Fibrin(ogen)olytic enzymes in scorpion (Tityus discrepans) venom

• Published in: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 2014-02, Vol.168, p.62-69
• Main Authors: Brazón, Josmary, Guerrero, Belsy, D'Suze, Gina, Sevcik, Carlos, Arocha-Piñango, Carmen L.
• Format: Article
• Language: English
• Subjects: Animals; Buthidae; Fibrin - metabolism; Fibrino(geno)lytic activity; Fibrinogen; Metalloproteases - metabolism; Scorpion venom; Scorpion Venoms - enzymology; Scorpions - enzymology; Serine Proteases - metabolism; Tityus discrepans; α-Fibrinogenases
• ISSN: 1096-4959; 1879-1107
• DOI: 10.1016/j.cbpb.2013.11.007

Several fibrin(ogen)olytic enzymes from Tityus discrepans (Buthidae, Buthoidea) venom (TdV) were partially purified on a Sephadex G-50 column, by affinity and molecular exclusion high-performance chromatography. Fractions SB1-I and SB1-II had fibrinolytic, fibrinogenolytic (Aα-chains degradation) and tissue plasminogen activator (t-PA)-like activities. SB1-III was only fibrinogenolytic (fast degradation of Aα-chains and slower degradation of fibrinogen Bβ-chains). These results showed the presence of α-fibrinogenases in TdV. The fibrino(geno)lytic activity in these fractions was abolished by metalloprotease inhibitors (MPI). Fractions SB3-I and SB3-II contain fibrinogenolytic (Aα-chains degradation) and fibronectinolytic activities. Also fraction SB3-I had a t-PA-like activity. Activities in SB3-I and SB3-II were abolished by serine protease inhibitors (SPI). None of the fractions degraded fibrinogen γ-chains. Fibrinogen degradation by active fractions is associated with an anticoagulant effect supported by a reduced coagulant activity. The overall outcome suggests that metalloproteases and serine proteases in TdV are responsible for fibrin(ogen)olytic activity because MPI and SPI inhibited these activities.