Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/79631
Type: Artigo de periódico
Title: Structural and biological characterization of a crotapotin isoform isolated from Crotalus durissus cascavella venom
Author: de Oliveira, DG
Toyama, MH
Martins, AMC
Havt, A
Nobre, ACL
Marangoni, S
Camara, PR
Antunes, E
de Nucci, G
Beliam, LOS
Fonteles, MC
Monteiro, HSA
Abstract: Envenoming by Crotalus durissus subspecies leads to coagulation disorders, myotoxicity, neurotoxicity and acute renal failure. The most serious systemic alteration and primary cause of death after snakebite is acute renal failure. In this work, we isolated crotapotin, an acid component (Crtp) of crotoxin from Crotalus durissus cascavella venom and we investigated its bactericidal and pro-inflammatory activities as well as its renal effects in rat isolated perfused kidneys. Crtp was bactericidal to the Gram-negative species Xanthomonas axonopodis pv. passiflorae, but was less effective against the Gram-positive Claribacteri ssp, probably because of differences in the cell wall composition. Crtp showed a high amino acid sequence homology with other Crtps described in the literature (around of 90%) and its A and B chains had high conserved regions corresponding to the calcium-binding loop, catalytic site and helix 3 of PLA(2). The Crtp showed moderate pro-inflammatory activity and increased significantly the inflammation evoked by PLA(2) when co-injected or co-incubated with PLA(2). The renal parameters evaluated included the perfusion pressure (PP), renal vascular resistance (RVR), urinary flow (UF), glomerular filtration rate (GFR) and percent of sodium tubular transport (%TNa+). Crotapotin (5 mug/ml) significantly increased the PP and RVR, whereas the GFR, UF and %TNa+ were unaffected. These results suggest that crotoxin is the main venom component responsible for nephrotoxicity and crotapotin contributes little to this phenomenom. The biological and bactericidal actions of Crtp also suggest that this protein may have functions other than simply acting as a chaperone for PLA(2). (C) 2003 Elsevier Science Ltd. All rights reserved.
Subject: Crotalus durissus cascavella
Crotapotin isoform
PLA(2)
venom
rattlesnake
neurotoxins
Country: Inglaterra
Editor: Pergamon-elsevier Science Ltd
Rights: fechado
Identifier DOI: 10.1016/S0041-0101(03)00100-4
Date Issue: 2003
Appears in Collections:Unicamp - Artigos e Outros Documentos

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