Thromb Haemost 2003; 89(06): 996-1003
DOI: 10.1055/s-0037-1613401
Platelets and Blood Cells
Schattauer GmbH

A new monoclonal antibody, mAb 204-11, that influences the binding of platelet GPVI to fibrous collagen

Masaaki Moroi
1   Department of Protein Biochemistry, Institute of Life Science, Kurume University, Kurume, Fukuoka, Japan
,
Jun Mizuguchi
2   Blood Products Research Department, The Chemo-Sero-Therapeutic Research Institute, Kumamoto, Kumamoto, Japan
,
Sachiko Kawashima
3   Department of Veterinary Pharmacology, Faculty of Agriculture, Miyazaki University, Miyazaki, Miyazaki, Japan
,
Michiko Nagamatsu
2   Blood Products Research Department, The Chemo-Sero-Therapeutic Research Institute, Kumamoto, Kumamoto, Japan
,
Yoshiki Miura
1   Department of Protein Biochemistry, Institute of Life Science, Kurume University, Kurume, Fukuoka, Japan
,
Tomohiro Nakagaki
2   Blood Products Research Department, The Chemo-Sero-Therapeutic Research Institute, Kumamoto, Kumamoto, Japan
,
Katsuaki Ito
3   Department of Veterinary Pharmacology, Faculty of Agriculture, Miyazaki University, Miyazaki, Miyazaki, Japan
,
Stephanie M. Jung
1   Department of Protein Biochemistry, Institute of Life Science, Kurume University, Kurume, Fukuoka, Japan
› Author Affiliations
Further Information

Publication History

Received 17 September 2002

Accepted after revision 03 March 2003

Publication Date:
08 December 2017 (online)

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Summary

The newly identified platelet collagen receptor glycoprotein VI binds to fibrous collagen, inducing platelet activation. Several antibodies against GPVI have been reported, including a patient’s auto-antibodies, that activates platelets through their ability to crosslink this glycoprotein. We have developed a monoclonal antibody (mAb) against GPVI using the recombinant extracellular domain of GPVI as an antigen. This antibody, mAb 204-11, induced platelet aggregation and tyrosine phosphorylation of proteins similar to those induced by GPVI-reactive proteins, collagen and convulxin. Its interaction with GPVI was analyzed by measuring the effect of the antibody on GPVI binding to collagen using a dimeric form of recombinant GPVI, GPVI-Fc2. MAb 204-11 inhibited the binding of GPVI-Fc2 to fibrous collagen particles, but enhanced the GPVI binding to immobilized collagen, suggesting that the antibody binds to a region near the collagen binding site of GPVI. MAb 204-11 also inhibited the GPVI binding to convulxin at a low concentration, but not completely. Since mAb 204-11 reacts specifically with GPVI and is applicable for immunoblotting and immunoprecipitation, this antibody would be useful for studies on GPVI.