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Studies of Multimerin in Human Endothelial Cells
Catherine P. M. Hayward,
Elisabeth M. Cramer,
Zhili Song,
Shilun Zheng,
Roxanna Fung,
Jean-Marc Massé,
Ron H. Stead, and
Thomas J. Podor
From the Departments of Pathology and Medicine, McMaster University,
Hamilton, Ontario, Canada; the Hamilton Health Sciences Corporation,
Hamilton, Ontario, Canada; and INSERM U91, Hôpital Henri Mondor,
Créteil, France.
Multimerin is a novel, massive, soluble protein that resembles von
Willebrand factor in its repeating, homomultimeric structure. Both
proteins are expressed by megakaryocytes and endothelial cells and are
stored in the region of platelet  -granules resembling Weibel-Palade
bodies. These findings led us to study the distribution of multimerin
within human endothelial cells. Multimerin was identified in vascular
endothelium in situ. In cultured endothelial cells, multimerin was
identified within round to rod-shaped, dense-core granules, some of
which contained intragranular, longitudinally arranged tubules and
resembled Weibel-Palade bodies. However, multimerin was found primarily
in different structures than the Weibel-Palade body proteins von
Willebrand factor and P-selectin. After stimulation with secretagogues,
multimerin was observed to redistribute from intracellular structures
to the external cellular membrane, without detectable accompanied
secretion of multimerin into the culture media. In early passage
endothelial cell cultures, multimerin was associated with extensive,
fibrillary, extracellular matrix structures, in a different
distribution than fibronectin. Although multimerin and von Willebrand
factor are stored together in platelets, they are mainly found within
different structures in endothelial cells, indicating that there are
tissue-specific differences in the sorting of these soluble, multimeric
proteins.
Blood, Vol. 91 No. 4 (February 15), 1998:
pp. 1304-1317
© 1998 by The American Society of Hematology.
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