Comparison of the primary structure of the functional domains of human and porcine von Willebrand factor that mediate platelet adhesion.

Abstract

Porcine von Willebrand factor (vWF) directly aggregates human platelets in vitro indicating a conformational difference between the human and porcine molecules. We amplified and directly sequenced 1242 nucleotides of porcine vWF cDNA that encodes functional domains which mediate the binding of vWF to platelets and subendothelium. The deduced amino acid sequence corresponds to residues 473-891 of the human mature vWF subunit and is 79% homologous with the human protein. Significant differences are found in two discontinuous segments thought to be involved in the binding of vWF to platelet glycoprotein Ib. Porcine vWF lacks four contiguous residues in the first segment and has two positively charged arginine residues in the second. Three point mutations associated with human type IIB von Willebrand disease in the first segment of a botrocetin binding site are at the same position as mismatches between the pig and human. The second segment of the botrocetin site is highly conserved while the third segment shows only a 60% homology.

• Authors: B R Bahnak, J M Lavergne, V Ferreira, D Kerbiriou-Nabias, D Meyer
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 182 Issue 2 Pg. 561-8 (Jan 31 1992) ISSN: 0006-291X [Print] United States
• PMID: 1370885 (Publication Type: Comparative Study, Journal Article)

Chemical References

• Macromolecular Substances
• Oligodeoxyribonucleotides
• von Willebrand Factor
• RNA
• RNA-Directed DNA Polymerase

Topics

• Amino Acid Sequence
• Animals
• Base Sequence
• Humans
• Lung (physiology)
• Macromolecular Substances
• Molecular Sequence Data
• Oligodeoxyribonucleotides
• Platelet Adhesiveness
• Polymerase Chain Reaction
• RNA (genetics, isolation & purification)
• RNA-Directed DNA Polymerase
• Sequence Homology, Nucleic Acid
• Swine
• von Willebrand Factor (genetics, physiology)