Biochemical and biological characterization of the venoms of Bothriopsis bilineata and Bothriopsis taeniata (Serpentes: Viperidae)
Snake venom is a complex mixture containing diverse protein components with different structures and functions that are used for prey immobilization and death. Snake venoms from the family Viperidae cause pronounced local and systemic effects, such as pain, edema, hemorrhage and necrosis. Here, we i...
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| Published in | Toxicon (Oxford) Vol. 50; no. 2; pp. 270 - 277 |
|---|---|
| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
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Oxford
Elsevier Ltd
01.08.2007
Elsevier Science |
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| Abstract | Snake venom is a complex mixture containing diverse protein components with different structures and functions that are used for prey immobilization and death. Snake venoms from the family Viperidae cause pronounced local and systemic effects, such as pain, edema, hemorrhage and necrosis. Here, we investigated the enzymatic and biological activities of venoms from two Amazonian snakes,
Bothriopsis bilineata and
Bothriopsis taeniata. Both venoms presented high enzymatic activities for proteases kallikrein, thrombin and plasmin, low levels of trypsin, cathepsin C and leucine aminopeptidase activities, while lacked acetylcholinesterase activity.
B. taeniata and
B. bilineata crude venoms caused inflammation inducing neutrophil recruitment into peritoneal cavity of mice 4
h after injection. Neutrophil recruitment induced by
B. taeniata venom was accompanied by hemorrhage. EDTA treatment profoundly impaired neutrophil recruitment, suggesting the involvement of a metalloproteinase on venoms-induced neutrophil recruitment. Pretreatment with dexamethasone and zileuton, a 5-lipoxygenase inhibitor, significantly reduced neutrophil migration, but indomethacin and montelukast, a cysteinyl leukotriene receptor antagonist, had no effect, suggesting the involvement of lipoxygenase-derived metabolites, probably LTB
4. Together, these results show that
B. bilineata and
B. taeniata venoms induce a marked inflammatory reaction, with leukocyte recruitment, and hemorrhage, which parallels to a high proteolytic activity found in these venoms. |
|---|---|
| AbstractList | Snake venom is a complex mixture containing diverse protein components with different structures and functions that are used for prey immobilization and death. Snake venoms from the family Viperidae cause pronounced local and systemic effects, such as pain, edema, hemorrhage and necrosis. Here, we investigated the enzymatic and biological activities of venoms from two Amazonian snakes,
Bothriopsis bilineata and
Bothriopsis taeniata. Both venoms presented high enzymatic activities for proteases kallikrein, thrombin and plasmin, low levels of trypsin, cathepsin C and leucine aminopeptidase activities, while lacked acetylcholinesterase activity.
B. taeniata and
B. bilineata crude venoms caused inflammation inducing neutrophil recruitment into peritoneal cavity of mice 4
h after injection. Neutrophil recruitment induced by
B. taeniata venom was accompanied by hemorrhage. EDTA treatment profoundly impaired neutrophil recruitment, suggesting the involvement of a metalloproteinase on venoms-induced neutrophil recruitment. Pretreatment with dexamethasone and zileuton, a 5-lipoxygenase inhibitor, significantly reduced neutrophil migration, but indomethacin and montelukast, a cysteinyl leukotriene receptor antagonist, had no effect, suggesting the involvement of lipoxygenase-derived metabolites, probably LTB
4. Together, these results show that
B. bilineata and
B. taeniata venoms induce a marked inflammatory reaction, with leukocyte recruitment, and hemorrhage, which parallels to a high proteolytic activity found in these venoms. Snake venom is a complex mixture containing diverse protein components with different structures and functions that are used for prey immobilization and death. Snake venoms from the family Viperidae cause pronounced local and systemic effects, such as pain, edema, hemorrhage and necrosis. Here, we investigated the enzymatic and biological activities of venoms from two Amazonian snakes, Bothriopsis bilineata and Bothriopsis taeniata. Both venoms presented high enzymatic activities for proteases kallikrein, thrombin and plasmin, low levels of trypsin, cathepsin C and leucine aminopeptidase activities, while lacked acetylcholinesterase activity. B. taeniata and B. bilineata crude venoms caused inflammation inducing neutrophil recruitment into peritoneal cavity of mice 4h after injection. Neutrophil recruitment induced by B. taeniata venom was accompanied by hemorrhage. EDTA treatment profoundly impaired neutrophil recruitment, suggesting the involvement of a metalloproteinase on venoms-induced neutrophil recruitment. Pretreatment with dexamethasone and zileuton, a 5-lipoxygenase inhibitor, significantly reduced neutrophil migration, but indomethacin and montelukast, a cysteinyl leukotriene receptor antagonist, had no effect, suggesting the involvement of lipoxygenase-derived metabolites, probably LTB sub(4). Together, these results show that B. bilineata and B. taeniata venoms induce a marked inflammatory reaction, with leukocyte recruitment, and hemorrhage, which parallels to a high proteolytic activity found in these venoms. Snake venom is a complex mixture containing diverse protein components with different structures and functions that are used for prey immobilization and death. Snake venoms from the family Viperidae cause pronounced local and systemic effects, such as pain, edema, hemorrhage and necrosis. Here, we investigated the enzymatic and biological activities of venoms from two Amazonian snakes, Bothriopsis bilineata and Bothriopsis taeniata. Both venoms presented high enzymatic activities for proteases kallikrein, thrombin and plasmin, low levels of trypsin, cathepsin C and leucine aminopeptidase activities, while lacked acetylcholinesterase activity. B. taeniata and B. bilineata crude venoms caused inflammation inducing neutrophil recruitment into peritoneal cavity of mice 4h after injection. Neutrophil recruitment induced by B. taeniata venom was accompanied by hemorrhage. EDTA treatment profoundly impaired neutrophil recruitment, suggesting the involvement of a metalloproteinase on venoms-induced neutrophil recruitment. Pretreatment with dexamethasone and zileuton, a 5-lipoxygenase inhibitor, significantly reduced neutrophil migration, but indomethacin and montelukast, a cysteinyl leukotriene receptor antagonist, had no effect, suggesting the involvement of lipoxygenase-derived metabolites, probably LTB(4). Together, these results show that B. bilineata and B. taeniata venoms induce a marked inflammatory reaction, with leukocyte recruitment, and hemorrhage, which parallels to a high proteolytic activity found in these venoms. |
| Author | Fin, Cyntia A. Alves, Letícia S. Thiesen, Flavia V. Renner, Márcia F. Bozza, Marcelo T. Dutra, Tatiana P. Porto, Bárbara N. Telli, Caliandra A. |
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| Keywords | Neutrophil migration Enzymes Pharmacological mediators Bothriopsis bilineata Bothriopsis taeniata Snake venoms Enzyme Animal origin Viperidae Ophidia Characterization Vertebrata Bothriopsis hilineata Venom Reptilia Neutrophil |
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Haemost. doi: 10.1055/s-0038-1646781 contributor: fullname: Nahas |
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| SubjectTerms | Animal poisons toxicology. Antivenoms Animals Biological and medical sciences Bothriopsis bilineata Bothriopsis taeniata Bothrops - physiology Cell Movement - drug effects Crotalid Venoms - chemistry Crotalid Venoms - enzymology Crotalid Venoms - toxicity Edetic Acid - pharmacology Enzymes Freeze Drying Inflammation - pathology Medical sciences Mice Mice, Inbred C57BL Neutrophil Infiltration - drug effects Neutrophil migration Neutrophils - drug effects Pharmacological mediators Serpentes Snake venoms South America Species Specificity Toxicology Viperidae |
| Title | Biochemical and biological characterization of the venoms of Bothriopsis bilineata and Bothriopsis taeniata (Serpentes: Viperidae) |
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