A Plasminogen Activator Inhibitor-2 from a Promyelocytic Leukemia Cell Line, PL-21, Binds to the Carboxy-Terminal Chain of Plasminogen Activators

Tetsuo Takeuchi; Kenji Niiya; Ichiro Kubonishi; Isao Miyoshi

doi:10.1055/s-0038-1645205

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 1990; 63(02): 259-264
DOI: 10.1055/s-0038-1645205

Original Article

Schattauer GmbH Stuttgart

A Plasminogen Activator Inhibitor-2 from a Promyelocytic Leukemia Cell Line, PL-21, Binds to the Carboxy-Terminal Chain of Plasminogen Activators

Authors

Tetsuo Takeuchi

The Department of Medicine, Kochi Medical School, Kochi, Japan
Kenji Niiya

The Department of Medicine, Kochi Medical School, Kochi, Japan
Ichiro Kubonishi

The Department of Medicine, Kochi Medical School, Kochi, Japan
Isao Miyoshi

The Department of Medicine, Kochi Medical School, Kochi, Japan

Abstract

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Summary

A promyelocytic leukemia cell line, PL-21, was found to produce an inhibitor of plasminogen activators (PAI). The PAI reacted to anti-PAl-2 but not anti-PAI-1 anti-serum and had an apparent molecular weight of 43 kDa on unreduced SDS-PAGE. The PAI inhibited not only urokinase-type plasminogen activator (u-PA) but single- and two-chain tissue-type plasminogen activators (t-PAs) on plasminogen-containing fibrin plate. It formed SDS-stable complexes with both t-PA and u-PA but not with prourokinase as demonstrated by both fibrin zymography and immunoblotting using anti-PA and anti-PAI-2 antisera after SDS-PAGE. These complexes were still present even after reduction with dithiothreitol. The PAI appears to bind to the carboxy-terminal chain of both PAs, because the part of the band corresponding to the carboxy-terminal chain of PAs moved to an upper position as a result of complex formation when two-chain form of PAs were incubated with the PAI and analyzed by SDS-PAGE followed by immunoblotting

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References

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