Thromb Haemost 1997; 78(02): 902-909
DOI: 10.1055/s-0038-1657650
Rapid Communication
Schattauer GmbH Stuttgart

Effect of a New Monoclonal Anti-Glycoprotein IX Antibody, KMP-9, on High Shear-Induced Platelet Aggregation[*]

Tetsuya Miyake
1  The First Department of Internal Medicine, Kansai Medical University, Osaka, Japan
,
Shosaku Nomura
1  The First Department of Internal Medicine, Kansai Medical University, Osaka, Japan
,
Yutaka Komiyama
2  Department of Clinical Sciences and Laboratory Medicine, Kansai Medical University, Osaka, Japan
,
Yasuhiko Miyazaki
1  The First Department of Internal Medicine, Kansai Medical University, Osaka, Japan
,
Hideo Kagawa
1  The First Department of Internal Medicine, Kansai Medical University, Osaka, Japan
,
Midori Masuda
2  Department of Clinical Sciences and Laboratory Medicine, Kansai Medical University, Osaka, Japan
,
Hakuo Takahashi
2  Department of Clinical Sciences and Laboratory Medicine, Kansai Medical University, Osaka, Japan
,
Yoshihiro Fujimura
3  Department of Blood Transfusion, Nara Medical College, Nara, Japan
,
Yasuo Ikeda
4  Department of Internal Medicine, Keio University School of Medicine, Tokyo, Japan
,
Shirou Fukuhara
1  The First Department of Internal Medicine, Kansai Medical University, Osaka, Japan
› Author Affiliations
Further Information

Publication History

Received 09 1996

Accepted after revision 03 April 1997

Publication Date:
12 July 2018 (online)

Summary

Human platelet glycoprotein Ib/IX complex acts as a receptor for von Willebrand factor. It is widely accepted that glycoprotein lb is the essential receptor component, but the role of glycoprotein IX is still unclear. We produced a new monoclonal anti-glycoprotein IX antibody (KMP-9) by the hybridoma technique using platelets from a patient with Glanzmann’s thrombasthenia. The epitope of KMP-9 was localized to the C-terminal 8 kD fragment of glycoprotein IX using ELISA analysis of polyethylene-pin-synthesized peptides, as well as Western blot analysis of platelets after digestion with N-glycosidase and Staphylococcus aureus V8 protease. KMP-9 partially inhibited high shear stress-induced platelet aggregation, but had no effect on aggregation induced by ristocetin or low shear stress. Its inhibitory effect on high shear stress-induced aggregation was weaker than that of antiglycoprotein lb or anti-glycoprotein Ilb/IIIa monoclonal antibodies. A 21-mer synthetic peptide (glycoprotein IX L110-G130) inhibited the binding of KMP-9 to platelets. It also competively inhibited the suppression of high shear stress-induced platelet aggregation by KMP-9, but had no direct effect on this aggregation. KMP-9 may be useful to clarify the physiological role of GPIX.

This work was partly supported by a Research Grant for Advanced Medical Care from the Ministry of Health and Welfare of Japan