Identification of Up-Regulated Low Molecular Weight Proteins in Human Adipocytes Treated with Glycoxidized Albumin

Nihar Ranjan Singh, Philippe Rondeau, Emmanuel Bourdon*
LBGM - Universite de la Reunion - 15, avenue Rene Cassin - BP 7151 - Cedex 09, 97715 Saint Denis de La Reunion, France.

© 2010 Singh et al.

open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

* Address correspondence to this author at the LBGM - Université de la Réunion - 15, avenue René Cassin – BP 7151 – Cedex 09, 97715 Saint Denis de La Réunion, France; Tel: (+262) 262 93 86 48; Fax: (+262) 262 93 82 37; E-mail:


Diabetes and Obesity are strongly associated with enhanced circulating advanced glycoxidation end products (AGEs), and adipose tissue constitutes a biological driver in the metabolic syndrome characterized by abdominal obesity, dyslipidemia and insulin resistance. We determined whether AGEs issued from glycoxidized albumin could induce expression of determinant proteins in human adipocyte cell lines (SW872).

Cell proteins separation by 2D gels and mass spectrometry were combined to identify up-regulated proteins in SW872 treated with AGEs. Four low molecular weight proteins appeared as more expressed in adipocytes treated with glycated albumin than with native albumin. All four proteins have determinant role in adipocyte physiology as they exert antioxidant activities (superoxide dismutase and proteasome subunit) or energy production properties (phosphoglycerate mutase and triosephosphate isomerase).

Proteomic analyses of SW872 cells have never been performed before. By using proteomic analyses, our results bring new evidence of AGEs-involvement in metabolic disorders at the adipocyte level.

Keywords: Glycoxidation, albumin, adipocytes, oxidative stress, SW872, glycation, diabetes.