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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

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
› Author Affiliations
Further Information

Publication History

Received 15 August 1989

Accepted after revision 21 December 1989

Publication Date:
02 July 2018 (online)

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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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