Quantitative Proteomic Analysis of Proteins Released by Neoplastic Prostate Epithelium
Cancer Research, ISSN: 0008-5472, Vol: 64, Issue: 1, Page: 347-355
2004
- 115Citations
- 50Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations115
- Citation Indexes115
- 115
- CrossRef94
- Captures50
- Readers50
- 50
Article Description
Prostate cancer is unusual among neoplasms in that it may be diagnosed at a curable stage through detection of a protein in serum, the serine protease prostate-specific antigen (PSA). PSA is secreted by both normal and neoplastic prostate epithelial cells in response to androgenic hormones and has found widespread use in cancer screening. Because PSA screening is controversial due to sensitivity and specificity issues, efforts continue to focus on the identification and characterization of additional markers that may be used for diagnostic and therapeutic purposes. In this study, we report the application of quantitative proteomic techniques that incorporate isotope coded affinity tag reagents and tandem mass spectrometry to comprehensively identify secreted and cell surface proteins from neoplastic prostate epithelium. LNCaP cells, a prostate tumor-derived cell line that secretes PSA in response to androgen exposure, were grown in a low protein-defined media under androgen-stimulated (A+) and -starved (A-) conditions. Proteomic analysis of the media identified in excess of 600 proteins, 524 of which could be quantified. Nine percent of the proteins had A+/A- ratios > 2.0, including PSA, and 2.5% had ratios < 0.5. A subset of these androgen-regulated proteins appeared to be expressed in abundance. Of these, selected mass spectrometry observations were confirmed by Western analysis. The findings suggest that androgen-mediated release of proteins may occur through the activation of proteolytic enzymes rather than exclusively through transcriptional or translational control mechanisms. On the basis of their known functional roles, several of the abundant androgen-regulated proteins may participate in the progression of neoplastic epithelial cell growth and should be considered as potential serum markers of neoplastic prostate diseases.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=1642535545&origin=inward; http://dx.doi.org/10.1158/0008-5472.can-03-2062; http://www.ncbi.nlm.nih.gov/pubmed/14729644; http://cancerres.aacrjournals.org/lookup/doi/10.1158/0008-5472.CAN-03-2062; https://syndication.highwire.org/content/doi/10.1158/0008-5472.CAN-03-2062; https://aacrjournals.org/cancerres/article/64/1/347/511264/Quantitative-Proteomic-Analysis-of-Proteins; https://dx.doi.org/10.1158/0008-5472.can-03-2062; https://cancerres.aacrjournals.org/content/64/1/347
American Association for Cancer Research (AACR)
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