observed between glycation and oxidation of methionine residues in samples glycated in vitro. The role of spatially proximate residues in facilitating the glycation process is evident. The tri- and tetra-glycated isoforms of albumin can serve as biomarkers for the severe uncontrolled diabetic state. © 2021 Elsevier B.V.
Item Type: | Journal Article |
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Publication: | Clinica Chimica Acta |
Publisher: | Elsevier B.V. |
Additional Information: | The copyright for this article belongs to Elsevier B.V. |
Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit Division of Interdisciplinary Sciences > Centre for Nano Science and Engineering |
Date Deposited: | 01 Sep 2021 08:35 |
Last Modified: | 01 Sep 2021 08:35 |
URI: | http://eprints.iisc.ac.in/id/eprint/69460 |
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