In:
Thrombosis and Haemostasis, Georg Thieme Verlag KG, Vol. 63, No. 02 ( 1990), p. 259-264
Abstract:
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
Type of Medium:
Online Resource
ISSN:
0340-6245
,
2567-689X
DOI:
10.1055/s-0038-1645205
Language:
English
Publisher:
Georg Thieme Verlag KG
Publication Date:
1990
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