Up regulated expression of β actin Glioma tumor discovery by tandem Mass Spectrometry

MALDI-TOF-TOF Mass Spectrometry based analysis of the low molecular weight fraction of serum proteome allow identifying proteome profiles (signatures) that are potentially useful in detection an classification of cancer. The major objective of clinical proteomics is to identify differences between proteomes of healthy and sick persons, relations between the state of the proteome and the degree of development of the disease, and changes initiated in response to the treatment. The primary aim of clinical proteomics is identification characterization, and verification of protein biomarkers useful in the molecular diagnostics of the cancer. We extracted proteins of tumor and normal brain tissues and then evaluated the protein purity by Bradford test. In this study, we separated proteins by Two-Dimensional Gel Electrophoresis method and the spots were then analyzed and compared using statistical data and specific software, Spots were identified by pH isoelectric, molecular weights and data banks. We have determined their protein profiles using a 2D gel electrophoresis and MALDI-TOF-TOF Mass Spectrometry approach. β actin has been shown to be up-regulated in liver, gastric, colorectal, lung cancers and in melanomas. The overexpression of b actin in cancers suggests that it may have altered function in carcinogenesis, including of glioblastoma as lung cancers and melanomas are primary tumours that are responsible for the occurrence of secondary GBM. Recent studies have shown that β actin polymerization can promote cell motility, invasiveness and metastasis.

کلیدواژه ها:

β actin ، Glioma ، Proteome ، MALDI-TOF-TOF