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    Characterization of L-amino Acid Oxidase Derived from Venom: Procoagulant and Anticoagulant Activities

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    Author
    Nielsen, Vance G
    Affiliation
    Univ Arizona, Coll Med, Dept Anesthesiol
    Issue Date
    2019-09-30
    Keywords
    L-amino acid oxidase
    anticoagulant
    carbon monoxide releasing molecule
    fibrinogen polymerizing enzyme
    procoagulant
    thrombelastography
    
    Metadata
    Show full item record
    Publisher
    MDPI
    Citation
    Nielsen, V.G. Characterization of L-amino Acid Oxidase Derived from Crotalus adamanteus Venom: Procoagulant and Anticoagulant Activities. Int. J. Mol. Sci. 2019, 20, 4853.
    Journal
    INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
    Rights
    Copyright © 2019 by the author. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
    Collection Information
    This item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at repository@u.library.arizona.edu.
    Abstract
    Snake venom enzymes of the L-amino acid oxidase (LAAO) class are responsible for tissue hemorrhage, edema, and derangement of platelet function. However, what role, if any, these flavoenzymes play in altering plasmatic coagulation have not been well defined. Using coagulation kinetomic analyses (thrombelastograph-based), it was determined that the LAAO derived from Crotalus adamanteus venom displayed a procoagulant activity associated with weak clot strength (no factor XIII activation) similar to thrombin-like enzymes. The procoagulant activity was not modified in the presence of reduced glutathione, demonstrating that the procoagulant activity was likely due to deamination, and not hydrogen peroxide generation by the LAAO. Further, unlike the raw venom of the same species, the purified LAAO was not inhibited by carbon monoxide releasing molecule-2 (CORM-2). Lastly, exposure of the enzyme to phenylmethylsulfonyl fluoride (PMSF) resulted in the LAAO expressing anticoagulant activity, preventing contact activation generated thrombin from forming a clot. In sum, this investigation for the first time characterized the LAAO of a snake venom as both a fibrinogen polymerizing and an anticoagulant enzyme acting via oxidative deamination and not proteolysis as is the case with thrombin-like enzymes (e.g., serine proteases). Using this thrombelastographic approach, future investigation of purified enzymes can define their biochemical nature.
    Note
    Open access journal
    ISSN
    1422-0067
    PubMed ID
    31574907
    DOI
    10.3390/ijms20194853
    Version
    Final published version
    ae974a485f413a2113503eed53cd6c53
    10.3390/ijms20194853
    Scopus Count
    Collections
    UA Faculty Publications

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