Increased susceptibility of von Willebrand factor to proteolysis by ADAMTS13: Should the multimer profile be normal or type 2A? [5]

Blood

Volumn 103, Issue 8, 2004, Pages 3246-

  Bowen, Derrick J ^a  

^a CARDIFF UNIVERSITY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; TYROSINE; VON WILLEBRAND FACTOR; VON WILLEBRAND FACTOR CLEAVING PROTEINASE;

HEMOSTASIS; HUMAN; LETTER; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DENATURATION; THROMBOCYTE ADHESION; THROMBOCYTE AGGREGATION; VON WILLEBRAND DISEASE;

EID: 1842422288     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood-2004-01-0376     Document Type: Letter

References (6)

1. Fischer BE, Thomas KB, Domer F. Von Willebrand factor: measuring its antigen or function? Correlation between the level of antigen, activity, and multimer size using various detection systems. Thromb Res. 1998;91:39-43.
2. Ginsburg D, Bowie EJW. Molecular genetics of von Willebrand disease. Blood. 1992;79:2507-2519.
3. O'Brien LA, James PD, Othman M, Berber E, et al. A founder von Willebrand factor haplotype associated with type 1 von Willebrand disease. Blood. 2003;102:549-557.
4. Bowen DJ, Collins PW. An amino acid polymorphism in von Willebrand factor correlates with increased susceptibility to proteolysis by ADAMTS13. Blood. Prepublished on October 2, 2003, as DOI 10.1182/blood-2003-05-1505. (Now available as Blood. 2004;103:941-947).
5. Bowen DJ, Collins PW. An amino acid polymorphism in von Willebrand factor correlates with increased susceptibility to proteolysis by ADAMTS13. Blood. Prepublished on October 2, 2003, as DOI 10.1182/blood-2003-05-1505. (Now available as Blood. 2004;103:941-947).
6. Tsai H, Sussman II, Ginsburg D, Lankhof H, Sixma JJ, Nagel RL. Proteolytic cleavage of recombinant type 2A von Willebrand factor mutants R843W and R834Q: inhibition by doxycycline and by monoclonal antibody VP-1. Blood. 1997;89:1654-1662.