Binding of the NG2 Proteoglycan to Kringle Domains Modulates the Functional Properties of Angiostatin and Plasmin(ogen)

Interactions of the developmentally regulated chondroitin sulfate proteoglycan NG2 with human plasminogen and kringle domain-containing plasminogen fragments have been analyzed by solid-phase immunoassays and by surface plasmon resonance. In immunoassays, the core protein of NG2 binds specifically a...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	The Journal of biological chemistry 2000-09, Vol.275 (37), p.28625-28633
Hauptverfasser:	Goretzki, L, Lombardo, C R, Stallcup, W B
Format:	Artikel
Sprache:	eng
Schlagworte:	Angiostatins Animals Antigens - metabolism Antigens - pharmacology Cell Division - drug effects Cells, Cultured Endothelium, Vascular - cytology Endothelium, Vascular - drug effects Humans Kringles Mice Mice, Inbred BALB C Peptide Fragments - physiology Plasminogen - physiology Proteoglycans - metabolism Proteoglycans - pharmacology Rabbits Urokinase-Type Plasminogen Activator - physiology
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!