Show simple item record

dc.creatorLizano González, Sergio
dc.creatorAngulo Ugalde, Yamileth
dc.creatorLomonte, Bruno
dc.creatorFox, Jay W.
dc.creatorLambeau, Gérard
dc.creatorLazdunski, Michel
dc.creatorGutiérrez, José María
dc.date.accessioned2017-01-24T17:55:48Z
dc.date.available2017-01-24T17:55:48Z
dc.date.issued2000-03-15
dc.identifier.citationhttp://www.biochemj.org/content/346/3/631es_ES
dc.identifier.issn1470-8728
dc.identifier.issn0264-6021
dc.identifier.urihttp://hdl.handle.net/10669/29461
dc.description.abstractMyotoxic phospholipases A2 (PLA2s; group II) account for most of the muscle-tissue damage that results from envenomation by viperid snakes. In the venom of the Godman's viper (Cerrophidion godmani, formerly Bothrops godmani), an enzymically active PLA2 (myotoxin I) and an inactive, Lys-49 variant (myotoxin II) induce extensive muscle damage and oedema. In this study, two distinct myotoxin inhibitor proteins of C. godmani, CgMIP-I and CgMIP-II, were purified directly from blood plasma by selective binding to affinity columns containing either myotoxin I or myotoxin II, respectively. Both proteins are glycosylated, acidic (pI = 4) and composed of 20-25-kDa subunits that form oligomers of 110 kDa (CgMIP-I) or 180 kDa (CgMIP-II). In inhibition studies, CgMIP-I specifically neutralized the PLA2 and the myotoxic, oedema-forming and cytolytic activities of myotoxins I, whereas CgMIP-II selectively inhibited the toxic properties of myotoxin II. N-terminal amino acid sequence analysis and sequencing of cDNAs encoding the two inhibitors revealed that CgMIP-I is similar to γ-type inhibitors, which share a pattern of cysteine residues present in the Ly-6 superfamily of proteins, whereas CgMIP-II shares sequence identity with α-type inhibitors that contain carbohydrate-recognition-like domains, also found in C-type lectins and mammalian PLA2 receptors. N-terminal sequencing of myotoxin I revealed a different primary structure from myotoxin II [De Sousa, Morhy, Arni, Ward, Díaz and Gutiérrez (1998) Biochim. Biophys. Acta 1384, 204-208], which provides insight into the nature of such pharmacological specificity.es_ES
dc.description.sponsorshipUniversidad de Costa Rica/[742-99-219]/UCR/Costa Ricaes_ES
dc.description.sponsorshipUniversidad de Costa Rica/[741-98-211]/UCR/Costa Ricaes_ES
dc.description.sponsorshipIternational Foundation for Science/[F/2485-2]/IFS/Sueciaes_ES
dc.description.sponsorshipIternational Foundation for Science/[F/2766-1]/IFS/Sueciaes_ES
dc.description.sponsorshipConsejo Nacional de Investigaciones Científicas y Tecnológicas/[98-013-F0]/CONICIT/Costa Ricaes_ES
dc.description.sponsorshipCentre National pour la Recherche Scientifique//CNRS/Franciaes_ES
dc.language.isoen_USes_ES
dc.sourceBiochemical Journal; Volumen 346, Número 3. 2000es_ES
dc.subjectCarbohydrate-recognition Domaines_ES
dc.subjectCrotalinaees_ES
dc.subjectMyotoxicityes_ES
dc.subjectThree-finger Domaines_ES
dc.subjectToxin Inhibitores_ES
dc.subjectSnake venomes_ES
dc.titleTwo phospholipase A2 inhibitors from the plasma of Cerrophidion (Bothrops) godmani which selectively inhibit two different group-II phospholipase A2 myotoxins from its own venom: isolation, molecular cloning and biological propertieses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1042/bj3460631
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.codproyecto741-98-211
dc.identifier.codproyecto742-99-219


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record