Alternative titles; symbols
HGNC Approved Gene Symbol: SPTB
SNOMEDCT: 9434008;
Cytogenetic location: 14q23.3 Genomic coordinates (GRCh38): 14:64,746,283-64,879,907 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 14q23.3 | Anemia, neonatal hemolytic, fatal or near-fatal | 617948 | 3 | |
| Elliptocytosis-3 | 617948 | 3 | ||
| Spherocytosis, type 2 | 616649 | Autosomal dominant | 3 |
Winkelmann et al. (1988) cloned the SPTB gene; they estimated the size of the mRNA to be 7.5 kb. Prchal et al. (1987) showed that the reticulocyte beta-spectrin mRNA is 7.8 kb long.
Winkelmann et al. (1990) sequenced overlapping cDNA clones for the entire coding sequence of beta-spectrin. The sequence encodes a 2,137-amino acid, 246-kD protein, consisting of 3 domains: domain I, at the N-terminus, is a 272-amino acid region lacking resemblance to the spectrin repetitive motif but showing striking homology at both nucleotide and amino acid levels to the N-terminal 'actin-binding' domains of alpha-actinin (102575) and dystrophin (300377); domain II consists of 17 spectrin repeats; and domain III, 52 amino acid residues at the C terminus, does not adhere to the spectrin repeat motif.
Kimberling et al. (1978) had found linkage of hereditary spherocytosis with Gm type (determined by the IGHG locus, or loci, on chromosome 14q34; see 147100). In 15 families, the maximum lod score was 3.42 at a recombination fraction of 22%. With the evidence that one form of spherocytosis has a defect in beta-spectrin, this linkage information could be added to the evidence of location of beta-spectrin on chromosome 14. Watkins et al. (1987) mapped the beta-spectrin gene to chromosome 14 by use of a cDNA probe in somatic cell hybrids.
Prchal et al. (1987) reported the isolation and characterization of a human erythroid-specific beta-spectrin cDNA clone that encodes parts of the beta-9 through beta-12 repeat segments. They used this cDNA as a hybridization probe to assign the beta-spectrin gene to chromosome 14 by hybridization to a panel of nitrocellulose filters containing DNA from sorted human chromosomes. Closely linked RFLPs useful in the analysis of congenital hemolytic anemias were described.
Winkelmann et al. (1988) assigned the SPTB gene to chromosome 14 by hybridization to DNA from a well-characterized panel of mouse-human somatic cell hybrids (Winkelmann et al., 1987).
By in situ hybridization with an erythroid beta-spectrin cDNA, Forget et al. (1988) concluded that the beta-spectrin gene is located considerably proximal to the IGH locus (147100), at 14q22-q23.2.
Forget et al. (1988) observed a kindred in which at least 3 members showed recombination between hereditary spherocytosis and RFLPs defined by the beta-spectrin clone. In the same kindred, alpha-spectrin and protein 4.1 were also ruled out as sites of the mutation.
By in situ hybridization, Fukushima et al. (1990) concluded that the SPTB gene is located in 14q23-q24.2.
Laurila et al. (1987) mapped the beta-spectrin gene to mouse chromosome 12. Birkenmeier et al. (1988) showed that the erythroid beta-spectrin gene is tightly linked to the 'jaundiced' (ja) locus on mouse chromosome 12. This assignment was considered consistent with the hypothesis that the defect in this disorder is the result of a mutation in the beta-spectrin gene.
Spherocytosis Type 2
In a family reported by Wolfe et al. (1982) with spherocytosis type 2 (SPH2; 616649), Becker et al. (1993) identified a mutation in the SPTB gene (182870.0007).
Gallagher and Forget (1998) tabulated 19 mutations of the SPTB gene that cause hereditary spherocytosis.
Maciag et al. (2009) found that levels of SPTB mRNA were 20 to 80% lower in unrelated patients with hereditary spherocytosis compared to controls. Direct sequencing identified 5 different pathogenic mutations in the SPTB gene (see, e.g., 182870.0015). Affected members of 1 family showed 2 mutations, consistent with the greatest decrease (80%) in SPTB mRNA. Maciag et al. (2009) noted that SPTB mutations tend to be unique to each family studied.
Elliptocytosis 3
Eber et al. (1988) found a truncated beta chain in affected members of a large German family in which several members suffered in varying degrees from a microcytic hemolytic anemia. The red cell morphology varied from smooth elliptocytes to predominantly poikilocytes. The abnormal spectrin made up about 30% of the total and was present almost entirely as the dimer.
Ohanian et al. (1985) described a case of hemolytic anemia with elliptocytosis in which a large part of the beta subunit of spectrin was truncated. Coetzer and Zail (1981) and Dhermy et al. (1982) found variants of the beta-subunit in patients with hereditary elliptocytosis.
Gallagher and Forget (1996) cataloged 15 reported beta-spectrin mutations found in cases of hereditary elliptocytosis and hereditary pyropoikilocytosis. Three were splicing mutations, 3 were deletions, 1 was an insertion, and the remainder were missense mutations.
Pothier et al. (1989) found this variant in a French family. Heterozygotes were clinically normal and showed no morphologic abnormalities of red cells. The abnormality resided in the beta-IV domain.
Pothier et al. (1989) described this variant in an Algerian individual who was heterozygous for the variant and was asymptomatic clinically with morphologically normal red cells. The mutation was located in the beta-IV domain. This 41-kD fragment is near the N terminus of the beta-spectrin chain. The proband was also heterozygous for an alpha mutant, spectrin Oran.
Tse et al. (1989) studied the family of an infant with severe neonatal hemolytic anemia with poikilocytosis (EL3; 617948). Biochemical studies were consistent with the parents being heterozygous for alpha-I/74 hereditary elliptocytosis and the proband being homozygous. Spectrin chain reconstitution and RFLP linkage studies indicated, however, that the primary defect resided in beta-spectrin. Nucleotide sequencing showed a substitution that changed alanine residue 2053 to proline (A2053P). Tse et al. (1989) suggested a model of interaction of the alpha- and beta-spectrin chains in such a way that a proline residue would disrupt the normal helical structure of the complex, thereby impairing spectrin dimer self-association and exposing the alpha chain to enhanced proteolysis. Thus, this is an example of apparent abnormality in one polypeptide resulting from a primary defect in another.
In a family with a chronic hemolytic form of hereditary elliptocytosis (EL3; 617948) and, by biochemical analysis, a truncated beta-spectrin chain with deletion of a peptide fragment near the C-terminus, Gallagher et al. (1990) showed that the next-to-last exon of beta-spectrin (exon Y) was absent. Nucleotide sequencing showed a mutation in the 5-prime donor consensus splice site of the intron following the Y exon, TGG/GTGAGT to TGG/GTTAGT, in 1 allele. The truncated donor spectrin chain was thought to be due to splicing out of exon Y because of the mutation, resulting in exon skipping. This variant was designated spectrin Rouen. Garbarz et al. (1991) stated that this was, to their knowledge, the first documented example of exon skipping as the cause of a shortened beta-spectrin chain in a case of hereditary elliptocytosis. The exon skip resulted in a loss of 17 amino acids and created a frameshift with the synthesis of 33 novel amino acids before premature chain termination 14 residues upstream from the normal carboxy-terminus of the beta-spectrin chain, giving a mutant beta-spectrin chain 31 amino acids shorter than the normal chain.
Pothier et al. (1987) described a new defect in the beta chain of spectrin, designated spectrin Nice, causing elliptocytosis with hemolytic anemia (EL3; 617948). The beta chain was truncated, resulting in an additional band migrating between the spectrin beta chain and ankyrin. It represented 30% of the total beta chain. Pothier et al. (1987) considered this to be a new mutation. By nucleotide sequencing, Tse et al. (1991) showed a normal beta-spectrin cDNA sequence from position 6153 to position 6231, at which point the sequencing pattern became a superimposition of 2 different sequencing ladders, presumably corresponding to the 2 beta-spectrin alleles of the propositus. An insertion of 2 extra bases, GA, was demonstrated at nucleotides 6232 and 6233 in exon X. The 2 extra bases were inserted after the first base of codon 2046. The insertion created a frameshift in the C-terminal region of the beta-spectrin chain. A new stop codon had been created 31 residues downstream in the new reading frame. The amino acid sequence of the abnormal chain showed a net loss of 61 residues which corresponded to a size difference of roughly 6 kD from the normal.
In a Japanese patient with elliptocytosis (EL3; 617948) and uncompensated hemolysis of moderate severity, Kanzaki et al. (1992) demonstrated a 1-bp deletion in codon 2059 in exon X of the SPTB gene. The change in code from GCCAGC to GCAGCT changed ala-ser to ala-ala. A missense sequence extended down to a new codon 2075. Serine-2060, a potential phosphorylation site, was replaced by alanine. The shortened beta chain failed to undergo phosphorylation in vitro. This mutation, designated spectrin Tokyo, shared the same TGA stop codon, overlapping normal codons 2076 and 2077 (CTGAAA), as spectrin Nice (182870.0005), which is caused by a 2-bp insertion in codon 2046 and contains 2,076 amino acids.
In affected members of a family with autosomal dominant hereditary spherocytosis (SPH2; 616649), Becker et al. (1993) identified a TGG (trp)-to-CGG (arg) change at codon 202 in the SPTB gene. This family was previously reported by Wolfe et al. (1982), who had shown that approximately 40% of spectrin was unable to bind protein 4.1 (EPB41; 130500). The mutation occurred de novo in the proband, who transmitted it to 2 of her 4 children. The mutation was not found in 20 other kindreds. The mutation was located within a conserved sequence among spectrin-like proteins and may define an amino acid critical for protein 4.1 binding. This variant was designated spectrin Kissimmee.
Sahr et al. (1993) defined the molecular defect, designated spectrin Cagliari, responsible for clinically asymptomatic hereditary elliptocytosis (EL3; 617948) and hereditary pyropoikilocytosis (266140) in 2 unrelated families from Cagliari, Sardinia. One family, earlier reported by Coetzer et al. (1990), was ascertained through 2 daughters with severe hemolytic anemia and findings on blood smears consistent with the diagnosis of pyropoikilocytosis. Both parents, who were related, were clinically asymptomatic but showed mild hemolysis and, like one other daughter, had approximately 20% elliptocytes. In the second family, the parents were also consanguineous but clinically normal. A son had severe neonatal hemolysis and findings of pyropoikilocytosis. The anemia was transfusion-dependent in all 3 with HPP; transfusion dependence was relieved by splenectomy in 1. Following linkage studies which were most consistent with a beta-spectrin mutation, a nucleotide change was identified in codon 2018 of the SPTB gene resulting in an ala-to-gly substitution in the first helical domain of beta-spectrin repeat 17. Because glycine is a strong helix breaker, the change was predicted to disrupt the conformation of this helical domain, which must play a direct role in alpha-beta interdimer interactions. The 3 persons with HPP were homozygous for the defect.
Gallagher et al. (1995) studied a Laotian kindred in which 4 third-trimester fetal losses occurred, associated with severe Coombs-negative hemolytic anemia and extensive extramedullary erythropoiesis (617948). Postmortem examination of 2 infants revealed overt hydrops fetalis. Studies of erythrocytes and erythrocyte membranes from the parents revealed abnormal membrane mechanical stability as well as structural and functional abnormalities in spectrin. Genetic studies identified a point mutation of the SPTB gene, resulting in an amino acid replacement, S2019P, in the C-terminal region of erythrocyte beta-spectrin that is critical for normal spectrin self-association. Both parents and 2 living children were heterozygous for this mutation. As determined by analysis of DNA obtained from autopsy material, the 3 deceased infants were homozygous for the mutation. The variant was named spectrin Providence.
In an apparent de novo case of hereditary spherocytosis (SPH2; 616649), Hassoun et al. (1995) demonstrated heterozygosity for a deletion of exons 22 and 23 of the SPTB gene. This variant was designated spectrin Durham. Although the mutated gene was efficiently transcribed and its mRNA abundant in reticulocytes, the mutant protein was normally synthesized in erythroid progenitor cells, and the stability of the mutant protein in the cytoplasm of erythroblasts paralleled that of the normal beta-spectrin, the abnormal protein was inefficiently incorporated into the membrane of the erythroblasts. Hassoun et al. (1995) presented evidence that misincorporation into the cell membrane resulted from conformational changes of the beta-spectrin subunit affecting the binding of the abnormal heterodimer to ankyrin. The rate of synthesis of alpha-spectrin is 3 times that of beta-spectrin, and therefore the availability of beta-spectrin determines the rate of assembly of the spectrin heterodimers on the membrane (Hanspal and Palek, 1987, Hanspal et al., 1992). No mutations of alpha-spectrin had been reported as the cause of hereditary spherocytosis. Mutations in band 3 (109270) and particularly in ankyrin (612641) had previously been described in dominantly inherited spherocytosis. One previous example of a heterozygous beta-spectrin mutation, spectrin Kissimmee, had been described (182870.0007).
Gallagher et al. (1997) found homozygosity for a mutation in the SPTB gene in an infant with severe nonimmune hemolytic anemia and hydrops fetalis at birth (617948). His neonatal course was marked by ongoing hemolysis requiring repeated erythrocyte transfusions. He had remained transfusion-dependent for more than 2 years. A previous sib born with hemolytic anemia and hydrops fetalis died on the second day of life. Peripheral blood smears from both parents revealed rare elliptocytes. Examination of the patient erythrocyte membranes revealed abnormal mechanical stability, as well as structural and functional abnormalities in spectrin. The proband and his deceased sister were found to be homozygous for an L2025R mutation in the region of spectrin that is critical for normal function. The importance of leucine in this position of the proposed triple helical model of spectrin repeats was highlighted by its evolutionary conservation in all beta-spectrins from Drosophila to humans. Molecular modeling demonstrated the disruption of hydrophobic interactions in the interior of the triple helix critical for spectrin function caused by the replacement of the hydrophobic, uncharged leucine by a hydrophilic, positively charged arginine. Gallagher et al. (1997) noted that this mutation must also be expressed in beta-spectrin found in muscle, yet pathologic and immunohistochemical examination of skeletal muscle from the deceased sib was unremarkable. The parents were Laotian and apparently nonconsanguineous. This mutation is known as spectrin Buffalo.
In a Calabrian family in Southern Italy, Qualtieri et al. (1997) found that hereditary elliptocytosis (EL3; 617948) in the heterozygous state was asymptomatic and associated with a defect in spectrin dimer self association and an increase of the alpha(I/74) kD fragment from the alpha-chain after partial tryptic digestion of spectrin. By SSCP followed by DNA sequencing, they identified a C-to-G substitution at position 6284 of the SPTB gene. The corresponding substitution at the protein level, referred to as spectrin Cosenza, was arg2064 to pro of the beta-spectrin chain.
Basseres et al. (1998) described the first example of a translation initiation mutation in the SPTB gene. A Brazilian family with hereditary spherocytosis in 8 individuals in 2 generations carried the mutation. The propositus was a 28-year-old black man with compensated hemolytic disease with splenomegaly, hyperbilirubinemia, increased osmotic fragility, and a regular number of spherocytes and acanthocytes in the blood smear. Affected members of the family were heterozygous for an A-to-G substitution converting the translation initiation codon from ATG to GTG. The mutation would be expected to convert the initiation methionine to a valine. Affected members would have only 1 functional allele and, as beta-spectrin quantities are probably limiting for membrane assembly, this would account for the picture of spherocytosis. This mutation was called beta-spectrin Promissao.
Basseres et al. (2001) identified beta-spectrin S-ta Barbara in a 25-year-old woman of Italian origin who presented with hemolytic anemia with splenomegaly, hyperbilirubinemia, increased osmotic fragility of the red cells, and many spherocytes and acanthocytes in the blood smear (SPH2; 616649). The mutation was a deletion of 1 cytosine at codon 638 in exon 14, causing a frameshift and premature termination after an additional 31 amino acids. The mutant protein was not detected in red cell membranes or in other cellular compartments, but detectable levels of mutant mRNA were found in the patient. The mutation was not present in the patient's parents but was present in her affected brother, suggesting mosaicism. DNA analyses of different tissues of the parents failed to reveal the mutation. A fingerprinting test using highly polymorphic markers failed to exclude paternity with a high confidence index in relation to both the patient and her affected brother.
In sibs with hereditary spherocytosis (SPH2; 616649), Maciag et al. (2009) found an approximately 25% decrease in SPTB mRNA compared to controls. Direct sequencing of the SPTB gene identified a heterozygous 5268C-T transition in exon 26, resulting in an arg1756-to-ter (R1756X) substitution. The findings suggested that the mutation did not lead to complete nonsense-mediated mRNA decay, perhaps because of its location. Maciag et al. (2009) postulated that the shortened protein was incorporated into the erythrocyte membrane, leading to mechanical instability.
Basseres, D. S., Duarte, A. S. S., Hassoun, H., Costa, F. F., Saad, S. T. O. Beta-spectrin S-ta Barbara: a novel frameshift mutation in hereditary spherocytosis associated with detectable levels of mRNA and a germ cell line mosaicism. Brit. J. Haemat. 115: 347-353, 2001. Note: Erratum: Brit. J. Haemat. 116: 925 only, 2002. [PubMed: 11703334] [Full Text: https://doi.org/10.1046/j.1365-2141.2001.03103.x]
Basseres, D. S., Vicentim, D. L., Costa, F. F., Saad, S. T. O., Hassoun, H. Beta-spectrin Promissao: a translation initiation codon mutation of the beta-spectrin gene (ATG-to-GTG) associated with hereditary spherocytosis and spectrin deficiency in a Brazilian family. (Letter) Blood 91: 368-369, 1998. [PubMed: 9414314]
Becker, P. S., Tse, W. T., Lux, S. E., Forget, B. G. Beta-spectrin Kissimmee: a spectrin variant associated with autosomal dominant hereditary spherocytosis and defective binding to protein 4.1. J. Clin. Invest. 92: 612-616, 1993. [PubMed: 8102379] [Full Text: https://doi.org/10.1172/JCI116628]
Birkenmeier, C. S., McFarland-Starr, E. C., Barker, J. E. Chromosomal location of three spectrin genes: relationship to the inherited hemolytic anemias of mouse and man. Proc. Nat. Acad. Sci. 85: 8121-8125, 1988. [PubMed: 3186715] [Full Text: https://doi.org/10.1073/pnas.85.21.8121]
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Dhermy, D., Lecomte, M. C., Garbarz, M., Bournier, O., Galand, C., Gautero, J., Feo, C., Alloisio, N., Delaunay, J., Boivin, P. Spectrin beta chain variant associated with hereditary elliptocytosis. J. Clin. Invest. 70: 707-715, 1982. [PubMed: 7119110] [Full Text: https://doi.org/10.1172/jci110666]
Eber, S. W., Morris, S. A., Schroter, W., Gratzer, W. B. Interactions of spectrin in hereditary elliptocytes containing truncated spectrin beta-chains. J. Clin. Invest. 81: 523-530, 1988. [PubMed: 3276733] [Full Text: https://doi.org/10.1172/JCI113350]
Forget, B. G., Chang, J. G., Coupal, E., Fukushima, Y., Stanislovitis, P., Costa, F., Byers, M., Winkelmann, J., Agre, P., Marchesi, V. T., Shows, T. B., Watkins, P. Molecular genetics of the human beta-spectrin gene. (Abstract) Clin. Res. 36: 612A, 1988.
Fukushima, Y., Byers, M. G., Watkins, P. C., Winkelmann, J. C., Forget, B. G., Shows, T. B. Assignment of the gene for beta-spectrin (SPTB) to chromosome 14q23-q24.2 by in situ hybridization. Cytogenet. Cell Genet. 53: 232-233, 1990. [PubMed: 2209094] [Full Text: https://doi.org/10.1159/000132939]
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Gallagher, P. G., Petruzzi, M. J., Weed, S. A., Zhang, Z., Marchesi, S. L., Mohandas, N., Morrow, J. S., Forget, B. G. Mutation of a highly conserved residue of beta-1 spectrin associated with fatal and near-fatal neonatal hemolytic anemia. J. Clin. Invest. 99: 267-277, 1997. [PubMed: 9005995] [Full Text: https://doi.org/10.1172/JCI119155]
Gallagher, P. G., Weed, S. A., Tse, W. T., Benoit, L., Morrow, J. S., Marchesi, S. L., Mohandas, N., Forget, B. G. Recurrent fatal hydrops fetalis associated with a nucleotide substitution in the erythrocyte beta-spectrin gene. J. Clin. Invest. 95: 1174-1182, 1995. [PubMed: 7883966] [Full Text: https://doi.org/10.1172/JCI117766]
Gallagher, P., Garbarz, M., Tse, W., Picat, C., Lecomte, M. C., Dhermy, D., Forget, B. G. Exon skipping due to a splice site mutation causes hereditary elliptocytosis (HE) associated with the shortened beta chain of spectrin Rouen. (Abstract) Clin. Res. 38: 266A, 1990.
Garbarz, M., Tse, W. T., Gallagher, P. G., Picat, C., Lecomte, M.-C., Galibert, F., Dhermy, D., Forget, B. G. Spectrin Rouen (beta-220-218), a novel shortened beta-chain variant in a kindred with hereditary elliptocytosis: characterization of the molecular defect as exon skipping due to a splice site mutation. J. Clin. Invest. 88: 76-81, 1991. [PubMed: 2056132] [Full Text: https://doi.org/10.1172/JCI115307]
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Hassoun, H., Vassiliadis, J. N., Murray, J., Yi, S. J., Hanspal, M., Ware, R. E., Winter, S. S., Chiou, S.-S., Palek, J. Molecular basis of spectrin deficiency in beta spectrin Durham: a deletion within beta spectrin adjacent to the ankyrin-binding site precludes spectrin attachment to the membrane in hereditary spherocytosis. J. Clin. Invest. 96: 2623-2629, 1995. [PubMed: 8675627] [Full Text: https://doi.org/10.1172/JCI118327]
Kanzaki, A., Rabodonirina, M., Yawata, Y., Wilmotte, R., Wada, H., Ata, K., Yamada, O., Akatsuka, J., Iyori, H., Horiguchi, M., Nakamura, H., Mishima, T., Morle, L., Delaunay, J. A deletional frameshift mutation of the beta-spectrin gene associated with elliptocytosis in spectrin Tokyo (beta-220/216). Blood 80: 2115-2121, 1992. [PubMed: 1391962]
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Qualtieri, A., Pasqua, A., Bisconte, M. G., Le Pera, M., Brancati, C. Spectrin Cosenza: a novel beta chain variant associated with Sp-alpha(I/74) hereditary elliptocytosis. Brit. J. Haemat. 97: 273-278, 1997. [PubMed: 9163587] [Full Text: https://doi.org/10.1046/j.1365-2141.1997.572703.x]
Sahr, K. E., Coetzer, T. L., Moy, L. S., Derick, L. H., Chishti, A. H., Jarolim, P., Lorenzo, F., del Giudice, E. M., Iolascon, A., Gallanello, R., Cao, A., Delaunay, J., Liu, S.-C., Palek, J. Spectrin Cagliari: an ala-to-gly substitution in helix 1 of beta-spectrin repeat 17 that severely disrupts the structure and self-association of the erythrocyte spectrin heterodimer. J. Biol. Chem. 268: 22656-22662, 1993. [PubMed: 8226774]
Tse, W. T., Costa, F. F., Lecomte, M.-C., Dhermy, D., Garbarz, M., Boivin, P., Forget, B. G. An ala-to-pro substitution in the beta-spectrin chain causes alpha-I/74 hereditary elliptocytosis (HE). (Abstract) Blood 74: 105A, 1989.
Tse, W. T., Gallagher, P. G., Pothier, B., Costa, F. F., Scarpa, A., Delaunay, J., Forget, B. G. An insertional frameshift mutation of the beta-spectrin gene associated with elliptocytosis in spectrin Nice (beta-220/216). Blood 78: 517-523, 1991. [PubMed: 2070088]
Watkins, P. C., Eddy, R., Winkelmann, J. C., Forget, B. G., Shows, T. B. Assignment of the gene for beta-spectrin (SPTB) to human chromosome 14. (Abstract) Cytogenet. Cell Genet. 46: 712, 1987.
Winkelmann, J. C., Chang, J.-G., Tse, W. T., Scarpa, A. L., Marchesi, V. T., Forget, B. G. Full-length sequence of the cDNA for human erythroid beta-spectrin. J. Biol. Chem. 265: 11827-11832, 1990. [PubMed: 2195026]
Winkelmann, J. C., Leto, T. L., Watkins, P. C., Eddy, R., Shows, T. B., Linnenbach, A. J., Sahr, K. E., Kathuria, N., Marchesi, V. T., Forget, B. G. Molecular cloning of the cDNA for human erythrocyte beta-spectrin. Blood 72: 328-334, 1988. [PubMed: 3390609]
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Wolfe, L. C., John, K. M., Falcone, J. C., Byrne, A. M., Lux, S. E. A genetic defect in the binding of protein 4.1 to spectrin in a kindred with hereditary spherocytosis. New Eng. J. Med. 307: 1367-1374, 1982. [PubMed: 6215583] [Full Text: https://doi.org/10.1056/NEJM198211253072203]