[Biology of von Willebrand factor].

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  • Author(s): Girma JP;Girma JP
  • Source:
    Nephrologie & therapeutique [Nephrol Ther] 2006 Jan; Vol. 2 Suppl 2, pp. S143-8.
  • Publication Type:
    English Abstract; Journal Article
  • Language:
    French
  • Additional Information
    • Transliterated Title:
      Biologie du facteur Willebrand.
    • Source:
      Publisher: John Libbey Eurotext Country of Publication: France NLM ID: 101248950 Publication Model: Print Cited Medium: Print ISSN: 1769-7255 (Print) Linking ISSN: 17697255 NLM ISO Abbreviation: Nephrol Ther Subsets: MEDLINE
    • Publication Information:
      Publication: 2023- : Arcueil : John Libbey Eurotext
      Original Publication: Paris : Elsevier, c2005-
    • Subject Terms:
      von Willebrand Factor/*physiology; Blood Coagulation ; Blood Platelets/physiology ; Endothelium, Vascular/physiology ; Humans ; Megakaryocytes/physiology ; Platelet Adhesiveness ; Platelet Aggregation
    • Abstract:
      Von Willebrand factor (VWF) is a multimeric glycoprotein synthesized by megakaryocytes and endothelial cells. It is stored in platelets and endothelial cells and secreted towards subendothelium and plasma. VWF multimers consist of linear arrangements of identical subunits with a molecular weight of 270 kDa. The longest multimers reach more than 20 x 10(6) Da in storage granules. In the circulation, the multimer size is limited by the specific protease ADAMTS13. In primary hemostasis, VWF plays a key role as a molecular bridge in adhesion between platelets and subendothelium and between platelets during their aggregation. These functions, which involve the interaction with platelet glycoprotein lb, are mainly enhanced by VWF immobilization onto hydrophobic surfaces (collagen, cell membrane) and by high shear rates found in microcirculation and stenosed arteries. In these functions, the higher molecular weight forms are the most efficient. Under such hemodynamic conditions, proteolytic activity of ADAMTS13 is also optimal and limits the multimer size to about 15 x 10(6) Da as soon as their secretion. Thus ADAMTS13 appears as a key physiologic regulator of the VWF platelet functions. In the microcirculation, the lack of ADAMTS13 activity can result in the formation of VWF-rich platelet aggregates responsible for thrombotic thrombocytopenic purpura.
    • Accession Number:
      0 (von Willebrand Factor)
    • Publication Date:
      Date Created: 20070322 Date Completed: 20070514 Latest Revision: 20070321
    • Publication Date:
      20240829
    • Accession Number:
      17373215