title: Emerging applications for phospho-proteomics in cancer molecular therapeutics.
abstract: Protein phosphorylation is a key mechanism of cell regulation in normal and cancer cells. Various new cancer drugs and drug candidates are aimed at protein kinase targets. However, selecting patients likely to respond to these treatments, even among individuals with tumors expressing validated kinase targets remains a major challenge. There exists a need for biomarkers to facilitate the monitoring of modulation of drug-targeted kinase pathways. Phospho-proteomics involves the enrichment of phosphorylated proteins from tissue, and the application of technologies such as mass spectrometry (MS) for the identification and quantification of protein phosphorylation sites. It has potential to provide pharmacodynamic readouts of disease states and cellular drug responses in tumor samples, but technical hurdles and bioinformatics challenges will need to be addressed.
authors.affiliation: Cancer Program, Hospital For Sick Children, and McLaughlin Centre for Molecular Medicine, and Banting and Best Department of Medical Research, University of Toronto, Ontario, Canada. m.moran@utoronto.ca
authors.forename: Michael F
authors.initials: MF
authors.lastname: Moran
authors.forename: Jiefei
authors.initials: J
authors.lastname: Tong
authors.forename: Paul
authors.initials: P
authors.lastname: Taylor
authors.forename: Robert M
authors.initials: RM
authors.lastname: Ewing
mesh_terms: D000970:Antineoplastic Agents / Q000494:pharmacology / Q000627:therapeutic use*; D001665:Binding Sites / Q000187:drug effects; D015195:Drug Design; D006801:Humans; D009369:Neoplasms / Q000188:drug therapy* / Q000378:metabolism; D010750:Phosphoproteins / Q000737:chemistry* / Q000187:drug effects* / Q000378:metabolism; D010766:Phosphorylation; D040901:Proteomics / Q000379:methods; D013329:Structure-Activity Relationship
chemical_list: D000970:Antineoplastic Agents; D010750:Phosphoproteins