Show simple item record

dc.creatorDíaz Oreiro, Cecilia
dc.creatorLeón Montero, Guillermo
dc.creatorRucavado Romero, Alexandra
dc.creatorRojas Campos, Norman
dc.creatorSchroit, Alan J.
dc.creatorGutiérrez, José María
dc.date.accessioned2017-02-02T14:36:08Z
dc.date.available2017-02-02T14:36:08Z
dc.date.issued2001-07-01
dc.identifier.citationhttp://www.sciencedirect.com/science/article/pii/S0003986101923860es_ES
dc.identifier.issn0003-9861
dc.identifier.urihttps://hdl.handle.net/10669/29479
dc.description.abstractCerrophidion (Bothrops) godmani myotoxins I (CGMT-I) and II (CGMT-II), Asp-49 and Lys-49 phospholipases A(2) (PLA2s), which drastically differ in enzymatic activity, were devoid of direct hemolytic effects on erythrocytes (RBC) from different species despite the fact that enzymatically active CGMT-I was able to hydrolyze RBC membrane phospholipids and disrupt liposomes prepared from RBC lipids. Human RBC did not become susceptible to the toxins after treatment with neuraminidase or after altering membrane fluidity with cholesterol or sublytic concentrations of detergent. Unlike normal RBC, significant hemolysis was induced by CGMT-II and another similar Lys-49 isoform, B. asper MT-II (BAMT-II), in RBC enriched with phosphatidylserine (PS). Hemolysis was greater in RBC preincubated with pyridyldithioethylamine (PDA), a potent inhibitor of aminophospholipid transport. RBC enriched with phosphatidic acid (PA) also became susceptible to the myotoxins but was unaffected by PDA. Cells enriched with phosphatidylcholine (PC) remained resistant to the action of the toxins. BAMT-II also induced damage in black lipid membranes prepared with PS but not PC alone. When RBC binding of BAMT-II was measured by enzyme-linked immunosorbent assay, it was observed that PS- and PA-enriched erythrocytes were always able to capture more toxin than normal and PC-enriched RBC. This effect was significantly improved by PDA (in the case of PS) and it was observed either in the presence or in the absence of calcium in the medium. These data suggest that negatively charged lipids in the outer leaflet of cell membranes constitute myotoxic PLA2 binding sites. The scarcity of anionic phospholipids in the outer leaflet of RBC could explain their resistance to the action of these PLA2s.es_ES
dc.description.sponsorshipInternational Foundation for Science//IFS/Sueciaes_ES
dc.description.sponsorshipUniversidad de Costa Rica//UCR/Costa Ricaes_ES
dc.language.isoen_USes_ES
dc.sourceArchives of Biochemistry and Biophysics; Volumen 391, Número 1. 2001es_ES
dc.subjectAnimalses_ES
dc.subjectBothropses_ES
dc.subjectCell Membranees_ES
dc.subjectCrotalid Venomses_ES
dc.subjectErythrocyteses_ES
dc.subjectGroup II Phospholipases A2es_ES
dc.subjectHumanses_ES
dc.subjectLipid Bilayerses_ES
dc.subjectLiposomeses_ES
dc.subjectMembrane Fluidityes_ES
dc.subjectNeuraminidasees_ES
dc.subjectNeurotoxinses_ES
dc.subjectPhospholipases Aes_ES
dc.subjectPhospholipases A2es_ES
dc.subjectPhospholipidses_ES
dc.subjectReptilian Proteinses_ES
dc.subjectSpecies Specificityes_ES
dc.titleModulation of the Susceptibility of Human Erythrocytes to Snake Venom Myotoxic Phospholipases A2: Role of Negatively Charged Phospholipids as Potential Membrane Binding Siteses_ES
dc.typeartículo científicoes_ES
dc.identifier.doi10.1006/abbi.2001.2386
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.pmid11414685


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record