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

J H Rand; N D Patel; E Schwartz; S L Zhou; B J Potter

doi:10.1172/JCI115285

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

Find articles by Rand, J. in: PubMed | Google Scholar

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

Find articles by Patel, N. in: PubMed | Google Scholar

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

Find articles by Schwartz, E. in: PubMed | Google Scholar

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

Find articles by Zhou, S. in: PubMed | Google Scholar

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

Find articles by Potter, B. in: PubMed | Google Scholar

Published in Volume 88, Issue 1 on July 1, 1991
J Clin Invest. 1991;88(1):253–259. https://doi.org/10.1172/JCI115285.
© 1991 The American Society for Clinical Investigation

Published July 1, 1991 - Version history

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.

Images.