Abstract:Clearance of coagulation factor VIII (fVIII) is mediated by a hepatic receptor low-density lipoprotein receptor-related protein (LRP), a member of low-density lipoprotein receptor (LDLR) family. It has been recently discovered that LDLR acts in concert with LRP in regulating fVIII level. FVIII has the domain structure A1-A2-B-A3-C1-C2, and to identify the portions providing the interaction with LDLR, in surface plasmon resonance-based assay we studied the binding of fVIII and its fragments to immobilized recom… Show more
“…In vivo , FVIII circulates in a tight complex with VWF, which protects FVIII from premature clearance [5–7]. The protective effect of VWF can be understood by the finding that VWF competes for interaction of LRP to the FVIII light chain [14,40]. Thus, none of the LRP‐binding regions may be accessible when non‐activated FVIII circulates in plasma.…”
To cite this article: Bovenschen N, van Stempvoort G, Voorberg J, Mertens K, Meijer AB. Proteolytic cleavage of factor VIII heavy chain is required to expose the binding-site for low-density lipoprotein receptor-related protein within the A2 domain.
“…In vivo , FVIII circulates in a tight complex with VWF, which protects FVIII from premature clearance [5–7]. The protective effect of VWF can be understood by the finding that VWF competes for interaction of LRP to the FVIII light chain [14,40]. Thus, none of the LRP‐binding regions may be accessible when non‐activated FVIII circulates in plasma.…”
To cite this article: Bovenschen N, van Stempvoort G, Voorberg J, Mertens K, Meijer AB. Proteolytic cleavage of factor VIII heavy chain is required to expose the binding-site for low-density lipoprotein receptor-related protein within the A2 domain.
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