Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/93544
Type: Artigo de periódico
Title: Biological And Enzymatic Activities Of Micrurus Sp. (coral) Snake Venoms
Author: Cecchini A.L.
Marcussi S.
Silveira L.B.
Borja-Oliveira C.R.
Rodrigues-Simioni L.
Amara S.
Stabeli R.G.
Giglio J.R.
Arantes E.C.
Soares A.M.
Abstract: The venoms of Micrurus lemniscatus carvalhoi, Micrurus frontalis frontalis, Micrurus surinamensis surinamensis and Micrurus nigrocinctus nigrocinctus were assayed for biological activities. Although showing similar liposome disrupting and myotoxic activities, M. frontalis frontalis and M. nigrocinctus nigrocinctus displayed higher anticoagulant and phospholipase A2 (PLA 2) activities. The latter induced a higher edema response within 30 min. Both venoms were the most toxic as well. In the isolated chick biventer cervicis preparation, M. lemniscatus carvalhoi venom blocked the indirectly elicited twitch-tension response (85±0.6% inhibition after a 15 min incubation at 5 μg of venom/mL) and the response to acetylcholine (ACh; 55 or 110 μM), without affecting the response to KCl (13.4 mM). In mouse phrenic nerve-diaphragm preparation, the venom (5 μg/mL) produced a complete inhibition of the indirectly elicited contractile response after 50 min incubation and did not affect the contractions elicited by direct stimulation. M. lemniscatus carvalhoi inhibited 3H-l-glutamate uptake in brain synaptosomes in a Ca2+-, but not time, dependent manner. The replacement of Ca2+ by Sr2+ and ethylene glycol-bis(β-aminoethyl ether) (EGTA), or alkylation of the venom with p-bromophenacyl bromide (BPB), inhibited 3H-l-glutamate uptake. M. lemniscatus carvalhoi venom cross-reacted with postsynaptic α-neurotoxins short-chain (antineurotoxin-II) and long-chain (antibungarotoxin) antibodies. It also cross-reacted with antimyotoxic PLA2 antibodies from M. nigrocinctus nigrocinctus (antinigroxin). Our results point to the need of catalytic activity for these venoms to exert their neurotoxic activity efficiently and to their components as attractive tools for the study of molecular targets on cell membranes. © 2004 Elsevier Inc. All rights reserved.
Editor: 
Rights: fechado
Identifier DOI: 10.1016/j.cbpb.2004.11.012
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-19944434170&partnerID=40&md5=e2a536785db4a4b81aeff02a49e0cea0
Date Issue: 2005
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File Description SizeFormat 
2-s2.0-19944434170.pdf358.94 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.