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Phosphoproteomics is a branch of proteomics that identifies, catalogs, and characterizes proteins containing a phosphate group as a post-translational modification. Phosphorylation is a key reversible modification that regulates protein function, subcellular localization, complex formation, degradation of proteins and therefore cell signalling networks. With all of these modification results, it is assumed that up to 30% of all proteins may be phosphorylated, some multiple times. Compared to expression analysis, phosphoproteomics provides two additional layers of information. First, it provides clues on what protein or pathway might be activated because a change in phosphorylation status almost always reflects a change in protein activity. Second, it indicates what proteins might be potential drug targets as exemplified by the kinase inhibitor Gleevec. While phosphoproteomics will greatly expand knowledge about the numbers and types of phosphoproteins, its greatest promise is the rapid analysis of entire phosphorylation based signalling networks. == Overview of phosphoproteomic analysis == A sample large-scale phosphoproteomic analysis includes #Cultured cells undergo SILAC encoding. #Cells are stimulated with factor of interest (e.g. growth factor, hormone). #Stimulation can occur for various lengths of time for temporal analysis. #Cells are lysed and enzymatically digested. #Peptides are separated using ion exchange chromatography. #Phosphopeptides are enriched using phosphospecific antibodies, immobilized metal affinity chromatography or titanium dioxide (TiO2) chromatography. #Phosphopeptides are analyzed using mass spectrometry. #Peptides are sequenced and analyzed. 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Phosphoproteomics」の詳細全文を読む スポンサード リンク
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