ADAMTS13 bound to endothelial cells exhibits enhanced cleavage of von Willebrand factor

Anthony N. Vomund, Elaine M. Majerus

Research output: Contribution to journalArticle

24 Scopus citations

Abstract

ADAMTS13 is a plasma metalloprotease that cleaves ultra-large von Willebrand factor multimers to generate less thrombogenic fragments. Although this cleavage can occur at the surface of endothelial cells, it is currently unknown whether this process involves binding of the ADAMTS13 to the endothelial cell plasma membrane. Using different assay systems, we present evidence that ADAMTS13 binds to endothelial cells in a specific, reversible, and time-dependent manner with a Kd of 58 nM. This binding requires the COOH-terminal thrombospondin type 1 repeats of the protease. Binding is inhibited in the presence of heparin and by trypsin treatment of the cells. ADAMTS13 that was prebound to endothelial cells exhibited increased proteolysis of VWF as compared with ADAMTS13 present only in solution. These data support the notion that cleavage of VWF occurs mainly at the endothelial cell surface.

Original languageEnglish
Pages (from-to)30925-30932
Number of pages8
JournalJournal of Biological Chemistry
Volume284
Issue number45
DOIs
StatePublished - Nov 6 2009

Fingerprint Dive into the research topics of 'ADAMTS13 bound to endothelial cells exhibits enhanced cleavage of von Willebrand factor'. Together they form a unique fingerprint.

  • Cite this