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Topology and order of formation of interchain disulfide bonds in von
Willebrand factor
DD Wagner, SO Lawrence, BM Ohlsson-Wilhelm, PJ Fay and VJ Marder
Interchain disulfide bonds between the subunits in von Willebrand factor
(vWf) dimers and in vWf multimers have been studied using some unique
features of the cultured human umbilical vein endothelial cell system.
Ammonium chloride inhibition of multimerization of vWf allowed selective
examination of vWf dimeric molecules, and monoclonal antibody against the
vWf propolypeptide was used to separate pro-vWf dimers from mature dimers.
After cleavage of dimers and multimers with Staphylococcus aureus V-8
protease, the location of interchain disulfide bonds in amino (N)-terminal
or carboxyl (C)-terminal fragments was determined by gel electrophoresis
under reduced and nonreduced conditions. The first interchain disulfide
bonds formed during dimerization are in the C-terminal region of the
subunits, whereas interdimer disulfide bonds are located in the N-terminal
portion. These data confirm recent electron microscopic projections of
disulfide bond locations and provide support to the hypothetical role of
the propolypeptide in the multimerization process.
Volume 69,
Issue 1,
pp. 27-32,
01/01/1987
Copyright © 1987 by The American Society of Hematology
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