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  • Title: Defective organization of the erythroid cell membrane in a novel case of congenital anemia.
    Author: Antonelou MH, Papassideri IS, Karababa FJ, Stravopodis DJ, Loutradi A, Margaritis LH.
    Journal: Blood Cells Mol Dis; 2003; 30(1):43-54. PubMed ID: 12667986.
    Abstract:
    In the present paper, we demonstrate the erythroid cell membrane unique properties in a previously characterized case of hemoglobin-H disease, associated with congenital dyserythropoietic anemia type-I features. In order to explain the patient's cell membrane distortions and the high affinity for the various intracellular inclusions, we studied its composition and structure in comparison to other anemic and non-anemic cases. Red cells from peripheral blood were fractionated into cellular, membrane and protein extracts. Membrane attached immunocomplexes were separated and collected by immunoprecipitation. The subcellular fractions were analyzed by SDS-PAGE electrophoresis and immunoblotted against a variety of erythroid-specific antibodies. The protein composition of the membrane was characterized by immunogold electron microscopy. In the membrane of the CDA-associated case, we identified sialic acid and protein deficiencies, formation of protein crosslinkings, excesses of bound globin and immunoglobulins and aberrant peptides. In contrast to the typical hemoglobin-H disease, the ghost-bound globin exhibited preferential attachment to the skeletal proteins than the band 3 and the skeleton-bound globin consisted not only of beta- but also of alpha-globin chains. Another hallmark, probably associated with the CDA defect, was the participation of glycophorins in the membrane-bound immunocomplexes and the pathological clustering of the latter in the membrane. This study strongly suggests that the result of the combinatorial effects on the diseased membrane created a unique profile, quite distinct from the one observed in several typical hemoglobinopathies. Our observations shed light into critical membrane alterations leading to hemolysis in the novel CDA-associated disease and probably into the CDA-I or CDA-I-like diseases.
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