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Impact of Plasminogen Activator Inhibitor-1 Serum Levels and the -675 4G/5G Variant in the SERPINE1 Gene on Systemic Sclerosis in a Mexican Population. [PDF]
Lomelí-Nieto JA +10 more
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Increased plasminogen activator inhibitor-1 (PAI-1) and its associations with metabolic risk in healthy young adults with early life stress. [PDF]
Kudinova AY +8 more
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Plasminogen activator inhibitor-1 promotes immune evasion in tumors by facilitating the expression of programmed cell death-ligand 1. [PDF]
Ibrahim AA +9 more
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Plasminogen Activator Inhibitor-1
Current Medicinal Chemistry, 2004Plasminogen activator inhibitor-1 (PAI-1) is an important component of the plasminogen/plasmin system as it is the main inhibitor of tissue-type and urokinase-type plasminogen activator. Consequently, PAI-1 plays an important role in cardiovascular diseases (mainly through inhibition of t-PA) and in cell migration and tumor development (mainly through ...
Ann, Gils, Paul J, Declerck
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Plasminogen Activator Inhibitor-1 in Aging
Seminars in Thrombosis and Hemostasis, 2014Plasminogen activator inhibitor-1 (PAI-1), a principal inhibitor of fibrinolysis, is induced in thrombotic, fibrotic, and cardiovascular diseases, which in turn primarily afflict the older population. This induction of PAI-1 may play an important role in the pathology of these diseases as PAI-1 can regulate the dissolution of fibrin and also inhibit ...
Koji, Yamamoto +2 more
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Plasminogen Activator Inhibitor-1 and Restenosis
Current Drug Targets, 2007Despite the introduction of drug-eluting stents restenosis remains an important clinical problem. In this review we examine the role of plasminogen activator inhibitor-1 (PAI-1) in controlling restenosis after balloon angioplasty and stent implantation.
Nadish, Garg, William P, Fay
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Reversible interactions between plasminogen activators and plasminogen activator inhibitor-1
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1992We have shown that the urokinase (UK) kringle domain contains a high-affinity plasminogen activator inhibitor-1 (PAI-1) binding site, responsible for the 10-fold faster complex formation between UK and PAI-1 than between PAI-1 and low-molecular-weight urokinase (LMWUK).
J, Mimuro +4 more
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