Original Article

Identification of secreted glycoproteins of human prostate and bladder stromal cells by comparative quantitative proteomics

  1. Young Ah Goo1,2,3,*,
  2. Alvin Y. Liu1,3,4,
  3. Soyoung Ryu2,
  4. Scott A. Shaffer2,
  5. Lars Malmström2,
  6. Laura Page1,4,
  7. Liem T. Nguyen2,
  8. Catalin E. Doneanu5,
  9. David R. Goodlett2,3,*

Article first published online: 15 SEP 2008

DOI: 10.1002/pros.20853

Issue

The Prostate

The Prostate

Volume 69, Issue 1, pages 49–61, 1 January 2009

Additional Information

How to Cite

Goo, Y. A., Liu, A. Y., Ryu, S., Shaffer, S. A., Malmström, L., Page, L., Nguyen, L. T., Doneanu, C. E. and Goodlett, D. R. (2009), Identification of secreted glycoproteins of human prostate and bladder stromal cells by comparative quantitative proteomics. The Prostate, 69: 49–61. doi: 10.1002/pros.20853

Author Information

  1. 1

    Department of Urology, University of Washington, Seattle, Washington

  2. 2

    Department of Medicinal Chemistry, University of Washington, Seattle, Washington

  3. 3

    Institute for Systems Biology, Seattle, Washington

  4. 4

    Institute for Stem Cell and Regenerative Medicine, University of Washington, Seattle, Washington

  5. 5

    Waters Corporation, Milford, Massachusetts

*Department of Medicinal Chemistry, University of Washington, Box 357610, Seattle, WA 98195-7610.

Publication History

  1. Issue published online: 21 NOV 2008
  2. Article first published online: 15 SEP 2008
  3. Manuscript Accepted: 12 AUG 2008
  4. Manuscript Received: 30 MAY 2008

Funded by

  • Department of Army Grant. Grant Number: W81XWH-06-1-0108
  • National Institutes of Health. Grant Numbers: CA101052, DK63630, CA111244
  • UW Ecogenetics and Environmental Health. Grant Number: NIEHS P30ES07033
  • NW RCE for Biodefense and Emerging Infectious Diseases. Grant Number: 1U54 AI57141

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Keywords:

  • bladder;
  • prostate;
  • stromal cells;
  • secreted proteins

Abstract

BACKGROUND

Functional development of the prostate is governed by stromal mesenchyme induction and epithelial response. Stromal/epithelial signaling can be mediated through direct cell–cell contact and diffusible factors and their cell surface receptors. These inducers are likely secreted or membrane-associated extracellular proteins. Given the importance of intercellular communication, it is possible that diseases like cancer could arise from a loss of this communication. One approach to gain a molecular understanding of stromal cells is to identify, as a first step, secreted stromal signaling factors. We proposed to do this by comparative analysis between bladder and prostate.

METHODS

Secreted proteins were identified from cultured normal prostate and bladder stromal mesenchyme cells by glycopeptide-capture method followed by mass spectrometry. Differences in protein abundance between prostate and bladder were quantified from calculated peptide ion current area (PICA) followed by Western validation. Functional and pathway analyses of the proteins were carried out by Gene Ontology (GO) and Teranode software.

RESULTS

This analysis produced a list of 116 prostate and 84 bladder secreted glycoproteins with ProteinProphet probability scores ≥0.9. Stromal proteins upregulated in the prostate include cathepsin L, follistatin-related protein, neuroendocrine convertase, tumor necrosis factor receptor, and others that are known to be involved in signal transduction, extracellular matrix interaction, differentiation and transport.

CONCLUSIONS

We have identified a number of potential proteins for stromal signaling and bladder or prostate differentiation program. The prostate stromal/epithelial signaling may be accomplished through activation of the ECM–receptor interaction, complement and coagulation cascades, focal adhesion and cell adhesion pathways. Prostate 69: 49–61, 2009. © 2008 Wiley–Liss, Inc.

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