Literature DB >> 6710439

Histidine-rich glycoprotein and alpha 2-plasmin inhibitor in inhibition of plasminogen binding to fibrin.

A Ichinose, J Mimuro, T Koide, N Aoki.   

Abstract

The plasma proteins alpha 2-plasmin inhibitor and histidine-rich glycoprotein were compared directly with respect to their effectiveness in inhibiting the binding of plasminogen to fibrin under the same experimental conditions. At their physiological concentrations, the presence of alpha 2-plasmin inhibitor more markedly decreased the binding of plasminogen to fibrin than histidine-rich glycoprotein. Significance of these findings in inhibition of fibrinolysis is discussed.

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Year:  1984        PMID: 6710439     DOI: 10.1016/0049-3848(84)90079-3

Source DB:  PubMed          Journal:  Thromb Res        ISSN: 0049-3848            Impact factor:   3.944


  4 in total

1.  alpha 2-Antiplasmin Enschede: dysfunctional alpha 2-antiplasmin molecule associated with an autosomal recessive hemorrhagic disorder.

Authors:  C Kluft; H K Nieuwenhuis; D C Rijken; E Groeneveld; G Wijngaards; W van Berkel; G Dooijewaard; J J Sixma
Journal:  J Clin Invest       Date:  1987-11       Impact factor: 14.808

2.  The mechanism of activation of plasminogen at the fibrin surface by tissue-type plasminogen activator in a plasma milieu in vitro. Role of alpha 2-antiplasmin.

Authors:  D Rouy; E Anglés-Cano
Journal:  Biochem J       Date:  1990-10-01       Impact factor: 3.857

3.  Interaction of histidine-rich glycoprotein with fibrinogen and fibrin.

Authors:  L L Leung
Journal:  J Clin Invest       Date:  1986-04       Impact factor: 14.808

4.  Functional factor XIII-A is exposed on the stimulated platelet surface.

Authors:  Joanne L Mitchell; Ausra S Lionikiene; Steven R Fraser; Claire S Whyte; Nuala A Booth; Nicola J Mutch
Journal:  Blood       Date:  2014-10-20       Impact factor: 22.113

  4 in total

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