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Cloning, expression and functional characterization of the full-length murine ADAMTS13
Bruno, K.; Völkel, D.; Plaimauer, B.; Antoine, G.; Pable, S.; Motto, D. G.; Lemmerhirt, H. L.; Dorner, F.; Zimmermann, K.; Scheiflinger, F.
2005-05
Citation:BRUNO, K.; VÖLKEL, D.; PLAIMAUER, B.; ANTOINE, G.; PABLE, S.; MOTTO, D. G.; LEMMERHIRT, H. L.; DORNER, F.; ZIMMERMANN, K.; SCHEIFLINGER, F. (2005). "Cloning, expression and functional characterization of the full-length murine ADAMTS13 ." Journal of Thrombosis and Haemostasis 3(5): 1064-1073. <http://hdl.handle.net/2027.42/73592>
Abstract: Functional deficiency or absence of the human von Willebrand factor (VWF)-cleaving protease (VWF-cp), recently termed ADAMTS13, has been shown to cause acquired and congenital thrombotic thrombocytopenic purpura (TTP), respectively. As a first step towards developing a small animal model of TTP, we have cloned the complete (non-truncated) murine Adamts13 gene from BALB/c mice liver poly A + mRNA. Murine ADAMTS13 is a 1426-amino-acid protein with a high homology and similar structural organization to the human ortholog. Transient expression of the murine Adamts13 cDNA in HEK 293 cells yielded a protein with a molecular weight of approximately 180 kDa which degraded recombinant murine VWF (rVWF) in a dose-dependent manner. The cleavage products of murine rVWF had the expected size of 140 and 170 kDa. Murine ADAMTS13 was inhibited by EDTA and the plasma from a TTP patient.
