Thromb Haemost 1989; 62(03): 984-988
DOI: 10.1055/s-0038-1651039
Original Article
Schattauer GmbH Stuttgart

Mechanism of Potentiation by Manganese Ion of Aggregation of Porcine Pancreatic Elastase-Treated Human Platelets

Hiroyuki Azuma
The First Department of Internal Medicine, School of Medicine, The University of Tokushima, Tokushima, Japan
,
Toshio Shigekiyo
The First Department of Internal Medicine, School of Medicine, The University of Tokushima, Tokushima, Japan
,
Shinji Miura
The First Department of Internal Medicine, School of Medicine, The University of Tokushima, Tokushima, Japan
,
Yuka Uno
The First Department of Internal Medicine, School of Medicine, The University of Tokushima, Tokushima, Japan
,
Shiro Saito
The First Department of Internal Medicine, School of Medicine, The University of Tokushima, Tokushima, Japan
› Author Affiliations
Further Information

Publication History

Received: 23 August 1988

Accepted after revision 30 June 1989

Publication Date:
30 June 2018 (online)

Summary

The effect of manganese ion (Mn2+) on the aggregation of porcine pancreatic elastase-treated platelets (ETP) induced by fibrinogen (Fbg) was studied. Mn2+ enhanced the aggregation of ETP on addition of Fbg specifically and dose-dependently. This effect of Mn2+ was not associated with the formation of thromboxane A2, and was not affected by pretreatment of ETP with acetylsalicylic acid in the presence of Mn2+. Moreover, it was not dependent on extracellular adenosine diphosphate, as shown by removal of extracellular adenosine diphosphate by pretreatment of ETP with creatine phosphate/creatine phosphokinase. Studies on the binding of 125I-Fbg to ETP showed that Mn2+ increased the Kd value of binding but did not affect the number of Fbg binding sites. These results indicate that Mn2+ specifically and dose-dependently potentiated Fbg-induced aggregation of ETP and that this effect of Mn2+ may be due to an increase in the affinity of binding of Fbg to the glycoprotein IIb-IIIa complex on the membranes of ETP.

 
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