Proteomics analyses enable the identification and quantitation of
proteins. From a purely clinical perspective, the application of proteomics based on innovations, may greatly affect the future management of malignant
brain tumors. This optimism is based on four main reasons: diagnosis, prognosis, selection of targeted
therapy based on molecular profile of the
brain tumor and monitoring therapeutic response, or resistance. We extracted the
proteins of
tumor and normal brain tissues, and then evaluated the
protein purity by Bradford test. In this study, we separated the
proteins by two-dimensional (2DG) gel electrophoresis methods. Then spots were analyzed, compared using statistical data and specific software and were identified by pH isoelectric, molecular weights and data banks. The
protein profiles were determined using 2D gel electrophoresis and MALDI TOF/TOF mass spectrometry approaches. Simple statistical tests were used to establish a putative hierarchy in which the change in
protein level was ranked according to a cut-off point with p<0.05. The 2D gel showed a total of 1328 spots among which 157 spots were under-expressed and 276 spots were overexpressed. Most
proteins are subjects to post-translational modifications, where
amino acid residues may be chemically modified or conjugated by small
proteins like
ubiquitin. Proteomics is a powerful way to identifying multiple
proteins which are altered following a neuropharmacological intervention in a
CNS disease.