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Multimeric composition of endothelial cell-derived von Willebrand factor
HM Tsai, RL Nagel, VB Hatcher and II Sussman
Division of Hematology, Montefiore Medical Center, Bronx, NY 10467.
The multimeric composition of human endothelial cell (EC)-derived von
Willebrand factor (vWF) was studied using SDS-agarose gel electrophoresis
and autoradiography. Two multimers were found in lysates prepared from
confluent cultures of human umbilical vein endothelial cells. The smaller
multimer had a molecular weight (mol wt) of approximately 950 Kd, while the
second was larger than those seen in plasma. When electrophoresis was
performed using the discontinuous buffer system of Ruggeri and Zimmerman,
the small multimer consisted of a single band migrating with the
slowest-moving component of the corresponding plasma triplet. The large
EC-vWF multimer was detected in culture media conditioned with EC
monolayers for ten minutes. It remained the only multimer in media
conditioned for up to three days. Calcium ionophore A23187 increased the
amount of the large vWF multimer released into the culture media, but did
not change its multimeric composition. The small multimer was never
detected in the EC- conditioned media. These findings suggest that (1) a
large, fully polymerized multimer of vWF is released from the ECs, while
the small multimer probably represents a major intermediate component in
the process of multimerization, and (2) plasma vWF multimers are probably
generated from the large endothelial vWF after it is released into the
circulation.
Volume 73,
Issue 8,
pp. 2074-2076,
06/01/1989
Copyright © 1989 by The American Society of Hematology
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