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© Institut Pasteur
Structure de macromolécules : dimère d'aquométhémoglobine de cheval. Dérivé toxique oxydé de l'hémoglobine, représentant 1 à 2% du total.
Publication : EMBO reports

A short synthetic peptide inhibits signal transduction, migration and angiogenesis mediated by Tie2 receptor

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in EMBO reports - 20 Feb 2004

Tournaire R, Simon MP, le Noble F, Eichmann A, England P, Pouysségur J

Link to Pubmed [PMID] – 14978510

EMBO Rep. 2004 Mar;5(3):262-7

Tie2, an endothelial cell-specific receptor kinase, has an important role in tumour angiogenesis. In an attempt to identify peptides that specifically interact with and block the Tie2 pathway, a phage-displayed peptide library was screened on a recombinant Tie2 receptor. One peptide, NLLMAAS, completely abolished the binding to Tie2 of both angiopoietin 2 and angiopoietin 1 (Ang1). We further show that NLLMAAS specifically suppresses both Ang1-induced ERK activity and migration in human umbilical endothelial cells. Moreover, in vivo, this peptide inhibits angiogenesis in the chick chorioallantoic membrane assay. NLLMAAS is the first peptide described to interact with Tie2. Our results demonstrate that it is an efficient and specific antagonist of the binding of Tie2 ligands, and suggest that this peptide or its derivates may have potential applications in the treatment of angiogenesis diseases. It also represents a potent tool to dissect the molecular mechanisms involved in the Tie2 pathway.

http://www.ncbi.nlm.nih.gov/pubmed/14978510