Important Clues of Current Phosphoproteomic Approaches for Clinical Research
|Elena López1*, Juan López Pascual2 and Julia Sequí3|
|1Centro de Investigación i+12, Hospital 12 de Octubre, Av. De Córdoba s/n 28040, Madrid, Spain|
|2Hematology Department, Hospital Universitario 12 de Octubre, Av. De Córdoba s/n 28040, Madrid, Spain|
|3Immunology Department, Hospital Carlos III, Sinesio Delgado 28029, Madrid, Spain|
|Corresponding Author :||Elena López
Ministerio de Ciencia e Innovacion
Centro de Investigacion i+12
Hospital Universitario 12 de Octubre, Madrid, Spain
E-mail: [email protected]
|Received November 17, 2011; Accepted December 17, 2011; Published December 19, 2011|
|Citation: López E, Pascual JL, Sequí J (2011) Important Clues of Current Phosphoproteomic Approaches for Clinical Research. J Clin Cell Immunol S5:003. doi:10.4172/2155-9899.S5-003|
|Copyright: © 2011 López E, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.|
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Mass Spectrometry-based phosphoproteomics tools are critical to understand the structure and dynamics of signalling that engages and migrates through the entire proteome. Approaches such as affinity purification followed by Mass Spectrometry (MS) have been used to elucidate relevant biological questions in health and disease. Thousands of proteins interact via physical and chemical association. Certain proteins can covalently modify other proteins post-translationally. These post-translational modifications (PTMs) ultimately give rise to the emergent functions of cells in sequence, space and time.
Understanding the functions of phosphorylated proteins thus requires one to study proteomes as linked-systems rather than collections of individual protein molecules.
The interacting proteome or protein-network knowledge has recently received much attention, as networksystems (signalling pathways) are effective snapshots in time of the proteome as a whole. MS approaches are clearly essential, in spite of the difficulties of some low abundance proteins (e.g some kinases).