ABSTRACT
Chronic hypoxia exists in many diseases, including cancer. The subject of our study is analysis of molecular pathways affected in the chronically hypoxic mouse brain. Using the emPAl protocol, we performed a quantitative proteomic approach to characterize the global proteome in the mouse brain exposed to 7% O[2] for 48 hours. Utilizing the emPAl protocol to estimate protein abundance and assign molar concentrations to all proteins, we were able to identify 33 proteins with significant changes in their expression. Deregulated proteins were mainly involved in cell metabolism, apoptosis, Ca[2+] signaling, pentose phosphate pathway, 14-3-3 protein mediated signaling cascades and protein degradation. The obtained data will provide some clues for understanding mechanisms with which cells respond and adapt to chronic hypoxia
ABSTRACT
Proteomics concerns itself with the characterization and function of all cellular proteins, the ultimate determinants of cellular function. Mass spectrometry has emerged as the preferred method for in-depth characterization of the protein components of biological systems. Using mass spectrometry, key insights into the composition, regulation and function of molecular complexes and pathways have been gained. Now days, mass spectrometry-based proteomics has become an indispensable tool in the cellular and molecular life sciences. This review discusses current mass spectrometry-based proteomics technologies