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Science 23 May 1986:
Vol. 232. no. 4753, pp. 995 - 998
DOI: 10.1126/science.3486471
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Articles

Science, Vol 232, Issue 4753, 995-998
Copyright © 1986 by American Association for the Advancement of Science

articles

Propolypeptide of von Willebrand factor circulates in blood and is identical to von Willebrand antigen II

PJ Fay, Y Kawai, DD Wagner, D Ginsburg, D Bonthron, BM Ohlsson-Wilhelm, SI Chavin, GN Abraham, RI Handin, SH Orkin, and al. et

The generally mild bleeding disorder of von Willebrand disease is associated with abnormalities of two distinct plasma proteins, the large multimeric von Willebrand factor (vWF), which mediates platelet adhesion, and von Willebrand antigen II (vW AgII), which is of unknown function. The two proteins were found to have a common biosynthetic origin in endothelial cells and megakaryocytes, which explains their simultaneous absence in the severe form of this hereditary disease. Shared amino acid sequences from a 100-kilodalton plasma glycoprotein and from vW AgII are identical to amino acid sequences predicted from a complementary DNA clone encoding the 5' end of vWF. In addition, these proteins have identical molecular weights and immunologic cross reactivities. Monoclonal antibodies prepared against both proteins recognize epitopes on the pro-vWF subunit and on a 100-kilodalton protein that are not present on the mature vWF subunit in endothelial cell lysates. In contrast, polyclonal antibodies against vWF recognize both pro-vWF and vWF subunits. Thus, the 100-kilodalton plasma glycoprotein and vW AgII are identical proteins and represent an extremely large propolypeptide that is first cleaved from pro-vWF during intracellular processing and then released into plasma.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Differential Kinetics of Cell Surface Loss of von Willebrand Factor and Its Propolypeptide after Secretion from Weibel-Palade Bodies in Living Human Endothelial Cells.
M. J. Hannah, P. Skehel, M. Erent, L. Knipe, D. Ogden, and T. Carter (2005)
J. Biol. Chem. 280, 22827-22830
   Abstract »    Full Text »    PDF »
Evidence for Extracellular Processing of Pro-von Willebrand Factor After Infusion in Animals With and Without Severe von Willebrand Disease.
P.L. Turecek, L. Pichler, W. Auer, G. Eder, K. Varadi, A. Mitterer, W. Mundt, U. Schlokat, F. Dorner, L.O. Drouet, et al. (1999)
Blood 94, 1637-1647
   Abstract »    Full Text »    PDF »
von Willebrand Factor Propeptide in Vascular Disorders: A Tool to Distinguish Between Acute and Chronic Endothelial Cell Perturbation.
J. A. van Mourik, R. Boertjes, I. A. Huisveld, K. Fijnvandraat, D. Pajkrt, P. J.J. van Genderen, and R. Fijnheer (1999)
Blood 94, 179-185
   Abstract »    Full Text »    PDF »
Propolypeptide of von Willebrand Factor Is a Novel Ligand for Very Late Antigen-4 Integrin.
T. Isobe, T. Hisaoka, A. Shimizu, M. Okuno, S. Aimoto, Y. Takada, Y. Saito, and J. Takagi (1997)
J. Biol. Chem. 272, 8447-8453
   Abstract »    Full Text »    PDF »
Cloning of cDNA and Genomic DNA for Human von Willebrand Factor.
J.E. Sadler, B.B. Shelton-Inloes, J.M. Sorace, and K. Titani (1986)
Cold Spring Harb Symp Quant Biol 51, 515-523
   Abstract »    PDF »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)