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Journal of Biomedicine and Biotechnology
Volume 2008, Article ID 564127, 10 pages
Research Article

Protein Alterations in Infiltrating Ductal Carcinomas of the Breast as Detected by Nonequilibrium pH Gradient Electrophoresis and Mass Spectrometry

1Laboratoire d'Immuno-Oncologie Moléculaire, Faculté de Médecine de Monastir, 5019 Monastir, Tunisia
2Institut Supérieur de Biotechnologie de Monastir, 5000 Monastir, Tunisia
3Plate Forme Protéomique, Institut de Biologie Moléculaire et Cellulaire, CNRS, 67084 Strasbourg, France
4Departement de Pathologie, Centre Hospitalo-Universitaire Farhat-Hached, 4002 Sousse, Tunisia
5Laboratoire Cytopath, 4000 Sousse, Tunisia
6Immunologie et Chimie thérapeutiques, UPR 9021-CNRS, Institut de Biologie Moléculaire et Cellulaire, 67084 Strasbourg, France
7Department of Genetic Medicine, Weill Cornell Medical College in Qatar, and Qatar Foundation, Doha, Qatar

Received 8 April 2007; Revised 20 November 2007; Accepted 19 January 2008

Academic Editor: Halima Bensmail

Copyright © 2008 Maria Kabbage et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Improvement of breast-cancer detection through the identification of potential cancer biomarkers is considered as a promising strategy for effective assessment of the disease. The current study has used nonequilibrium pH gradient electrophoresis with subsequent analysis by mass spectrometry to identify protein alterations in invasive ductal carcinomas of the breast from Tunisian women. We have identified multiple protein alterations in tumor tissues that were picked, processed, and unambiguously assigned identities by matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF). The proteins identified span a wide range of functions and are believed to have potential clinical applications as cancer biomarkers. They include glycolytic enzymes, molecular chaperones, cytoskeletal-related proteins, antioxydant enzymes, and immunologic related proteins. Among these proteins, enolase 1, phosphoglycerate kinase 1, deoxyhemoglobin, Mn-superoxyde dismutase, -B-crystallin, HSP27, Raf kinase inhibitor protein, heterogeneous nuclear ribonucleoprotein A2/B1, cofilin 1, and peptidylprolyl isomerase A were overexpressed in tumors compared with normal tissues. In contrast, the IGHG1 protein, the complement C3 component C3c, which are two newly identified protein markers, were downregulated in IDCA tissues.