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Clinical Chemistry 0: clinchem.2006.070979v1, 2006; 10.1373/clinchem.2006.070979
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Received on ,
Accepted on ,

Technical Briefs

Direct-Tissue SELDI-TOF Mass Spectrometry Analysis: A New Application for Clinical Proteomics,

Ali Bouamrani 1, Jessica Ternier 2, David Ratel 1, Alim-Louis Benabid 2, Jean-Paul Issartel 1, Elisabeth Brambilla 3, François Berger 1*

1 INSERM U318, Université de Grenoble, Grenoble, France
2 INSERM U318, Université de Grenoble, Grenoble, France, and Department of Neurosurgery, Centre Hospitalier Universitaire Grenoble, Grenoble, France
3 Department of Pathology, Centre Hospitalier Universitaire Grenoble, Grenoble, France

* To whom correspondence should be addressed. E-mail: fberger{at}ujf-grenoble.fr.

Background: New molecular profiling technologies can aid in analysis of small pathologic samples obtained by minimally invasive biopsy and may enable the discovery of key biomarkers synergistic with anatomopathologic analysis related to prognosis, therapeutic response, and innovative target validation. Thus proteomic analysis at the histologic level in healthy and pathologic settings is a major issue in the field of clinical proteomics.

Methods: We used surface-enhanced laser desorption ionization-time-of-flight mass spectrometry (SELDI-TOF MS) technology with surface chromatographic subproteome enrichment and preservation of the spatial distribution of proteomic patterns to detect discrete modifications of protein expression. We performed in situ proteomic profiling of mouse tissue and samples of human cancer tissue, including brain and lung cancer.

Results: This approach permitted the discrimination of glioblastomas from oligodendrogliomas and led to the identification of 3 potential markers.

Conclusion: Direct tissue proteomic analysis is an original application of SELDI-TOF MS technology that can expand the use of clinical proteomics as a complement to the anatomopathological diagnosis.


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