Human Complement Factor H Is a Reductase for Large Soluble von Willebrand Factor Multimers—Brief Report | Zendy

Leticia Nolasco | Zendy; Jennifer Nolasco | Zendy; Shuju Feng | Zendy; Vahid AfsharKharghan | Zendy; Joel L. Moake | Zendy

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Human Complement Factor H Is a Reductase for Large Soluble von Willebrand Factor Multimers—Brief Report

Author(s) -

Leticia Nolasco,

Jennifer Nolasco,

Shuju Feng,

Vahid AfsharKharghan,

Joel L. Moake

Publication year - 2013

Publication title -

arteriosclerosis thrombosis and vascular biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.007

H-Index - 270

eISSN - 1524-4636

pISSN - 1079-5642

DOI - 10.1161/atvbaha.113.302280

Subject(s) - von willebrand factor , disintegrin , chemistry , metalloproteinase , recombinant dna , thrombospondin , biochemistry , alternative complement pathway , microbiology and biotechnology , platelet , complement system , antibody , enzyme , biology , immunology , gene

Ultralarge von Willebrand factor (vWF) strings are secreted by, and anchored to, stimulated human endothelial cells. A disintegrin and metalloprotease with thrombospondin domains-type 13 cleaves the ultralarge vWF strings into large soluble vWF multimers. Normal plasma contains a nonproteolytic reducing activity that subsequently rapidly diminishes the size of the large soluble vWF multimers.

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