150-kD von Willebrand factor binding protein extracted from human vascular subendothelium is type VI collagen. Academic Article uri icon

Overview

abstract

  • We have previously shown that von Willebrand factor (vWF), a glycoprotein which plays a critical role in the adhesion of platelets to injured blood vessels, is present within vascular subendothelium. We investigated the identity of the subendothelial binding site(s) for vWF by examining vWF binding to subendothelial constituents and solubilized a 150-kD protein with SDS-urea that bound vWF. This protein had an amino-acid composition similar to that of the type VI collagen alpha-1/alpha-2 chains, was recognized by specific polyclonal antibodies against type VI collagen, and had a similar acidic isoelectric point. Furthermore, we found that purified type VI collagen also bound vWF. Thus, we have identified the extracted 150-kD protein as type VI collagen. This protein may play a significant role in the binding of vWF to vascular subendothelium in vivo.

publication date

  • July 1, 1991

Research

keywords

  • Carrier Proteins
  • Collagen
  • Endothelium, Vascular
  • von Willebrand Factor

Identity

PubMed Central ID

  • PMC296027

Scopus Document Identifier

  • 0025770612

Digital Object Identifier (DOI)

  • 10.1172/JCI115285

PubMed ID

  • 2056120

Additional Document Info

volume

  • 88

issue

  • 1