Ananlysis of Phosphoproteins and Signalling Pathwaysby Quantitative Proteomics

Czech version

Authors: M. Pjechová ¹; L. Hernychová ¹; P. Tomašec ^1,2; G. W. Wilkinson ^1,2; B. Vojtěšek ¹
Authors‘ workplace: Regionální centrum aplikované molekulární onkologie, Masarykův onkologický ústav, Brno ¹; Department of Medical Microbiology, Institute of Infection and Immunity, School of Medicine, Cardiff University, United Kingdom ²
Published in: Klin Onkol 2014; 27(Supplementum): 116-120

Overview

Protein phosphorylation is a key regulator in cellular signaling pathways. It is involved in most cellular events in which interplay between phosphatases and kinases strictly controls biological processes, such as differentiation, proliferation and apoptosis. Altered or defective signaling pathways often result in various diseases, emphasizing the importance of studying the phosphoproteome. The abundance of phosphoproteins in the proteome is often very low, which requires specific and highly sensitive approaches. By using quantitative proteomics methods, we are able to analyze changes in abundance of proteins and their posttranslational modifications and then changes in signaling pathways. In this review, we describe quantitative proteomics methods, which could be used for study of phosphoproteins and their connection in signaling pathways.

Key words:
proteomics – phosphoproteins – signaling pathways

This work was supported by the European Regional Development Fund and the State Budget of the Czech Republic (RECAMO, CZ.1.05/2.1.00/03.0101) and by MH CZ – DRO (MMCI, 00209805).

The authors declare they have no potential conflicts of interest concerning drugs, products, or services used in the study.

The Editorial Board declares that the manuscript met the ICMJE “uniform requirements” for biomedical papers.

Submitted:
30. 1. 2014

Accepted:
14. 4. 2014

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