An urokinase receptor antagonist that inhibits cell migration by blocking the formyl peptide receptor

Katia Bifulco, Immacolata Longanesi-Cattani, Lucia Gargiulo, Ornella Maglio, Mauro Cataldi, Mario De Rosa, Maria Patrizia Stoppelli, Vincenzo Pavone, Maria Vincenza Carriero

Research output: Contribution to journalArticlepeer-review

Abstract

Urokinase receptor (uPAR) plays a key role in physiological and pathological processes sustained by an altered cell migration. We have developed peptides carrying amino acid substitutions along the Ser88-Arg-Ser-Arg-Tyr92 (SRSRY) uPAR chemotactic sequence. The peptide pyro glutamic acid (pGlu)-Arg-Glu-Arg-Tyr-NH2 (pERERY-NH2) shares the same binding site with SRSRY and competes with N-formyl-Met-Leu-Phe (fMLF) for binding to the G-protein-coupled N-formyl-peptide receptor (FPR). pERERY-NH2 is a dose-dependent inhibitor of both SRSRY- and fMLF-directed cell migration, and prevents agonist-induced FPR internalization and fMLF-dependent ERK1/2 phosphorylation. pERERY-NH2 is a new and potent uPAR inhibitor which may suggest the generation of new pharmacological treatments for pathological conditions involving increased cell migration.

Original languageEnglish
Pages (from-to)1141-1146
Number of pages6
JournalFEBS Letters
Volume582
Issue number7
DOIs
Publication statusPublished - Apr 2 2008

Keywords

  • Formyl-peptide receptor
  • Inhibitors of Cell Migration
  • Urokinase receptor

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Fingerprint

Dive into the research topics of 'An urokinase receptor antagonist that inhibits cell migration by blocking the formyl peptide receptor'. Together they form a unique fingerprint.

Cite this