Conformational change of plasminogen: effects of N-terminal peptides of Glu-plasminogen.

Abstract:

:Seven peptides were synthesized to analyze the mechanism of the intramolecular binding of the N-terminal peptide of Glu-plasminogen (Glu-plg) to its kringles. They were Ala44-Lys50, Ala44-Glu51, Ala44-Ser49, Val17-Gly23, Lys19-Gly23, Lys19-Gln21 and Lys19-Lys20. Ala44-Lys50, Ala44-Glu51 and Lys19-Lys20.enhanced the activation of Glu-plg by tissue plasminogen activator (t-PA) or urinary plasminogen activator (u-PA). The activation of Lys-plg, however, was not influenced by these peptides. Therefore, it is suggested that these three peptides worked on Glu-plg in a similar manner as lysine analogue by making the conformation of Glu-plg looser. These peptides did not have any direct effects on u-PA and t-PA. Concerning the effect on fibrinolysis Ala44-Lys50 and Lys19-Lys20 prolonged euglobulin clot lysis time. These results indicate that Ala44-Glu51 may be a responsible binding site in the N-terminal portion of Glu-plg, and LBS of kringle 1 or 4 is the binding site of N-terminal portion of Glu-plg.

journal_name

Thromb Res

journal_title

Thrombosis research

authors

Takada Y,Urano T,Takada A

doi

10.1016/0049-3848(93)90156-i

subject

Has Abstract

pub_date

1993-04-15 00:00:00

pages

151-9

issue

2

eissn

0049-3848

issn

1879-2472

pii

0049-3848(93)90156-I

journal_volume

70

pub_type

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