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Review
. 2009 Sep;182(3):835-43.
doi: 10.1016/j.juro.2009.05.001. Epub 2009 Jul 17.

Proteomics and opportunities for clinical translation in urological disease

Affiliations
Review

Proteomics and opportunities for clinical translation in urological disease

Ali R Vaezzadeh et al. J Urol. 2009 Sep.

Abstract

Purpose: Proteomics is a rapidly growing new discipline that has the potential to increase and improve the understanding of protein function and interaction in the context of systems biology. As a translational science it has the potential to identify many new therapeutic targets as well as diagnostic and prognostic biomarkers of disease. Proteomics approaches consist of a combination of powerful technologies such as protein/peptide separation, identification and bioinformatic detection, and quantitation based on powerful computational data processing tools. We present an overview of current proteomics technologies, a review of proteomics applications in urology and a perspective on the future of proteomics in clinical medicine.

Materials and methods: A literature search was performed on the basic concepts of proteomics and technologies commonly used in this field. Advantages, challenges and limitations of current proteomics approaches are discussed, and proteomics applications in the field of urology are presented.

Results: The proteomics approaches to answer clinical questions have only recently been introduced. Many different technologies have been used in this field, which is moving from simple description to quantitative clinical applications.

Conclusions: Proteomics offers new approaches to the study of genitourinary tract diseases, and the potential to identify clinically relevant biomarkers and new therapeutic targets.

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Figures

Figure 1
Figure 1
Number of research articles published in “PubMed” during 2000–2007 with A. Proteomics in their title or as keyword and B. Number of research articles on Urinary proteomics published during 2000–2007.
Figure 2
Figure 2
Current Proteomics workflows. Samples, in form of body fluids/tissues/cells are prepared by extraction, LCM or cell culture. Highly abundant proteins can be depleted or specific PTMs can be enriched. Proteins are then separated according to their different physicochemical properties in one or several dimensions. This step is usually followed by protein identification by mass spectrometry. In the shotgun approach, proteins are first digested and then analyzed by LC-MS/MS and identified using bioinformatics tools. SELDI, protein/peptide microarrays and imaging mass spectrometry are among alternative approaches to the two previously mentioned mainstream techniques.
Figure 3
Figure 3
Characteristics and performances of commonly used mass analyzers.

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