Monoclonal Antibodies against the Human Mannose Receptor that Inhibit the Binding of Tissue-type Plasminogen Activator

Marrie Barrett-Bergshoeff; Femke Noorman; Rogier Bos; Dingeman C Rijken

doi:10.1055/s-0038-1656040

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 1997; 77(04): 718-724
DOI: 10.1055/s-0038-1656040

Fibrinolysis

Schattauer GmbH Stuttgart

Monoclonal Antibodies against the Human Mannose Receptor that Inhibit the Binding of Tissue-type Plasminogen Activator

Authors

Marrie Barrett-Bergshoeff

The Gaubius Laboratory, TNO Prevention and Health, Leiden, The Netherlands
Femke Noorman

The Gaubius Laboratory, TNO Prevention and Health, Leiden, The Netherlands
Rogier Bos

The Gaubius Laboratory, TNO Prevention and Health, Leiden, The Netherlands
Dingeman C Rijken

The Gaubius Laboratory, TNO Prevention and Health, Leiden, The Netherlands

Abstract

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Summary

To study the role of the mannose receptor in cellular uptake and degradation of tissue-type plasminogen activator (t-PA), a set of five monoclonal antibodies (Moab) was generated against the mannose receptor isolated from human placental tissue.

All Moab specifically recognised the 175 kDa mannose receptor in a crude placenta extract, as shown in Western blot analysis. By use of im- munohistochemistry, we showed that in human placenta only the Hof- bauer cells (fetal macrophages) express the mannose receptor. Epitope competition experiments indicated that the Moab bound to at least two different epitopes on the receptor molecule. Moab 14-3, 14-5, and 15-2, which are directed against one of these epitopes, strongly inhibited the interaction between the purified mannose receptor and t-PA. These Moab also inhibited mannose receptor-mediated degradation of t-PA by cultured human macrophages. The low density lipoprotein receptor-related protein (LRP) mediated t-PA degradation was not affected by the Moab.

It is concluded that the Moab are useful for studying the expression of the human mannose receptor in Western blot and in immunohisto-chemistry, and for studying the interactions between the human mannose receptor and the mannose-containing ligand t-PA.

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References

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