%0 Journal Article %T Mapping and Identification of the Urine Proteome of Prostate Cancer Patients by 2D PAGE/MS %A Sanja Kiprijanovska %A Sotir Stavridis %A Oliver Stankov %A Selim Komina %A Gordana Petrusevska %A Momir Polenakovic %A Katarina Davalieva %J International Journal of Proteomics %D 2014 %I Hindawi Publishing Corporation %R 10.1155/2014/594761 %X Proteome analysis of the urine has shown that urine contains disease-specific information for a variety of urogenital system disorders, including prostate cancer (PCa). The aim of this study was to determine the protein components of urine from PCa patients. Urine from 8 patients with clinically and histologically confirmed PCa was analyzed by conventional 2D PAGE. The MS identification of the most prominent 125 spots from the urine map revealed 45 distinct proteins. According to Gene Ontology, the identified proteins are involved in a variety of biological processes, majority of them are secreted (71%), and half of them are enzymes or transporters. Comparison with the normal urine proteome revealed 11 proteins distinctive for PCa. Using Ingenuity Pathways Analysis, we have found 3 proteins (E3 ubiquitin-protein ligase rififylin, tumor protein D52, and thymidine phosphorylase) associated with cellular growth and proliferation ( ). The top network of functional associations between 11 proteins was Cell Death and Survival, Cell-To-Cell Signaling and Interaction, and System Development and Function . In summary, we have created an initial proteomic map of PCa patient¡¯s urine. The results from this study provide some leads to understand the molecular bases of prostate cancer. 1. Introduction Urine has become one of the most attractive biofluids in clinical proteomics because it can be obtained in large quantities, can be sampled noninvasively, and does not undergo significant proteolytic degradation compared with other biofluids [1]. The urine contains water, glucose, salt, and proteins derived from plasma or the urogenital tract. It can be viewed as modified ultrafiltrate of plasma combined with proteins derived from kidney and urinary tract, with protein concentration approximately 1000-fold lower than in plasma itself [2]. Even though the urinary proteome is much less complex than the plasma proteome, it contains high number of proteins. The urinary proteome has been studied by almost any proteomics technology. The first proteomic profiling of the normal urine was performed in 1979 using two-dimensional electrophoresis (2D) [3]. Afterwards, 2D, liquid chromatography (LC) and capillary electrophoresis (CE), all of them coupled to mass spectrometry (MS), have been used extensively in the proteomics definition of the urine. With the advent of the high throughput proteomics platforms consisting of 1D SDS-PAGE or LC coupled with high resolution mass spectrometers such as LTQ-FT and LTQ-Orbitrap, the number of detected proteins in healthy urine reached from %U http://www.hindawi.com/journals/ijpro/2014/594761/