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Thromb Haemost 2000; 83(05): 769-776
DOI: 10.1055/s-0037-1613906
Review Article
Schattauer GmbH

Involvement of Activated Integrin α2β1 in the Firm Adhesion of Platelets onto a Surface of Immobilized Collagen under Flow Conditions

Masaaki Moroi
1   From the Department of Protein Biochemistry, Institute of Life Science, Kurume University, Kurume-shi, Fukuoka-ken, Japan
,
Ichiro Onitsuka
1   From the Department of Protein Biochemistry, Institute of Life Science, Kurume University, Kurume-shi, Fukuoka-ken, Japan
2   The Third Department of Internal Medicine, Faculty of Medicine, Kurume University, Kurume-shi, Fukuoka-ken, Japan
,
Tsutomu Imaizumi
2   The Third Department of Internal Medicine, Faculty of Medicine, Kurume University, Kurume-shi, Fukuoka-ken, Japan
,
Stephanie M. Jung
1   From the Department of Protein Biochemistry, Institute of Life Science, Kurume University, Kurume-shi, Fukuoka-ken, Japan
› Author Affiliations
We thank Dr. B. S. Coller (Mount Sinai School of Medicine, New York, NY) for the kind gift of antibodies, 6F1 and 10E5, and thank Drs. Yuji Saito and Junichi Takagi (Tokyo Institute of Technology, Tokyo, Japan) for the antibody TS2/16.
Further Information

Publication History

Received 31 December 1998

Accepted after revision 25 November 1999

Publication Date:
08 December 2017 (online)

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Summary

Recently, we demonstrated that agonist-induced activation of the platelet surface collagen-receptor integrin α1 β2 converts it to an active form that can bind soluble collagen with high affinity (Jung, SM, Moroi, M: J Biol Chem 1998; 273: 14827-37). Here, the involvement of α2 β1 activation and the high affinity binding property of activated α2β1 in platelet adhesion to a collagen surface under flow conditions were analyzed. Platelet adhesion to immobilized collagen was measured in the presence of TS2/16, an activating anti-integrin α2β1 antibody, and inhibiting antibodies, Gi9 and 6F1. TS2/16 decreased the moving velocity of platelets on the collagen surface, but Gi9 and 6F1 increased it, indicating that α2β1 activation induces the tight binding of platelets to immobilized collagen under flow. Platelet adhesion, expressed as the surface area occupied by adhered platelets, in the presence of TS2/16 was similar to that in its absence. In contrast, adding Gi9 or 6F1 caused biphasic adhesion composed of a first phase, a lag phase whose length differed in each experiment, and a second phase adhesion with a rate similar to that of the control. This biphasic adhesion indicates that α2β1 activity is inhibited and also suggests that some other factor(s) may contribute to the adhesion under flow. At concentrations where neither 6F1 nor Gi9 affected collagen-induced aggregation, these antibodies inhibited soluble collagen binding to thrombin-activated platelets. Only at much higher concentration did 6F1 inhibit collagen-induced aggregation. TS2/16 had no effect on the aggregation. The present results are evidence against the major involvement of integrin α2β1 in platelet aggregation; instead, they indicate that integrin α2β1 would be mainly associated with the tight binding of platelets to collagen.

Key words

Integrin α2β1 - platelet - flow adhesion - collagen
 

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