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Alboserpin, a Factor Xa Inhibitor from the Mosquito Vector of Yellow Fever, Binds Heparin and Membrane Phospholipids and Exhibits Antithrombotic Activity

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    SYSNO ASEP0364839
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleAlboserpin, a Factor Xa Inhibitor from the Mosquito Vector of Yellow Fever, Binds Heparin and Membrane Phospholipids and Exhibits Antithrombotic Activity
    Author(s) Calvo, E. (US)
    Mizurini, D.M. (BR)
    Sa-Nunes, A. (US)
    Ribeiro, J.M.C. (US)
    Andersen, J. F. (US)
    Mans, B.J. (US)
    Monteiro, R.Q. (BR)
    Kotsyfakis, Michalis (BC-A) RID, ORCID
    Francischetti, I.M.B. (US)
    Source TitleJournal of Biological Chemistry. - : Elsevier - ISSN 0021-9258
    Roč. 286, č. 32 (2011), 27998-28010
    Number of pages13 s.
    Languageeng - English
    CountryUS - United States
    Keywordsserpin ; mosquito ; Aedes albopictus ; phospholipids ; Factor Xa ; heparin ; binding affinity ; coagulation ; thrombus ; bleeding
    Subject RIVGJ - Animal Vermins ; Diseases, Veterinary Medicine
    CEZAV0Z60220518 - PAU-O, BC-A (2005-2011)
    UT WOS000293557800018
    DOI10.1074/jbc.M111.247924
    AnnotationThe function of a mosquito anticoagulant serpin named as Alboserpin is presented. The recombinant protein binds to phospholipids and it inhibits the activity of human coagulation factor Xa. Binding is highly specific and is not detectable for FX, catalytic site-blocked FXa, thrombin and 12 other enzymes. Alboserpin displays high-affinity binding to heparin, but no change in FXa inhibition was observed in the presence of the cofactor, implying that bridging mechanisms did not take place. Alboserpin displays a potent pharmacological activity since it prevents thrombus formation provoked by ferric chloride injury of the carotid artery and it increases bleeding in a dose-dependent manner.
    WorkplaceBiology Centre (since 2006)
    ContactDana Hypšová, eje@eje.cz, Tel.: 387 775 214
    Year of Publishing2012
Number of the records: 1  

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