Plasminogen and tissue plasminogen activator interact with antithrombin III.

Abstract:

:Human antithrombin III was demonstrated to bind plasminogen specifically in a time and concentration-dependent manner. The above binding was also confirmed using ligand western blot assays. The interaction of plasminogen was significantly (>90%) inhibited by lysine, indicating the involvement of kringles in binding antithrombin III. Plasminogen also bound to heparin-antithrombin III complex. In converse experiments, antithrombin III also interacted with immobilized plasminogen. Using carboxypeptidase B digestion, the plasminogen-binding site of antithrombin III was localized to the carboxy-terminus lysine of the anticoagulant protein. Tissue plasminogen activator also interacted with antithrombin III in a time- and concentration-dependent manner and its binding was also significantly (>90%) inhibited by lysine. Moreover, the interaction of plasminogen and tissue plasminogen activator with antithrombin III was competitive. These results provide the first evidence for the interaction of antithrombin III with fibrinolytic factors and suggest that antithrombin III may serve to localize these factors at the site of clot formation.

journal_name

Thromb Res

journal_title

Thrombosis research

authors

Dudani AK

doi

10.1016/s0049-3848(00)00268-1

subject

Has Abstract

pub_date

2000-09-15 00:00:00

pages

635-41

issue

6

eissn

0049-3848

issn

1879-2472

pii

S0049-3848(00)00268-1

journal_volume

99

pub_type

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