Falcón-Dieguez JE, Rodi P, Lores-Guevara MA, Gennaro AM

Language: Spanish
References: 24
Page: 13-20
PDF size: 155.34 Kb.

ABSTRACT

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.

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