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Clinical Chemistry 53: 429-437, 2007. First published January 26, 2007; 10.1373/clinchem.2006.077370
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Right arrow Proteomics and Protein Markers
(Clinical Chemistry. 2007;53:429-437.)
© 2007 American Association for Clinical Chemistry, Inc.

Proteomics and Protein Markers

Discovery of Candidate Tumor Markers for Prostate Cancer via Proteomic Analysis of Cell Culture–Conditioned Medium

Girish Sardana1,2,3, John Marshall4 and Eleftherios P. Diamandis1,2,3,a

1 Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, Canada.
2 Department of Pathology and Laboratory Medicine, Mount Sinai Hospital, Toronto, ON, Canada.
3 Department of Clinical Biochemistry, University Health Network and Toronto Medical Laboratories, Toronto, ON, Canada.
4 Department of Chemistry and Biology, Ryerson University, Toronto, ON, Canada.

aAddress correspondence to this author at: Department of Pathology and Laboratory Medicine, Mount Sinai Hospital, 600 University Avenue, Toronto, Ontario, M5G 1X5, Canada. Fax 416-586-8628; e-mail ediamandis{at}mtsinai.on.ca.

Objective: Prostate-specific antigen measurement, widely used for early detection of prostate cancer (CaP), suffers from low specificity. Additional tumor markers are needed for the early detection of clinically relevant CaP. Our objective was to perform a qualitative proteomic analysis of conditioned medium (CM) from the CaP cell line PC3(AR)6.

Methods: We used a roller bottle culture system to culture the PC3(AR)6 cell line in chemically defined serum-free medium for 14 days. By using strong anion-exchange chromatography, we fractionated the CM and trypsinized the fractions. The tryptic peptides were further fractionated by reversed-phase C-18 chromatography before being subjected to electrospray ionization tandem mass spectrometry. We used MASCOT software to search the mass spectra generated and organized identified proteins based on their genome ontology classification of cellular location. We used an immunoassay to measure a newly identified secreted protein, Mac-2BP, and kallikreins 5, 6, and 11 in serum samples from CaP patients and healthy men.

Results: We classified 262 proteins according to cellular location; the sample was found to contain a significant proportion of secreted (23%) and membrane (16%) proteins. In a proportion of cancer patients compared with healthy men, we determined by ELISA that serum concentrations of a novel candidate biomarker Mac-2BP were increased.

Conclusions: These identified proteins, and possibly many others found in the CM, may have utility as novel CaP biomarkers.




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V. Kulasingam and E. P. Diamandis
Proteomics Analysis of Conditioned Media from Three Breast Cancer Cell Lines: A Mine for Biomarkers and Therapeutic Targets
Mol. Cell. Proteomics, November 1, 2007; 6(11): 1997 - 2011.
[Abstract] [Full Text] [PDF]


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