Work

von Willebrand factor binds specifically to sulfated glycolipids.

Year: 1986

Type: article

Abstract: The human plasma glycoprotein Factor VIII/von Willebrand factor (vWF) binds specifically and with high affinity to sulfatides (galactosylceramide-I3-sulfate). vWF does not bind to gangliosides, neutral glycolipids, phospholipids, or cholesterol 3-sulfate. Although the largest oligomers of vWF bind preferentially to sulfatides, vWF monomers and dimers also bind but with reduced affinity. vWF binding is inhibited at high ionic strength or low pH, by some sulfated polysaccharides and by antibodies to vWF. Binding of vWF to sulfatides is probably responsible for its agglutination of aldehyde-fixed erythrocytes and may play a role in vWF-induced platelet adhesion or platelet aggregation.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(17)35782-4

Authors: D D Roberts, S B Williams, H R Gralnick, V Ginsburg

Institutions: National Institutes of Health, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health Clinical Center

Language: English

Topic: Platelet Disorders and Treatments

Subfield: Hematology

Field: Medicine

Domain: Health Sciences

SDG: Good health and well-being

Open Access status: hybrid

Estimated APC paid: $3,430