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Sulfation of von Willebrand factor
JA Carew, PJ Browning and DC Lynch
Department of Medicine, Harvard Medical School, Boston, MA.
von Willebrand factor (vWF) is a multimeric adhesive glycoprotein essential
for normal hemostasis. We have discovered that cultured human umbilical
vein endothelial cells incorporate inorganic sulfate into vWF. Following
immunoisolation and analysis by polyacrylamide or agarose gel
electrophoresis, metabolically labeled vWF was found to have incorporated
[35S]-sulfate into all secreted multimer species. The time course of
incorporation shows that sulfation occurs late in the biosynthesis of vWF,
near the point at which multimerization occurs. Quantitative analysis
suggests the presence, on average, of one molecule of sulfate per mature
vWF subunit. Virtually all the detectable sulfate is released from the
mature vWF subunit by treatment with endoglycosidases that remove
asparagine-linked carbohydrates. Sulfated carbohydrate was localized first
to the N-terminal half of the mature subunit (amino acids 1 through 1,365)
by partial proteolytic digestion with protease V8; and subsequently to a
smaller fragment within this region (amino acids 273 through 511) by
sequential digestions with protease V8 and trypsin. Thus, the carbohydrate
at asparagine 384 and/or 468 appears to be the site of sulfate
modification. Sodium chlorate, an inhibitor of adenosine triphosphate-
sulfurylase, blocks sulfation of vWF without affecting either the ability
of vWF to assemble into high molecular weight multimers or the ability of
vWF multimers to enter Weible-Palade bodies. The stability of vWF multimers
in the presence of an endothelial cell monolayer also was unaffected by the
sulfation state. Additionally, we have found that the cleaved propeptide of
vWF is sulfated on asparagine-linked carbohydrate.
Volume 76,
Issue 12,
pp. 2530-2539,
12/15/1990
Copyright © 1990 by The American Society of Hematology
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