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Galectin-1 and Galectin-3 Constitute Novel-Binding Partners for Factor VIII
Author(s) -
Jamie M. O’Sullivan,
P. Vincent Jenkins,
Orla Rawley,
Kristina Gegenbauer,
Alain Chion,
Michelle Lavin,
Barry J. Byrne,
Richard O’Kennedy,
Roger J. S. Preston,
Teresa M. Brophy,
James S. O’Donnell
Publication year - 2016
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.115.306915
Subject(s) - von willebrand factor , galectin , chemistry , chinese hamster ovary cell , glycan , recombinant dna , galectin 1 , glycosylation , exoglycosidase , galectin 3 , plasma protein binding , in vivo , microbiology and biotechnology , biochemistry , biology , immunology , receptor , glycoprotein , gene , platelet
Recent studies have demonstrated that galectin-1 (Gal-1) and galectin-3 (Gal-3) can bind von Willebrand factor and directly modulate von Willebrand factor-dependent early thrombus formation in vivo. Because the glycans expressed on human factor VIII (FVIII) are similar to those of von Willebrand factor, we investigated whether galectins might also bind and modulate the activity of FVIII.

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