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150-kD von Willebrand factor binding protein extracted from human vascular subendothelium is type VI collagen

J H Rand1, N D Patel, E Schwartz

  • 1Department of Medicine, Mount Sinai School of Medicine, New York, New York 10029.

The Journal of Clinical Investigation
|July 1, 1991
PubMed

Insights

Von Willebrand factor (vWF) binds to vascular subendothelium. Researchers identified type VI collagen as the binding site for vWF, revealing its role in platelet adhesion to blood vessels.

Area of Science:

  • Biochemistry
  • Vascular Biology
  • Hematology

Background:

  • Von Willebrand factor (vWF) is crucial for platelet adhesion to injured blood vessels.
  • vWF is known to be present within the vascular subendothelium.

Purpose of the Study:

  • To identify the specific binding site(s) for vWF within the vascular subendothelium.
  • To elucidate the molecular interactions governing vWF's role in hemostasis.

Main Methods:

  • Investigated vWF binding to various subendothelial components.
  • Solubilized and characterized a 150-kD protein from the subendothelium that binds vWF.
  • Analyzed amino acid composition, antibody recognition, and isoelectric point of the binding protein.
  • Tested binding of purified type VI collagen to vWF.

Main Results:

  • A 150-kD protein was isolated from the subendothelium that demonstrated vWF binding.
  • This protein exhibited characteristics consistent with type VI collagen.
  • Purified type VI collagen was confirmed to bind vWF.

Conclusions:

  • The 150-kD protein binding vWF in the subendothelium is identified as type VI collagen.
  • Type VI collagen is a significant binding site for vWF in the vascular subendothelium.
  • This interaction likely plays a key role in platelet adhesion in vivo.

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