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Snake venom metalloproteinases (SVMPs) play an important role in local tissue damage of snakebite patients, mostly by hydrolysis of basement membrane (BM) components. We evaluated the proinflammatory activity of SVMPs Atroxlysin-Ia (ATXL) and Batroxrhagin (BATXH) from Bothrops atrox venom and their hydrolysis products of Matrigel. BALB/c mice were injected with SVMPs (2 μg), for assessment of paw edema and peritoneal leukocyte accumulation. Both SVMPs induced edema, representing an increase of ~70% of the paw size. Leukocyte infiltrates reached levels of 6 × 106 with ATXL and 5 × 106 with BATXH. TNF-α was identified in the supernatant of BATXH—or venom-stimulated MPAC cells. Incubation of Matrigel with the SVMPs generated fragments, including peptides from Laminin, identified by LC–MS/MS. The Matrigel hydrolysis peptides caused edema that increased 30% the paw size and promoted leukocyte accumulation (4–5 × 106) to the peritoneal cavity, significantly higher than Matrigel control peptides 1 and 4 h after injection. Our findings suggest that ATXL and BATXH are involved in the inflammatory reaction observed in B. atrox envenomings by direct action on inflammatory cells or by releasing proinflammatory peptides from BM proteins that may amplify the direct action of SVMPs through activation of endogenous signaling pathways.
Michelle Teixeira De Almeida; Luciana Aparecida Freitas-De-Sousa; Monica Colombini; Sarah Gimenes; Eduardo S. Kitano; Eliana L. Faquim-Mauro; Solange M. T. Serrano; Ana Maria Moura-Da-Silva. Inflammatory Reaction Induced by Two Metalloproteinases Isolated from Bothrops atrox Venom and by Fragments Generated from the Hydrolysis of Basement Membrane Components. Toxins 2020, 12, 96 .
AMA StyleMichelle Teixeira De Almeida, Luciana Aparecida Freitas-De-Sousa, Monica Colombini, Sarah Gimenes, Eduardo S. Kitano, Eliana L. Faquim-Mauro, Solange M. T. Serrano, Ana Maria Moura-Da-Silva. Inflammatory Reaction Induced by Two Metalloproteinases Isolated from Bothrops atrox Venom and by Fragments Generated from the Hydrolysis of Basement Membrane Components. Toxins. 2020; 12 (2):96.
Chicago/Turabian StyleMichelle Teixeira De Almeida; Luciana Aparecida Freitas-De-Sousa; Monica Colombini; Sarah Gimenes; Eduardo S. Kitano; Eliana L. Faquim-Mauro; Solange M. T. Serrano; Ana Maria Moura-Da-Silva. 2020. "Inflammatory Reaction Induced by Two Metalloproteinases Isolated from Bothrops atrox Venom and by Fragments Generated from the Hydrolysis of Basement Membrane Components." Toxins 12, no. 2: 96.
Jellyfish venoms are of medical and biotechnological importance, with toxins displaying antimicrobial, analgesic and anti-tumor activities. Although proteolytic enzymes have also been described, detailed characterisation of these proteins is scant in Olindias spp. High throughput mass spectrometry profiling of cnidarian venoms has become increasingly popular since the first description of the proteomic profile of putative toxins isolated from nematocysts of the hydrozoan jellyfish Olindias sambaquiensis describing the presence of orthologous enzymes as presented in venoms of advanced species as snakes. Rigorous bioinformatics analyses can aid functional annotation, but biochemical assays are prerequisite to unambiguously assign toxic function to a peptide or protein. Here we present results that experimentally confirm previously predicted proteomic analysis that crude venom extracts from tentacles of O. sambaquiensis are composed of polypeptides with metalloproteinase, serine proteinase and phospholipases A2 activities. Surprisingly, levels of serine proteinase and phospholipase A2 activities were comparable to those observed in venoms of Bothrops snakes which were used as positive controls in this study. Hence, these data offer new opportunities to explore serine proteinase and phospholipase A2 activities in the clinical sequelae following O. sambaquiensis envenomation, with future possible biopharmaceutical applications.
Paloma S. Knittel; Paul Long; Lucas Brammall; Antonio C. Marques; Michelle T. Almeida; Gabriel Padilla; Ana M. Moura-Da-Silva. Characterising the enzymatic profile of crude tentacle extracts from the South Atlantic jellyfish Olindias sambaquiensis (Cnidaria: Hydrozoa). Toxicon 2016, 119, 1 -7.
AMA StylePaloma S. Knittel, Paul Long, Lucas Brammall, Antonio C. Marques, Michelle T. Almeida, Gabriel Padilla, Ana M. Moura-Da-Silva. Characterising the enzymatic profile of crude tentacle extracts from the South Atlantic jellyfish Olindias sambaquiensis (Cnidaria: Hydrozoa). Toxicon. 2016; 119 ():1-7.
Chicago/Turabian StylePaloma S. Knittel; Paul Long; Lucas Brammall; Antonio C. Marques; Michelle T. Almeida; Gabriel Padilla; Ana M. Moura-Da-Silva. 2016. "Characterising the enzymatic profile of crude tentacle extracts from the South Atlantic jellyfish Olindias sambaquiensis (Cnidaria: Hydrozoa)." Toxicon 119, no. : 1-7.
Snake venom metalloproteinases (SVMPs) are abundant in the venoms of vipers and rattlesnakes, playing important roles for the snake adaptation to different environments, and are related to most of the pathological effects of these venoms in human victims. The effectiveness of SVMPs is greatly due to their functional diversity, targeting important physiological proteins or receptors in different tissues and in the coagulation system. Functional diversity is often related to the genetic diversification of the snake venom. In this review, we discuss some published evidence that posit that processing and post-translational modifications are great contributors for the generation of functional diversity and for maintaining latency or inactivation of enzymes belonging to this relevant family of venom toxins.
Ana M. Moura-Da-Silva; Michelle T. Almeida; José A. Portes-Junior; Carolina A. Nicolau; Francisco Gomes-Neto; Richard H. Valente. Processing of Snake Venom Metalloproteinases: Generation of Toxin Diversity and Enzyme Inactivation. Toxins 2016, 8, 183 .
AMA StyleAna M. Moura-Da-Silva, Michelle T. Almeida, José A. Portes-Junior, Carolina A. Nicolau, Francisco Gomes-Neto, Richard H. Valente. Processing of Snake Venom Metalloproteinases: Generation of Toxin Diversity and Enzyme Inactivation. Toxins. 2016; 8 (6):183.
Chicago/Turabian StyleAna M. Moura-Da-Silva; Michelle T. Almeida; José A. Portes-Junior; Carolina A. Nicolau; Francisco Gomes-Neto; Richard H. Valente. 2016. "Processing of Snake Venom Metalloproteinases: Generation of Toxin Diversity and Enzyme Inactivation." Toxins 8, no. 6: 183.