
handle: 11336/37783
En la anemia drepanocítica ha sido previamente documentada una anormal interacción hemoglobina-membrana. Sin embargo, no se conoce cómo se modifica ésta durante el proceso de polimerización de la hemoglobina S. En este trabajo empleamos un modelo de eritrocitos reconstituidos a partir de membranas fantasmas cuyas proteínas del citoesqueleto se marcaron con el marcador de espín 4-maleimido Tempo y posteriormente se resellaron con hemoglobina S o hemoglobina A. Estudiamos la variación temporal del parámetro espectral W/S, indicativo del estado conformacional de las proteínas del citoesqueleto, principalmente de la espectrina, a fin de detectar los eventuales efectos debidos al proceso de polimerización por desoxigenación espontánea. Las diferencias observadas en los comportamientos de la variación temporal de W/S en eritrocitos reconstituidos con ambas hemoglobinas fueron consideradas como evidencia experimental de un incremento de la interacción hemoglobina S-membrana como resultado del proceso de polimerización de la hemoglobina S bajo condiciones de desoxigenación espontánea.
An enhanced hemoglobin-membrane association has been previously documented in the sickle cell disease. However, it is not known how this interaction is modified during the hemoglobin S polymerization process. In this work, we use a model of reconstituted erythrocytes from ghost membranes whose cytoskeleton proteins were labelled with the 4-maleimido Tempo spin label, and that were subsequently resealed with haemoglobin S or A. We studied the time dependence of the spectral W/S parameter, indicative of the conformational state of cytoskeleton proteins (mainly spectrin), with the aim of detecting the eventual effects due to hemoglobin S polymerization. The differences observed in the temporal behavior of W/S in erythrocytes reconstituted with both hemoglobins were considered as experimental evidence of an increment in hemoglobin S-membrane interaction, as a result of the hemoglobin S polymerization process under spontaneous deoxygenation.
Fil: Rodi, Pablo Marcelo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina
Fil: Gennaro, Ana Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina
Fil: Falcón Dieguez, J.E.. Universidad de Oriente; Cuba
Fil: Lores Guevara, M.A.. Universidad de Oriente; Cuba
Polimerización Hemoglobina S, https://purl.org/becyt/ford/1.6, Eritrocitos Reconstituidos, Hemoglobina-Membrana, https://purl.org/becyt/ford/1, 4-Maleimido Tempo
Polimerización Hemoglobina S, https://purl.org/becyt/ford/1.6, Eritrocitos Reconstituidos, Hemoglobina-Membrana, https://purl.org/becyt/ford/1, 4-Maleimido Tempo
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