Research Article

Phage display selection of peptides that affect prostate carcinoma cells attachment and invasion

  1. Victor I. Romanov1,*,
  2. David B. Durand2,
  3. Valery A. Petrenko3

Article first published online: 1 JUN 2001

DOI: 10.1002/pros.1068

Issue

The Prostate

The Prostate

Volume 47, Issue 4, pages 239–251, 1 June 2001

Additional Information

How to Cite

Romanov, V. I., Durand, D. B. and Petrenko, V. A. (2001), Phage display selection of peptides that affect prostate carcinoma cells attachment and invasion. The Prostate, 47: 239–251. doi: 10.1002/pros.1068

Author Information

  1. 1

    Department of Medicine; State University of New York at Stony Brook, Stony Brook, New York 11794

  2. 2

    Department of Pathology, State University of New York at Stony Brook, Stony Brook, New York 11794

  3. 3

    Department of Pathobiology, College of Veterinary Medicine, Auburn University, Alabama, 36849–5519

*SUNY at Stony Brook, Department of Medicine, HSC T15, Rm 020, Stony Brook, NY 11794–8152.

Publication History

  1. Issue published online: 1 JUN 2001
  2. Article first published online: 1 JUN 2001
  3. Manuscript Accepted: 5 FEB 2001
  4. Manuscript Received: 27 OCT 2000

Funded by

  • CaPCURE

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Keywords:

  • phage display;
  • peptide ligands;
  • metastasis

Abstract

BACKGROUND

Prostate cancer-specific proteins must be identified to serve as diagnostic and prognostic markers. Cell surface proteins are especially important, because they have potential utility as diagnostic markers and therapeutic targets. Identification of ligands for these proteins will allow use of these ligands as diagnostic and therapeutic tools and permit the investigation of receptor function. We performed a search for peptide ligands to prostate cancer cell-specific receptors.

METHODS

Peptide phage display library was used to isolate specific ligands to LNCaP prostate carcinoma cells receptors. Selected phage and cognate peptides were investigated for their cancer-related functions, such as the ability to interfere with cell adhesion, spreading, motility, and invasion.

RESULTS

Phage designated pg35, blocked spreading of LNCaP cells and their derivatives C4–2 and C4–2b. Cognate peptide did not inhibit spreading, but incubation of C4–2 and C4–2b cells with cognate peptide increased their affinity for endothelial cells and invasiveness. In addition, the peptide activates matrix metalloproteinase (MMP)-2 and 9 in C4–2 and C4–2b cells.

CONCLUSIONS

These results indicate that identified ligands may play a role in tumorigenicity and metastatic transformation of prostate cancer. To our knowledge, this is the first identification of a functional cancer-specific peptide ligand using the phage display approach. Prostate 47:239–251, 2001. © 2001 Wiley-Liss, Inc.

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