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Retracted: Clinical and Technical Phosphoproteomic Research

Elena López1*, Isabel López2, Antonio Ferreira3 and Julia Sequí4

Author Affiliations

1 Inflammatory core, Centro de Investigación i+12 del Hospital Universitario 12 de Octubre, Avda de Córdoba s/n 28041, Madrid, Spain

2 Hematology Department, Hospital Universitario 12 Octubre, Avda de Córdoba s/n 28041, Madrid, Spain

3 Immunology Department, Hospital Universitario La Paz, P° de la Castellana 261-28046, Madrid, Spain

4 Immunology Department, Hospital Carlos III, Sinesio Delgado 28029, Madrid, Spain

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Proteome Science 2011, 9:27  doi:10.1186/1477-5956-9-27

Published: 2 June 2011


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An encouraging approach for the diagnosis and effective therapy of immunological pathologies, which would include cancer, is the identification of proteins and phosphorylated proteins. Disease proteomics, in particular, is a potentially useful method for this purpose. A key role is played by protein phosphorylation in the regulation of normal immunology disorders and targets for several new cancer drugs and drug candidates are cancer cells and protein kinases. Protein phosphorylation is a highly dynamic process. The functioning of new drugs is of major importance as is the selection of those patients who would respond best to a specific treatment regime. In all major aspects of cellular life signalling networks are key elements which play a major role in inter- and intracellular communications. They are involved in diverse processes such as cell-cycle progression, cellular metabolism, cell-cell communication and appropriate response to the cellular environment. A whole range of networks that are involved in the regulation of cell development, differentiation, proliferation, apoptosis, and immunologic responses is contained in the latter. It is so necessary to understand and monitor kinase signalling pathways in order to understand many immunology pathologies. Enrichment of phosphorylated proteins or peptides from tissue or bodily fluid samples is required. The application of technologies such as immunoproteomic techniques, phosphoenrichments and mass spectrometry (MS) is crucial for the identification and quantification of protein phosphorylation sites in order to advance in clinical research. Pharmacodynamic readouts of disease states and cellular drug responses in tumour samples will be provided as the field develops. We aim to detail the current and most useful techniques with research examples to isolate and carry out clinical phosphoproteomic studies which may be helpful for immunology and cancer research. Different phosphopeptide enrichment and quantitative techniques need to be combined to achieve good phosphopeptide recovery and good up- and-down phospho-regulation protein studies.