Analysis of the red cell membrane in a family with hereditary elliptocytosis--total or partial of protein 4.1

• Published in: Human genetics Vol. 59; no. 1; p. 68
• Main Authors: Alloisio, N, Dorléac, E, Girot, R, Delaunay, J
• Format: Journal Article
• Language: English
• Published: Germany 01.01.1981
• Subjects: Ankyrins - chemistry; Child; Cytoskeletal Proteins; Electrophoresis, Polyacrylamide Gel; Elliptocytosis, Hereditary; Erythrocyte Membrane - chemistry; Erythrocytes - pathology; Female; Heterozygote; Humans; Male; Membrane Proteins - analysis; Neuropeptides; Phosphoproteins; Protein Binding; Talin - chemistry
• ISSN: 0340-6717
• DOI: 10.1007/BF00278857

In a 12-year-old boy carrying a clinically silent elliptocytosis, we observed a total lack of red cell membrane band 4.1. Band 4.1 was partially absent in the father who also displayed a clinically silent elliptocytosis and, remarkably, in the mother although she presented normal discocytes. Band (2 and 2.1.) phosphorylation was sharply reduced in the three persons examined. In the propositus and his mother, but not in his father, a clearly phosphorylated band appeared at the level of band 4.2. We suggest that the father and the mother carry two distinct alleles affecting differently the interactions within the spectrin-actin protein 4.1 complex. The father's allele is elliptocytogenic in the heterozygous state and, among other molecular alterations, prevents the attachment of protein 4.1. The mother's allele is morphologically silent in the heterozygous state, yet it also affects the binding of protein 4.1, possibly because the latter is shortened. The propositus, being doubly heterozygous, has the same morphological phenotype as his father, but his protein 4.1 electrophoretic phenotype is the addition of both parental phenotypes. The distinct phosphorylation patterns in the region of bands 4.1 and 4.2 are also consistent with the two-allele hypothesis.