TITLE

Structure, Function, and Activation of Coagulation Factor VII

AUTHOR(S)
Eigenbrot, Charles
PUB. DATE
June 2002
SOURCE
Current Protein & Peptide Science;Jun2002, Vol. 3 Issue 3, p287
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
Factor VII is the coagulation protease responsible for starting a cascade of proteolytic events that lead to thrombin generation, fibrin deposition, and platelet activation. As such, FVII has attracted wide interest as a target for clinical anti-coagulant applications. Commensurate with the critical importance of maintaining balance between thrombosis and hemostasis and its place at the beginning of the coagulation process, FVII is subject to a variety of biological and biochemical control mechanisms, among them allosteric influences exerted by cofactors, substrates, and inhibitors. Sites on FVIIa where allosteric influences are exerted and manifested have been identified and characterized in considerable detail. In recent years, a three-dimensional context for the interpretation of these results has become available from structural studies. New X-ray structures have augmented specific aspects of our understanding, in particular the X-ray structure of a fragment of the FVII zymogen. This review summarizes general allosteric behaviors of FVIIa and recapitulates structural findings since 1996, with particular emphasis on the recently determined zymogen structure.
ACCESSION #
11134750

 

Related Articles

  • Thrombin-Activated Receptors: Promising Targets for Cancer Therapy? Garcia-Lopez, M. T.; Gutierrez-Rodriguez, M.; Herranz, R. // Current Medicinal Chemistry;Jan2010, Vol. 17 Issue 2, Special section p109 

    In addition to the key role of thrombin in blood coagulation, this multifunctional serine protease activates platelets and regulates the behavior of other cells through G-protein coupled protease activated receptors (PARs). PAR-1 is the principal thrombin-activated receptor involved in platelet...

  • The Extended Cleavage Specificity of Human Thrombin. Gallwitz, Maike; Enoksson, Mattias; Thorpe, Michael; Hellman, Lars // PLoS ONE;Feb2012, Vol. 7 Issue 2, p1 

    Thrombin is one of the most extensively studied of all proteases. Its central role in the coagulation cascade as well as several other areas has been thoroughly documented. Despite this, its consensus cleavage site has never been determined in detail. Here we have determined its extended...

  • Synthesis and Biological Activity of N-Sulfonyltripeptides with C-Terminal Arginine as Potential Serine Proteases Inhibitors. Markowska, Agnieszka; Bruzgo, Magdalena; Gorodkiewicz, Ewa; Surażyński, Arkadiusz // International Journal of Peptide Research & Therapeutics;Sep2013, Vol. 19 Issue 3, p191 

    Tripeptides of the general X-SO- d-Ser-AA-Arg-CO-Y formula, where X = α-tolyl, p-tolyl, 2,4,6-triisopropylphenyl; AA = alanine, glycine, norvaline and Y = OH, NH-(CH)NH were obtained and tested for their effect on the amidolytic activities of urokinase, thrombin, trypsin, plasmin, t-PA and...

  • Tissue Factor in the myocardium: Evidence of roles in haemostasis and inflammation. Mumford, Andrew D.; McVey, John H. // Disease Markers;2004, Vol. 20 Issue 6, p353 

    The interaction between cell-surface tissue factor (TF) and the plasma coagulation factor VII (FVII) initiates the coagulation network that leads to the generation of thrombin and the formation of a fibrin clot. Thrombin also activates cellular protease activated receptors (PARs) through which...

  • The Extended Cleavage Specificity of Human Thrombin. Gallwitz, Maike; Enoksson, Mattias; Thorpe, Michael; Hellman, Lars // PLoS ONE;Feb2012, Vol. 7 Issue 2, p1 

    Thrombin is one of the most extensively studied of all proteases. Its central role in the coagulation cascade as well as several other areas has been thoroughly documented. Despite this, its consensus cleavage site has never been determined in detail. Here we have determined its extended...

  • Distinct yet complementary mechanisms of heparin and glycoprotein llb/Illa inhibitors on platelet activation and aggregation: implications for restenosis during percutaneous coronary intervention. Day, J. R. S.; Malik, I. S.; Weerasinghe, A.; Poullis, M.; Nadra, I.; Haskard, D. O.; Taylor, K. M.; Landis, R. C. // Heart;Jul2004, Vol. 90 Issue 7, p794 

    Objective: To study the effect of unfractionated heparin (UFH) venus low molecular weight heparin (LMWH) in combination with glycoprotein (Gp) IIb/IIIa blockers on platelet activation and aggregation. Methods: Washed platelets were stimulated with thrombin in the presence or absence of UFH...

  • TRA 2°P-TIMI 50 Results. Alexander, Lori // MD Conference Express;Oct2012, p25 

    The article discusses the findings from the Thrombin Receptor Antagonist in Secondary Prevention of Atherothrombotic Ischemic Events-Thrombolysis in Myocardial Infarction (MI) 50 (TRA 2°P-TIMI 50) clinical trial. Medical director Benjamin M. Scirica has presented the efficacy and safety of...

  • Thrombin-Receptor Antagonist Vorapaxar in Acute Coronary Syndromes. Tricoci, Pierluigi; Huang, Zhen; Held, Claes; Moliterno, David J.; Armstrong, Paul W.; Van de Werf, Frans; White, Harvey D.; Aylward, Philip E.; Wallentin, Lars; Chen, Edmond; Lokhnygina, Yuliya; Pei, Jinglan; Leonardi, Sergio; Rorick, Tyrus L.; Kilian, Ann M.; Jennings, Lisa H.K.; Ambrosio, Giuseppe; Bode, Christoph; Cequier, Angel; Cornel, Jan H. // New England Journal of Medicine;1/5/2012, Vol. 366 Issue 1, p20 

    Background: Vorapaxar is a new oral protease-activated�receptor 1 (PAR-1) antagonist that inhibits thrombin-induced platelet activation. Methods: In this multinational, double-blind, randomized trial, we compared vorapaxar with placebo in 12,944 patients who had acute coronary syndromes...

  • PAR3 is a cofactor for PAR4 activation by thrombin. Nakanishi-Matsui, Mayumi; Zheng, Yao-Wu // Nature;4/6/2000, Vol. 404 Issue 6778, p609 

    Reports on findings regarding the interaction between protease-activated G-protein-coupled receptors, mPAR3 and mPAR4, in the platelets of mice. Insights into the mechanism of coagulation protease thrombin's activation of platelets during hemostasis and thrombosis.

Share

Read the Article

Courtesy of THE LIBRARY OF VIRGINIA

Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics