An active zymogen: unravelling the mystery of tissue-type plasminogen activator.

Abstract:

:In contrast to almost all other proteinases, human tissue-type plasminogen activator (tPA) is also proteolytically active in its zymogen or single-chain form. The closely related plasminogen activator isolated from vampire bat saliva (vPA) acts exclusively in the single-chain form, lacking the requisite cleavage site for proteolytic activation. Recent structural studies on the proteolytic domains of vPA and human tPA in two- and single-chain forms reveal the mechanism of this anomalous activity. The PA-catalyzed proteolytic conversion of plasminogen to plasmin, responsible for the initiation of fibrinolysis, is fibrin-dependent; comparative structural analysis of the plasminogen activators provides clues as to the role of fibrin as cofactor.

journal_name

Biol Chem

journal_title

Biological chemistry

authors

Stubbs MT,Renatus M,Bode W

doi

10.1515/bchm.1998.379.2.95

subject

Has Abstract

pub_date

1998-02-01 00:00:00

pages

95-103

issue

2

eissn

1431-6730

issn

1437-4315

journal_volume

379

pub_type

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