Artikel
Proteomics-based identification of differentially expressed proteins in human meningiomas
Proteom-basierte Identifikation von unterschiedlich exprimierten Proteinen bei menschlichen Meningeomen
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Autoren
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M. Scholz
- Neurochirurgische Universitätsklinik, Ruhr-Universität Bochum
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M. Schönenbrücher
- Neurochirurgische Universitätsklinik, Ruhr-Universität Bochum
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U. Schlegel
- Neurologische Universitätsklinik, Ruhr-Universität Bochum
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K. Koch
- Neurologische Universitätsklinik, Ruhr-Universität Bochum
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C. Knobbe
- Institut für Neuropathologie, Heinrich-Heine-Universität Düsseldorf
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G. Reifenberger
- Institut für Neuropathologie, Heinrich-Heine-Universität Düsseldorf
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K. Stühler
- Medizinisches Proteom-Center, Ruhr-Universität Bochum
| Veröffentlicht: | 8. Mai 2006 |
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Gliederung
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Objective: Meningiomas are primary tumors of the nervous system consisting of neoplastic meningeal cells. The vast majority of meningiomas are benign tumors of World Health Organization (WHO) grade I. Approximately 10% of meningiomas correspond to WHO grade II (atypical meningiomas) and 2-3% to WHO grade III (anaplastic meningiomas). Clinically, atypical meningiomas are associated with an increased likelihood of local recurrence, even after complete resection. Anaplastic meningiomas are highly malignant tumors associated with poor prognosis as indicated by a mean survival time of only 2-3 years after diagnosis. The aim of our study was to identify novel molecular markers for the different meningioma grades using state of the art proteomic techniques.
Methods: For differential proteome analysis protein lysates from 5 normal arachnoidal tissue samples, 6 benign meningiomas (WHO grade I), 6 atypical meningiomas (WHO grade II), and 4 anaplastic meningiomas (WHO grade III) were analysed using fluorescence difference gel electrophoresis (DIGE). Age of the patients at operation ranged between 48-83 years. Subsequent image analysis using DeCyder software (v.6.0, GE Healthcare) differentially expressed proteins were excised from the two dimensional electrophoresis (2-DE) gel; in-gel digested and subjected to MALDI-TOF mass spectrometry analysis.
Results: Proteomic analysis could be successfully performed for all samples. So far, we identified and characterized a total of 33 different proteins showing evidence of differential expression between different meningioma grades or between meningiomas and normal arachnoidal tissue. Differential expression of these candidate proteins will be verified by using independent techniques such as Western blot analysis and/or immunohistochemistry.
Conclusions: Proteomic analysis represents a feasible approach to identify novel molecular markers for human meningiomas of different WHO grades. Further studies are in progress to independently verify the identified candidate proteins and to evaluate their potential utility as diagnostic and/or prognostic markers.
