Phosphoproteomics and cancer research

被引:49
作者
Ashman, Keith [1 ]
Lopez Villar, Elena [1 ]
机构
[1] CNIO, Biotechnol Programme, ES-28029 Madrid, Spain
关键词
Immobilised metal ion affinity chromatography (IMAC); Titanium dioxide; Mass spectrometry (MS); Protein phosphorylation; Kinase signalling; Cancer; MULTIPLY PHOSPHORYLATED PEPTIDES; QUANTITATIVE PROTEOMIC ANALYSIS; ION AFFINITY-CHROMATOGRAPHY; STAINED POLYACRYLAMIDE-GELS; MASS-SPECTROMETRIC ANALYSIS; TYROSINE KINASE INHIBITORS; POSTTRANSLATIONAL MODIFICATIONS; SIGNALING NETWORKS; IN-VIVO; PHOSPHOPEPTIDE ENRICHMENT;
D O I
10.1007/s12094-009-0369-z
中图分类号
R73 [肿瘤学];
学科分类号
100214 [肿瘤学];
摘要
Protein phosphorylation plays key roles in the regulation of normal and cancer cells. It is a highly dynamic process. Protein kinases are the targets of several new cancer drugs and drug candidates. However, some of the main issues related to new drugs are how they function and the selection of those patients that will likely respond best to a particular treatment regime. There is an urgent need to understand and monitor kinase signalling pathways. Phosphoproteomics requires the enrichment of phosphorylated proteins or peptides from tissue or bodily fluids, and the application of technologies such as mass spectrometry (MS) to the identification and quantification of protein phosphorylation sites. As the field develops it will provide pharmacodynamic readouts of disease states and cellular drug responses in tumour samples. There have been a number of recent advances, but there are still technical hurdles and bioinformatics challenges that need to be addressed.
引用
收藏
页码:356 / 362
页数:7
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