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PMID: 10819025 Published · ppublish English Case Reports Journal Article Research Support, Non-U.S. Gov't

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

Human genetics ·Vol. 59 ·No. 1 ·1981-00-00 ·Pages 68-71

Alloisio N, Dorléac E, Girot R, Delaunay J

Abstract

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.

MeSH Terms
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
Chemicals
ANK1 protein, human Ankyrins Cytoskeletal Proteins Membrane Proteins Neuropeptides Phosphoproteins Talin erythrocyte membrane band 4.1 protein erythrocyte membrane protein band 4.1-like 1
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Alloisio N
Laboratoire de Chimie Biologique, Faculté de Médecine Grange Blanche, Lyon, France.
Dorléac E
Girot R
Delaunay J
References (16)
16 references, click to expand
  1. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane.
    Biochemistry. 1971 Jun 22;10(13):2606-17 PMID: 4326772
  2. The erythrocyte membrane abnormality of hereditary spherocytosis.
    Br J Haematol. 1977 Nov;37(3):305-10 PMID: 146514
  3. Phosphorylation in erythrocyte membranes from abnormally shaped cells.
    Blood. 1976 Dec;48(6):877-86 PMID: 187264
  4. Associations of erythrocyte membrane proteins. Binding of purified bands 2.1 and 4.1 to spectrin.
    J Biol Chem. 1980 Jul 25;255(14):7034-9 PMID: 6771281
  5. Dissecting the red cell membrane skeleton.
    Nature. 1979 Oct 11;281(5731):426-9 PMID: 573863
  6. Phosphorylation of endogenous substrates by erythrocyte membrane protein kinases. I. A monovalent cation-stimulated reaction.
    Biochemistry. 1974 Dec 31;13(27):5507-14 PMID: 4457110
  7. Marked reduction of spectrinin hereditary spherocytosis in the common house mouse.
    Blood. 1978 Jun;51(6):1149-55 PMID: 647119
  8. The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes.
    Arch Biochem Biophys. 1963 Jan;100:119-30 PMID: 14028302
  9. Spectrin-actin membrane skeleton of normal and abnormal red blood cells.
    Semin Hematol. 1979 Jan;16(1):21-51 PMID: 370983
  10. The molecular lesion of hereditary spherocytosis (HS): a continuing enigma.
    Blood. 1977 Feb;49(2):241-5 PMID: 831876
  11. Purification of two spectrin-binding proteins: biochemical and electron microscopic evidence for site-specific reassociation between spectrin and bands 2.1 and 4.1.
    Proc Natl Acad Sci U S A. 1979 Oct;76(10):5192-6 PMID: 291934
  12. Properties of a non-specific nucleotidase in the membrane of rabbit red cells.
    Biochim Biophys Acta. 1978 Dec 8;527(2):425-31 PMID: 728445
  13. Erythrocyte protein phosphorylation.
    J Biol Chem. 1973 Feb 25;248(4):1408-11 PMID: 4346955
  14. Proteins of the camel erythrocyte membrane.
    Biochim Biophys Acta. 1975 Aug 5;401(1):83-94 PMID: 1096959
  15. Protein measurement with the Folin phenol reagent.
    J Biol Chem. 1951 Nov;193(1):265-75 PMID: 14907713
  16. Structural characterization of the phosphorylation sites of human erythrocyte spectrin.
    J Biol Chem. 1980 Dec 10;255(23):11512-20 PMID: 7440554
Article Info
Journal
Human genetics
Abbr.
Hum Genet
ISSN
0340-6717
Published
1981-00-00
Pages
68-71
Language
English
Region
Germany
NLM ID
7613873
Subset
IM
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