Identification of Differentially Expressed Proteins in Direct Expressed Prostatic Secretions of Men with Organ-confined Versus Extracapsular Prostate Cancer
Current protocols for the screening of prostate cancer cannot accurately discriminate clinically indolent tumors from more aggressive ones. One reliable indicator of outcome has been the determination of organ-confined versus nonorgan-confined disease but even this determination is often only made f...
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Published in | Molecular & cellular proteomics Vol. 11; no. 12; pp. 1870 - 1884 |
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Main Authors | , , , , , , , , , , , , , |
Format | Journal Article |
Language | English |
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United States
Elsevier Inc
01.12.2012
The American Society for Biochemistry and Molecular Biology |
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Abstract | Current protocols for the screening of prostate cancer cannot accurately discriminate clinically indolent tumors from more aggressive ones. One reliable indicator of outcome has been the determination of organ-confined versus nonorgan-confined disease but even this determination is often only made following prostatectomy. This underscores the need to explore alternate avenues to enhance outcome prediction of prostate cancer patients. Fluids that are proximal to the prostate, such as expressed prostatic secretions (EPS), are attractive sources of potential prostate cancer biomarkers as these fluids likely bathe the tumor. Direct-EPS samples from 16 individuals with extracapsular (n = 8) or organ-confined (n = 8) prostate cancer were used as a discovery cohort, and were analyzed in duplicate by a nine-step MudPIT on a LTQ-Orbitrap XL mass spectrometer. A total of 624 unique proteins were identified by at least two unique peptides with a 0.2% false discovery rate. A semiquantitative spectral counting algorithm identified 133 significantly differentially expressed proteins in the discovery cohort. Integrative data mining prioritized 14 candidates, including two known prostate cancer biomarkers: prostate-specific antigen and prostatic acid phosphatase, which were significantly elevated in the direct-EPS from the organ-confined cancer group. These and five other candidates (SFN, MME, PARK7, TIMP1, and TGM4) were verified by Western blotting in an independent set of direct-EPS from patients with biochemically recurrent disease (n = 5) versus patients with no evidence of recurrence upon follow-up (n = 10). Lastly, we performed proof-of-concept SRM-MS-based relative quantification of the five candidates using unpurified heavy isotope-labeled synthetic peptides spiked into pools of EPS-urines from men with extracapsular and organ-confined prostate tumors. This study represents the first efforts to define the direct-EPS proteome from two major subclasses of prostate cancer using shotgun proteomics and verification in EPS-urine by SRM-MS. |
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AbstractList | Current protocols for the screening of prostate cancer cannot accurately discriminate clinically indolent tumors from more aggressive ones. One reliable indicator of outcome has been the determination of organ-confined versus nonorgan-confined disease but even this determination is often only made following prostatectomy. This underscores the need to explore alternate avenues to enhance outcome prediction of prostate cancer patients. Fluids that are proximal to the prostate, such as expressed prostatic secretions (EPS), are attractive sources of potential prostate cancer biomarkers as these fluids likely bathe the tumor. Direct-EPS samples from 16 individuals with extracapsular (n = 8) or organ-confined (n = 8) prostate cancer were used as a discovery cohort, and were analyzed in duplicate by a nine-step MudPIT on a LTQ-Orbitrap XL mass spectrometer. A total of 624 unique proteins were identified by at least two unique peptides with a 0.2% false discovery rate. A semiquantitative spectral counting algorithm identified 133 significantly differentially expressed proteins in the discovery cohort. Integrative data mining prioritized 14 candidates, including two known prostate cancer biomarkers: prostate-specific antigen and prostatic acid phosphatase, which were significantly elevated in the direct-EPS from the organ-confined cancer group. These and five other candidates (SFN, MME, PARK7, TIMP1, and TGM4) were verified by Western blotting in an independent set of direct-EPS from patients with biochemically recurrent disease (n = 5) versus patients with no evidence of recurrence upon follow-up (n = 10). Lastly, we performed proof-of-concept SRM-MS-based relative quantification of the five candidates using unpurified heavy isotope-labeled synthetic peptides spiked into pools of EPS-urines from men with extracapsular and organ-confined prostate tumors. This study represents the first efforts to define the direct-EPS proteome from two major subclasses of prostate cancer using shotgun proteomics and verification in EPS-urine by SRM-MS. Current protocols for the screening of prostate cancer cannot accurately discriminate clinically indolent tumors from more aggressive ones. One reliable indicator of outcome has been the determination of organ-confined versus nonorgan-confined disease but even this determination is often only made following prostatectomy. This underscores the need to explore alternate avenues to enhance outcome prediction of prostate cancer patients. Fluids that are proximal to the prostate, such as expressed prostatic secretions (EPS), are attractive sources of potential prostate cancer biomarkers as these fluids likely bathe the tumor. Direct-EPS samples from 16 individuals with extracapsular ( n = 8) or organ-confined ( n = 8) prostate cancer were used as a discovery cohort, and were analyzed in duplicate by a nine-step MudPIT on a LTQ-Orbitrap XL mass spectrometer. A total of 624 unique proteins were identified by at least two unique peptides with a 0.2% false discovery rate. A semiquantitative spectral counting algorithm identified 133 significantly differentially expressed proteins in the discovery cohort. Integrative data mining prioritized 14 candidates, including two known prostate cancer biomarkers: prostate-specific antigen and prostatic acid phosphatase, which were significantly elevated in the direct-EPS from the organ-confined cancer group. These and five other candidates (SFN, MME, PARK7, TIMP1, and TGM4) were verified by Western blotting in an independent set of direct-EPS from patients with biochemically recurrent disease ( n = 5) versus patients with no evidence of recurrence upon follow-up ( n = 10). Lastly, we performed proof-of-concept SRM-MS-based relative quantification of the five candidates using unpurified heavy isotope-labeled synthetic peptides spiked into pools of EPS-urines from men with extracapsular and organ-confined prostate tumors. This study represents the first efforts to define the direct-EPS proteome from two major subclasses of prostate cancer using shotgun proteomics and verification in EPS-urine by SRM-MS. |
Author | Yao, Cindy Q. Gramolini, Anthony O. Boutros, Paul C. Nyalwidhe, Julius O. Kim, Yunee Drake, Richard R. Ignatchenko, Vladimir Kislinger, Thomas Lance, Raymond S. Semmes, O. John Kalatskaya, Irina Troyer, Dean A. Medin, Jeffrey A. Stein, Lincoln D. |
Author_xml | – sequence: 1 givenname: Yunee surname: Kim fullname: Kim, Yunee organization: Department of Medical Biophysics, University of Toronto, Toronto, Canada – sequence: 2 givenname: Vladimir surname: Ignatchenko fullname: Ignatchenko, Vladimir organization: Ontario Cancer Institute, University Health Network, Toronto, Canada – sequence: 3 givenname: Cindy Q. surname: Yao fullname: Yao, Cindy Q. organization: Department of Medical Biophysics, University of Toronto, Toronto, Canada – sequence: 4 givenname: Irina surname: Kalatskaya fullname: Kalatskaya, Irina organization: Informatics and Bio-computing Platform, Ontario Institute for Cancer Research, Toronto, Canada – sequence: 5 givenname: Julius O. surname: Nyalwidhe fullname: Nyalwidhe, Julius O. organization: Department of Microbiology and Molecular Cell Biology, Eastern Virginia Medical School, Norfolk, VA, USA – sequence: 6 givenname: Raymond S. surname: Lance fullname: Lance, Raymond S. organization: Leroy T. Canoles Jr., Cancer Research Center, Eastern Virginia Medical School, Norfolk, Virginia – sequence: 7 givenname: Anthony O. surname: Gramolini fullname: Gramolini, Anthony O. organization: Department of Physiology, University of Toronto, Toronto, Canada – sequence: 8 givenname: Dean A. surname: Troyer fullname: Troyer, Dean A. organization: Department of Microbiology and Molecular Cell Biology, Eastern Virginia Medical School, Norfolk, VA, USA – sequence: 9 givenname: Lincoln D. surname: Stein fullname: Stein, Lincoln D. organization: Informatics and Bio-computing Platform, Ontario Institute for Cancer Research, Toronto, Canada – sequence: 10 givenname: Paul C. surname: Boutros fullname: Boutros, Paul C. organization: Informatics and Bio-computing Platform, Ontario Institute for Cancer Research, Toronto, Canada – sequence: 11 givenname: Jeffrey A. surname: Medin fullname: Medin, Jeffrey A. organization: Department of Medical Biophysics, University of Toronto, Toronto, Canada – sequence: 12 givenname: O. John surname: Semmes fullname: Semmes, O. John organization: Department of Microbiology and Molecular Cell Biology, Eastern Virginia Medical School, Norfolk, VA, USA – sequence: 13 givenname: Richard R. surname: Drake fullname: Drake, Richard R. email: draker@musc.edu organization: Department of Microbiology and Molecular Cell Biology, Eastern Virginia Medical School, Norfolk, VA, USA – sequence: 14 givenname: Thomas surname: Kislinger fullname: Kislinger, Thomas email: Thomas.kislinger@utoronto.ca organization: Department of Medical Biophysics, University of Toronto, Toronto, Canada |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/22986220$$D View this record in MEDLINE/PubMed |
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Copyright | 2012 © 2012 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. 2012 by The American Society for Biochemistry and Molecular Biology, Inc. 2012 |
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Snippet | Current protocols for the screening of prostate cancer cannot accurately discriminate clinically indolent tumors from more aggressive ones. One reliable... |
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SubjectTerms | 14-3-3 Proteins - analysis Biomarkers, Tumor - analysis Biomarkers, Tumor - metabolism Exonucleases - analysis Exoribonucleases Gene Expression Regulation, Neoplastic Humans Intracellular Signaling Peptides and Proteins - analysis Isotope Labeling Male Oncogene Proteins - analysis Prostate - metabolism Prostate-Specific Antigen - metabolism Prostatic Neoplasms - metabolism Prostatic Secretory Proteins - analysis Prostatic Secretory Proteins - urine Protein Array Analysis Protein Deglycase DJ-1 Proteome - analysis Tissue Inhibitor of Metalloproteinase-1 - analysis Transglutaminases - analysis |
Title | Identification of Differentially Expressed Proteins in Direct Expressed Prostatic Secretions of Men with Organ-confined Versus Extracapsular Prostate Cancer |
URI | https://dx.doi.org/10.1074/mcp.M112.017889 https://www.ncbi.nlm.nih.gov/pubmed/22986220 https://search.proquest.com/docview/1222232671 https://pubmed.ncbi.nlm.nih.gov/PMC3518113 |
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