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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 383, Issue 1

Issues

Random Peptide Bacteriophage Display as a Probe for Urokinase Receptor Ligands

Susan Fong / Michael V. Doyle / Robert J. Goodson / Robert J. Drummond / Jennifer R. Stratton / Lisa McGuire / Laura V. Doyle / Harold A. Chapman / Steven Rosenberg
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2002.015

Abstract

The urokinase receptor is a multifunctional protein that plays a central role in cell surface plasminogen activation, cell migration, and cell adhesion. We previously demonstrated that high affinity peptide ligands for the urokinase receptor, which are urokinase competitors, can be obtained from a 15mer peptide library (Goodson et al., 1994). In order to probe for additional urokinase receptor binding sites we affinity selected the same bacteriophage library on complexes of soluble urokinase receptor (suPAR) and the receptor binding domain of urokinase, residues 1 48 (uPA1 48). Bacteriophage were isolated which bound to suPAR and suPAR:uPA1 48 complexes with high yield. The peptide sequences encoded by these bacteriophage were distinct from those obtained previously on urokinase receptor expressing cells, and comprise two groups based upon effects on su PAR:1-anilino-8-napthalene sulfonate (ANS) fluorescence, and vitronectin binding competition. Alanine scanning mutagensis of the soluble peptides was used to define minimal regions and key residues for suPAR binding by competition with the parent bacteriophage. A comparison of these results with sequences of domains of both vitronectin and integrin αchains, which have been reported to be important for urokinase receptor binding, suggests that the homology with the peptide sequences selected is functionally significant.

About the article

Published Online: 2005-06-01

Published in Print: 2002-01-23


Citation Information: Biological Chemistry, Volume 383, Issue 1, Pages 149–158, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2002.015.

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[1]
J. Krol, S. Sato, P. Rettenberger, I. Assfalg-Machleidt, M. Schmitt, V. Magdolen, and U. Magdolen
Biological Chemistry, 2003, Volume 384, Number 7

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