scholarly journals Expression of plasminogen activator inhibitor type 1 by human prostate carcinoma cells inhibits primary tumor growth, tumor-associated angiogenesis, and metastasis to lung and liver in an athymic mouse model.

1995 ◽  
Vol 96 (6) ◽  
pp. 2593-2600 ◽  
Author(s):  
G A Soff ◽  
J Sanderowitz ◽  
S Gately ◽  
E Verrusio ◽  
I Weiss ◽  
...  
Keyword(s):  
Mouse Model ◽  
Plasminogen Activator Inhibitor ◽  
Carcinoma Cells ◽  
Athymic Mouse ◽  
Primary Tumor Growth ◽  
Human Prostate Carcinoma ◽  
Inhibitor Type ◽  
Activator Inhibitor Type ◽  
Activator Inhibitor

Very long half-life plasminogen activator inhibitor type 1 reduces bleeding in a mouse model

2009 ◽  
Vol 105 (10) ◽  
pp. 1469-1476 ◽  
Author(s):  
Jerzy Jankun ◽  
Steven H. Selman ◽  
Rick W. Keck ◽  
Wiesława Łysiak-Szydłowska ◽  
Ewa Skrzypczak-Jankun
Keyword(s):  
Mouse Model ◽  
Plasminogen Activator ◽  
Half Life ◽  
Plasminogen Activator Inhibitor ◽  
Plasminogen Activator Inhibitor Type ◽  
Inhibitor Type ◽  
Activator Inhibitor Type ◽  
Activator Inhibitor

Limited Proteolysis of Vitronectin by Plasmin Destroys Heparin Binding Activity

1991 ◽  
Vol 66 (03) ◽  
pp. 310-314 ◽  
Author(s):  
David C Sane ◽  
Tammy L Moser ◽  
Charles S Greenberg
Keyword(s):  
Limited Proteolysis ◽  
Plasminogen Activator Inhibitor ◽  
Binding Activity ◽  
Binding Domain ◽  
Heparin Binding ◽  
Inhibitor Type ◽  
Activator Inhibitor Type ◽  
Activator Inhibitor ◽  
Pai 1

SummaryVitronectin (VN) stabilizes plasminogen activator inhibitor type 1 (PAI-1) activity and prevents the fibrin(ogen)-induced acceleration of plasminogen activation by t-PA. These antifibrinolytic activities as well as other functions are mediated by the glycosaminoglycan (GAG) binding domain of VN. Since the GAG binding region is rich in arginyl and lysyl residues, it is a potential target for enzymes such as plasmin. In this paper, the dose and time-dependent proteolysis of VN by plasmin is demonstrated. The addition of urokinase or streptokinase (200 units/ml) to plasma also produced proteolysis of VN. With minimal proteolysis, the 75 kDa band was degraded to a 62-65 kDa form of VN. This minimal proteolysis destroyed the binding of [3H]-heparin to VN and reversed the neutralization of heparin by VN.Thus, the plasmin-mediated proteolysis of the GAG binding activity of VN could destroy the antifibrinolytic activity of VN during physiologic conditions and during thrombolytic therapy. Furthermore, other functions of VN in complement and coagulation systems that are mediated by the GAG binding domain may be destroyed by plasmin proteolysis.

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