Structure and Function of the Von Willebrand Factor A1 Domain

Author(s): Kottayil I. Varughese, Reha Celikel, Zaverio M. Ruggeri.

Journal Name: Current Protein & Peptide Science

Volume 3 , Issue 3 , 2002

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Abstract:

The role of von Willebrand factor (VWF) in blocking hemorrhage is centered on its ability to act as a bridging adhesive molecule between platelets and components of the extracellular matrix or other platelets. In the course of chronic vascular diseases, moreover, the same properties of VWF may become the cause of pathological thrombus formation leading to arterial occlusion. There is convincing evidence that VWF functions involving interactions with platelets ultimately depend on binding to the membrane glycoprotein (GP) Ibα receptor mediated by the A1 domain. In this review, we present the current knowledge on the structural features of the VWF A1 domain that support its functions.

Keywords: vwf, pro-vwf, vwf a1, gp 1b

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Article Details

VOLUME: 3
ISSUE: 3
Year: 2002
Page: [301 - 312]
Pages: 12
DOI: 10.2174/1389203023380620
Price: $58