A Steady-state Template Model That Describes the Kinetics of Fibrin-stimulated [Glu1]- and [Lys78]Plasminogen Activation by Native tissue-type Plasminogen Activator and Variants That Lack Either the Finger or Kringle-2 Domain
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TLDR
The model indicates that catalytic efficiency is determined by the stability of the ternary activator-fibrin-plasminogen complex rather than the binding of the activator or plasminogens to fibrin, which implies that efforts to improve the enzymatic properties of t-PA might be more fruitfully directed at enhancing the Stability of the Ternary Complex rather than fibrIn binding.About:
This article is published in Journal of Biological Chemistry.The article was published on 1997-01-24 and is currently open access. It has received 66 citations till now. The article focuses on the topics: Plasminogen activator & Fibrin.read more
Citations
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A Study of the Mechanism of Inhibition of Fibrinolysis by Activated Thrombin-activable Fibrinolysis Inhibitor
TL;DR: It is concluded that TAFIa suppresses fibrinolysis by removing COOH-terminal lysine and arginine residues from fibrin, thereby reducing its cofactor functions in both plasminogen activation and the positive feedback conversion of Glu-plAsminogen to Lys-plasmineogen.
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Thrombin Activatable Fibrinolysis Inhibitor and an Antifibrinolytic Pathway
TL;DR: A historical account of efforts to isolate TAFI and characterize it with respect to its activation, activity, regulation, and potential function in vivo is encompassed.
Journal ArticleDOI
The Role of Annexin II Tetramer in the Activation of Plasminogen
Geetha Kassam,Kyu-Sil Choi,Jaspinder Ghuman,Hyoung-Min Kang,Sandra L. Fitzpatrick,Tracy Zackson,Saul L. Zackson,Mikayo Toba,Aya Shinomiya,David M. Waisman +9 more
TL;DR: Kinetic analysis established that AIIt produces a large increase of about 190-fold in the k cat, app and a small increase in theK m,app which resulted in a 90-fold increased in the catalytic efficiency of t-PA for [Glu]plasminogen.
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Basic mechanisms and regulation of fibrinolysis
TL;DR: A complete understanding of the regulation of fibrinolysis will come from the building of detailed mathematical models, and suitable models are at an early stage of development, but may improve as model clots increase in complexity to incorporate the components and interactions listed above.
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A novel approach to arterial thrombolysis.
TL;DR: Results indicate that inhibitors of TAFIa may comprise novel and very effective adjuncts to tPA and improve thrombolytic therapy to achieve both clot lysis and vessel patency.
References
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Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin.
TL;DR: The kinetic analysis suggested that the activation in the presence of fibrin occurs through binding of an activator molecule to the clot surface and subsequent addition of plasminogen (sequential ordered mechanism) to form a cyclic ternary complex.
Kinetics of the Activation of Plasminogen by Human Tissue Plasminogen Activator
TL;DR: In this paper, the activation of Gluplasminogen and Lys-minminogen in the presence of fibrinogen (f) was studied in purified systems, and the initial rate of activation (u) was calculated.
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On the regulation and control of fibrinolysis. Edward Kowalski Memorial Lecture.
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Studies on the kinetics of plasminogen activation by tissue plasminogen activator.
TL;DR: Fibrin was found to stimulate greatly (up to 1000-fold) the steady-state activation rate of plasminogen activation and a theory for the fibrin stimulating mechanism is presented.
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The binding of human plasminogen to fibrin and fibrinogen
M A Lucas,L J Fretto,P A McKee +2 more
TL;DR: It is the lower affinity binding site that interacts with fibrin(ogen) to accelerate activation of Glu-plasminogen activation over &fold, hence, while two lysine-binding sites may be involved in binding to fibrIn, it is theLower affinity binding sites that interactsWith only the high affinity lysin-binding site on GLU-plAsminogen blocked by EACA, fibr inogen still enhanced the rate of Glamorganisation.