Angiostatic peptides use plasma fibronectin to home to angiogenic vasculature
AUTOR(ES)
Åkerman, Maria E.
FONTE
National Academy of Sciences
RESUMO
A group of angiogenesis inhibitors are derived from fragments of extracellular matrix or blood proteins. Endostatin, antithrombin, and anastellin are members of this group of substances. The plasma adhesion proteins fibronectin and vitronectin serve as cofactors for these three antiangiogenic proteins. Anginex is a synthetic 33-amino acid peptide that was originally modeled to reproduce the β-sheet structure of antiangiogenic proteins. Here, we show that anginex initiates fibronectin polymerization and is inactive in mice that lack plasma fibronectin. Anginex shares these characteristics with anastellin. Fluorescein-labeled anginex and anastellin specifically localized in angiogenic vessels in vivo. This localization was dependent on plasma fibronectin and inhibited by an Arg-Gly-Asp peptide. Thus, anginex shares with several physiological angiogenesis inhibitors a dependence on plasma adhesion proteins. The role of the adhesion protein interaction apparently is to form integrin-binding complexes that deliver the antiangiogenic proteins to sites of angiogenesis. This functional convergence of several antiangiogenic factors has important implications for antiangiogenic therapies.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=548558Documentos Relacionados
- Human plasma fibronectin inhibits adherence of Streptococcus pyogenes to hexadecane.
- Lung vascular injury with protease infusion. Relationship to plasma fibronectin.
- Plasma Fibronectin: Structure and Function
- Plasma fibronectin and thyroid function.
- Fibronectin peptides in cell migration and wound repair