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Epitope mapping of the von Willebrand factor subunit distinguishes fragments present in normal and type IIA von Willebrand disease from those generated by plasmin

Academic Article
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Overview

authors

  • Berkowitz, S. D.
  • Dent, J.
  • Roberts, J.
  • Fujimura, Y.
  • Plow, E. F.
  • Titani, K.
  • Ruggeri, Zaverio
  • Zimmerman, T. S.

publication date

  • February 1987

journal

  • Journal of Clinical Investigation  Journal

abstract

  • A small but consistent proportion of the von Willebrand factor (vWF) in normal plasma is composed of 189, 176, and 140 kD fragments cleaved from the 225 kD subunit. A monoclonal antibody map of vWF, based on the reactivity of individual antibodies with cyanogen bromide and tryptic fragments of known carboxy and/or amino termini, showed that in normal and IIA von Willebrand disease (vWD) plasmas the 140 kD fragment was derived from the amino-terminal region, whereas the 176 kD fragment was derived from the carboxy-terminal region of the subunit. In type IIA vWD, however, the fragments comprised a greater proportion of circulating vWF. In contrast, plasmin cleaved a 176 kD fragment from the amino terminus and a 145 kD fragment from the carboxy terminus of the subunit. Species similar to these plasmin-cleaved fragments were demonstrated in plasmas from four patients treated with fibrinolytic agents, but not in IIA vWD.

subject areas

  • Antibodies, Monoclonal
  • Epitopes
  • Fibrinolysin
  • Humans
  • Macromolecular Substances
  • Molecular Weight
  • Peptide Fragments
  • von Willebrand Diseases
  • von Willebrand Factor
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Identity

PubMed Central ID

  • PMC424117

International Standard Serial Number (ISSN)

  • 0021-9738

Digital Object Identifier (DOI)

  • 10.1172/jci112843

PubMed ID

  • 2433308
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Additional Document Info

start page

  • 524

end page

  • 531

volume

  • 79

issue

  • 2

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