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Sulfation of tyrosine residues in coagulation factor V
GL Hortin
Edward Mallinckrodt Department of Pediatrics, Washington University School
of Medicine, St Louis, MO 63110.
Sulfation of human coagulation factor V was investigated by
biosynthetically labeling the products of HepG2 cells with [35S]sulfate.
There was abundant incorporation of the sulfate label into a product
identified as factor V by immunoprecipitation, lability to proteases,
affinity for the lectin jacalin, and sodium dodecyl sulfate-polyacrylamide
gel electrophoresis. Two or more sites in factor V incorporated sulfate as
indicated by labeling of different peptide chains of factor Va. The 150-Kd
activation fragment of factor Va incorporated the greatest amounts of
sulfate. This fragment of factor Va was bound selectively by
jacalin-agarose, reflecting its content of O-linked oligosaccharides.
Analysis of an alkaline hydrolysate of sulfate-labeled factor Va by
anion-exchange chromatography showed that the sulfate occurred partly in
tyrosine sulfate residues and partly in alkaline-labile linkages. Sulfate
groups are potentially important structural and functional elements in
factor V, and labeling with [35S]sulfate provides a useful approach for
examining the biosynthesis and processing of this protein. The hypothesis
is advanced that sites of sulfation in factor V and several other plasma
proteins contribute to the affinity and specificity of thrombin for these
molecules, just as it does for the interaction of thrombin with the potent
inhibitor hirudin from leeches.
Volume 76,
Issue 5,
pp. 946-952,
09/01/1990
Copyright © 1990 by The American Society of Hematology
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