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From Serological Proteome Analysis to Multiple Affinity Protein Profiling
a Protein Biochemistry and Proteomics Laboratory, UFR SMBH Leonard de Vinci, University Paris13, 93017 Bobigny cedex, France
Key Words: autoantibodies autoantibody autoantibody signature autoantigen biomarker cancer immunomics mass spectrometry proteome proteomics serological proteome analysis
Address for correspondence: Michel Caron, Protein Biochemistry and Proteomics Laboratory, CNRS UMR 7033 (BioMoCeti), UFR SMBH Leonard de Vinci, University Paris13, 74, rue Marcel Cachin, 93017 Bobigny cedex, France. Voice: 33-1-48-38-77-54; fax: 33-1-48-38-73-13. caron_prot{at}yahoo.fr.
Cancer remains one of the leading causes of death worldwide. Thus, to identify any useful biomarkers is still a need. We performed "cancer immunomics" to identify autoantibody signatures produced in response to the presence of either breast or colorectal cancer. SERological proteome analysis (SERPA) was performed by two-dimensional (2-D) electrophoresis separation, immunoblotting, image analysis, and mass spectrometry. Alternatively, to identify the antigens recognized by the autoantibodies of cancer patients, we developed an approach combining 2-D immunoaffinity chromatography, enzymatic digestion of the isolated antigens, nano flow separation of the resulting peptides, and identification: MAPPing (multiple affinity protein profiling). By these approaches we identified both proteins recognized by autoantibodies independently of a cancer status, and a limited number of proteins reacting preferentially with cancer sera.
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