title: Inhibition of enzymatic and pharmacological activities of some snake venoms and toxins by Mandevilla velutina (Apocynaceae) aqueous extract.
abstract: Phospholipases A(2) (PLA(2)) are multifunctional proteins which exhibit varied biological activities correlated to the structural diversities of the sub-classes. The crude aqueous extract from subterranean system of Mandevilla velutina, a plant found in Brazilian savanna, was assayed for its ability to inhibit biological activities of several snake venoms and isolated PLA(2)s. The extract induced total inhibition of the phospholipase activity of Crotalus durissus terrificus venom and only partial inhibition of Bothrops venoms. When assayed against purified toxins, the highest efficacy was detected against CB and crotoxin, while almost ineffective against PLA(2)s from the genus Bothrops. Although M. velutina crude extract significantly inhibited the myotoxic activity of C. d. terrificus venom and CB, it produced only partial inhibition of either Bothrops jararacussu venom or its main myotoxins BthTX-I (basic Lys49), BthTX-II (basic Asp49) and BthA-I-PLA(2) (acidic Asp49). The extract exhibited also full inhibition of hemorrhage caused by Bothrops alternatus, Bothrops moojeni and Bothrops pirajai snake venoms, but partial inhibition (90%) of that induced by B. jararacussu venom. The extract was ineffective to inhibit the fibrinogenolytic activity of B. moojeni, B. alternatus and B. pirajai crude venoms, while their caseinolytic activity was only partially inhibited. No inhibition of the anticoagulant activity, although partial reduction of the edema-inducing activity of C. d. terrificus and B. alternatus crude venoms, CB, PrTX-I, BthTX-I and crotoxin was observed. Besides extending survival of mice injected with lethal doses of C. d. terrificus and B. jararacussu venoms, M. velutina extract decreased to 50% the lethality of mice. Extracts of 18 month old micropropagated plants were able to partially neutralize the effect of the crude venoms and toxins.
authors.affiliation: Unidade de Biotecnologia, Universidade de Ribeirão Preto UNAERP, Bloco A, Avenida Costábile Romano 2201, CEP 14096 380 Ribeirão Preto, SP, Brazil.
authors.forename: Ronaldo
authors.initials: R
authors.lastname: Biondo
authors.forename: Ana Maria S
authors.initials: AM
authors.lastname: Pereira
authors.forename: Silvana
authors.initials: S
authors.lastname: Marcussi
authors.forename: Paulo S
authors.initials: PS
authors.lastname: Pereira
authors.forename: Suzelei C
authors.initials: SC
authors.lastname: França
authors.forename: Andreimar M
authors.initials: AM
authors.lastname: Soares
mesh_terms: D000818:Animals; D029062:Apocynaceae / Q000737:chemistry* / Q000145:classification; D017837:Bothrops; D003435:Crotalid Venoms / Q000037:antagonists & inhibitors / Q000201:enzymology / Q000633:toxicity; D017839:Crotalus; D004487:Edema / Q000139:chemically induced; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D008297:Male; D051379:Mice; D018482:Muscle, Skeletal / Q000187:drug effects / Q000473:pathology; D010741:Phospholipases A / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000633:toxicity; D010936:Plant Extracts / Q000737:chemistry / Q000494:pharmacology*; D014757:Viper Venoms / Q000037:antagonists & inhibitors* / Q000201:enzymology / Q000633:toxicity*
chemical_list: D003435:Crotalid Venoms; D004791:Enzyme Inhibitors; D010936:Plant Extracts; D014757:Viper Venoms; D010741:Phospholipases A