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Thromb Haemost 1992; 68(04): 464-469
DOI: 10.1055/s-0038-1646298
Original Article
Schattauer GmbH Stuttgart

The Interaction of Botrocetin with Normal or Variant von Willebrand Factor (Types IIA and IIB) and Its Inhibition by Monoclonal Antibodies that Block Receptor Binding

Y Fujimura
1   The Departments of Blood Transfusion and Pediatrics, Nara Medical College, Kashihara, Nara, Japan
,
S Miyata
1   The Departments of Blood Transfusion and Pediatrics, Nara Medical College, Kashihara, Nara, Japan
,
S Nishida
1   The Departments of Blood Transfusion and Pediatrics, Nara Medical College, Kashihara, Nara, Japan
,
S Miura
1   The Departments of Blood Transfusion and Pediatrics, Nara Medical College, Kashihara, Nara, Japan
,
M Kaneda
1   The Departments of Blood Transfusion and Pediatrics, Nara Medical College, Kashihara, Nara, Japan
,
A Yoshioka
1   The Departments of Blood Transfusion and Pediatrics, Nara Medical College, Kashihara, Nara, Japan
,
H Fukui
1   The Departments of Blood Transfusion and Pediatrics, Nara Medical College, Kashihara, Nara, Japan
,
M Katayama
2   The Takara-Shuzo Co, Ohtsu, Shiga, Japan
,
E G D Tuddenham
3   The Clinical Research Centre, Middlesex, U. K.
,
Y Usami
4   The Division of Biomedical Polymer Science, Fujita Health University School of Medicine, Toyoake, Aichi, Japan
,
K Titani
4   The Division of Biomedical Polymer Science, Fujita Health University School of Medicine, Toyoake, Aichi, Japan
› Author Affiliations
Further Information

Publication History

Received 18 October 1991

Accepted after revision 13 May 1992

Publication Date:
04 July 2018 (online)

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Summary

We have recently shown the existence of two distinct forms of botrocetin (one-chain and two-chain), and demonstrated that the two-chain species is approximately 30 times more active than the one-chain in promoting von Willebrand factor (vWF) binding to platelet glycoprotein (GP) Ib. The N-terminal sequence of two-chain botrocetin is highly homologous to sea-urchin Echinoidin and other Ca2+-dependent lectins (Fujimura et al., Biochemistry 1991; 30: 1957–64).

Present data indicate that purified two-chain botrocetin binds to vWF from plasmas of patients with type IIA or IIB von Willebrand disease and its interaction is indistinguishable from that with vWF from normal individuals. However, an “activated complex” formed between botrocetin and IIB vWF expresses an enhanced biological activity for binding to GP Ib whereas the complex with IIA vWF has a decreased binding activity. Among several anti-vWF monoclonal antibodies (MoAbs) which inhibit ristocetin-induced platelet aggregation and/or vWF binding to GPIb, only two MoAbs (NMC-4 and RFF-VIII RAG:1) abolished direct binding between purified botrocetin and vWF. This suggests that they recognize an epitope(s) on the vWF molecule in close proximity to the botrocetin binding site.

 

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