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The Procoagulant Snake Venom Serine Protease Potentially Having a Dual, Blood Coagulation Factor V and X-Activating Activity.

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  • Additional Information
    • Source:
      Publisher: MDPI Country of Publication: Switzerland NLM ID: 101530765 Publication Model: Electronic Cited Medium: Internet ISSN: 2072-6651 (Electronic) Linking ISSN: 20726651 NLM ISO Abbreviation: Toxins (Basel) Subsets: MEDLINE
    • Publication Information:
      Original Publication: Basel : MDPI
    • Subject Terms:
      Viperidae*; Blood Coagulation/*drug effects ; Coagulants/*pharmacology ; Factor Va/*metabolism ; Factor Xa/*metabolism ; Serine Proteases/*pharmacology ; Viper Venoms/*enzymology; Amino Acid Sequence ; Animals ; Coagulants/chemistry ; Coagulants/metabolism ; Humans ; Protein Conformation ; Serine Proteases/chemistry ; Serine Proteases/metabolism ; Structure-Activity Relationship
    • Abstract:
      A procoagulant snake venom serine protease was isolated from the venom of the nose-horned viper ( Vipera ammodytes ammodytes ). This 34 kDa glycoprotein, termed Vaa SP-VX, possesses five kDa N-linked carbohydrates. Amino acid sequencing showed Vaa SP-VX to be a chymotrypsin-like serine protease. Structurally, it is highly homologous to Vaa SP-6 from the same venom and to nikobin from the venom of Vipera nikolskii , neither of which have known functions. Vaa SP-VX does not affect platelets. The specific proteolysis of blood coagulation factors X and V by VaaSP-VX suggests that its blood-coagulation-inducing effect is due to its ability to activate these two blood coagulation factors, which following activation, combine to form the prothrombinase complex. Vaa SP-VX may thus represent the first example of a serine protease with such a dual activity, which makes it a highly suitable candidate to replace diluted Russell's viper venom in lupus anticoagulant testing, thus achieving greater reliability of the analysis. As a blood-coagulation-promoting substance that is resistant to serpin inhibition, Vaa SP-VX is also interesting from the therapeutic point of view for treating patients suffering from hemophilia.
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    • Grant Information:
      P1-0207 International Javna Agencija za Raziskovalno Dejavnost RS
    • Contributed Indexing:
      Keywords: FV activator; FX activator; procoagulant; serine protease; snake venom
    • Accession Number:
      0 (Coagulants)
      0 (Viper Venoms)
      65522-14-7 (Factor Va)
      EC 3.4.- (Serine Proteases)
      EC 3.4.21.6 (Factor Xa)
    • Publication Date:
      Date Created: 20200604 Date Completed: 20210303 Latest Revision: 20210303
    • Publication Date:
      20250114
    • Accession Number:
      PMC7354534
    • Accession Number:
      10.3390/toxins12060358
    • Accession Number:
      32485989