Alternative titles; symbols
HGNC Approved Gene Symbol: HBA1
SNOMEDCT: 36467003, 68913001, 74405003; ICD10CM: D56.0; ICD9CM: 282.43;
Cytogenetic location: 16p13.3 Genomic coordinates (GRCh38): 16:176,680-177,522 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 16p13.3 | Erythrocytosis, familial, 7 | 617981 | Autosomal dominant | 3 |
| Heinz body anemias, alpha- | 140700 | Autosomal dominant | 3 | |
| Hemoglobin H disease, nondeletional | 613978 | 3 | ||
| Methemoglobinemia, alpha type | 617973 | Autosomal dominant | 3 | |
| Thalassemias, alpha- | 604131 | 3 |
The alpha and beta loci determine the structure of the 2 types of polypeptide chains in the tetrameric adult hemoglobin, Hb A, alpha-2/beta-2. The alpha locus also determines a polypeptide chain, the alpha chain, in fetal hemoglobin (alpha-2/gamma-2), in hemoglobin A2(alpha-2/delta-2), and in embryonic hemoglobin (alpha-2/epsilon-2). The number of normal alpha genes (3, 2, 1 or none) in Asian cases of alpha-thalassemia (604131) results in 4 different alpha-thalassemia syndromes (Kan et al., 1976). Three normal alpha genes gives a silent carrier state. Two normal alpha genes results in microcytosis (so-called heterozygous alpha-thalassemia). One normal alpha gene results in microcytosis and hemolysis (so-called Hb H disease, 613978). No normal alpha gene results in 'homozygous alpha-thalassemia' manifested as fatal hydrops fetalis.
The alpha chain of human hemoglobin contains 141 amino acids (Konigsberg et al., 1961).
By studies of somatic cell hybrids, Deisseroth et al. (1976) showed that the alpha and beta loci are on different chromosomes.
Deisseroth et al. (1977) combined the methods of somatic cell hybridization and DNA-cDNA hybridization to establish assignment of the alpha-globin locus to chromosome 16. This represents an extension of the cell hybridization method permitting mapping of genes that are not functional in the cultured cell. Deisseroth and Hendrick (1978) confirmed the assignment of the alpha locus to chromosome 16 by means of cotransfer of this gene with the human APRT gene, known to be on 16 (see 102600), into mouse erythroleukemia cells. (The APRT gene is on the long arm of chromosome 16.)
Weitkamp et al. (1977) presented data concerning linkage of the alpha and beta loci to 34 marker loci. Data on alpha-thalassemia, combined with those on the Hopkins-2 variant, excluded linkage of alpha and haptoglobin (140100) at a recombination fraction less than 0.15.
On the basis of findings in a case of partial trisomy 16, Wainscoat et al. (1981) concluded that the alpha-globin genes are on segment 16pter-p12. By combining somatic cell hybridization with a cDNA probe in the study of a cell line with reciprocal translocation between 16q and 11q, Koeffler et al. (1981) showed that the alpha-globin genes are on the short arm of 16. Gerhard et al. (1981) used an improved method of in situ hybridization to confirm the assignment of the alpha-globin cluster to chromosome 16p.
On the basis of the findings in a fetus with an unbalanced translocation involving 16p, Breuning et al. (1987) concluded that the HBA cluster is distal to PGP (172280).
By a combination of in situ hybridization, Southern blot analysis, and linkage analysis using the fragile site 16p12.3 and translocation breakpoints within band 16p13.1, Simmers et al. (1987) mapped the alpha-globin gene complex to 16pter-p13.2.
Buckle et al. (1988) described a child in whom cytogenetic analysis indicated monosomy for 16pter-p13.3. DNA studies showed that the patient had not inherited either maternal alpha-globin allele. The child had the alpha-thalassemia trait as well as moderate mental retardation and dysmorphic features. They determined that the gene is located in the 16pter-p13.3 segment. After reviewing earlier data placing the alpha-globin cluster slightly more proximal, they concluded that the findings in this child may be more reliable.
Orkin (1978) identified alpha-globin gene fragments in restriction endonuclease digests of total DNA after electrophoresis by hybridization with P32-labeled cDNA probes. The data indicated that the alpha genes occur in duplicate and that the 2 copies lie close together. Thus direct physical evidence was provided for the duplication deduced from the findings with mutant alpha chains and with the alpha-thalassemias and the kinetics of hybridization in solution. The 2 alpha chains lie about 3.7 kilobases apart.
Leder et al. (1978) presented evidence that the alpha and beta genes of all adult mammalian hemoglobins have 2 intervening sequences at analogous positions.
Straub et al. (2012) reported a model for the regulation of nitric oxide (NO) signaling by demonstrating that hemoglobin alpha, encoded by the HBA1 and HBA2 (141850) genes, is expressed in human and mouse arterial endothelial cells and enriched at the myoendothelial junction, where it regulates the effects of NO on vascular reactivity. Notably, this function is unique to hemoglobin alpha and is abrogated by its genetic depletion. Mechanistically, endothelial hemoglobin alpha heme iron in the Fe(3+) state permits NO signaling, and this signaling is shut off when hemoglobin alpha is reduced to the Fe(2+) state by endothelial cytochrome b5 reductase 3 (CYB5R3; 613213). Genetic and pharmacologic inhibition of CYB5R3 increased NO bioactivity in small arteries. Straub et al. (2012) concluded that their data revealed a mechanism by which the regulation of the intracellular hemoglobin alpha oxidation state controls nitric oxide synthase (NOS; see 163729) signaling in nonerythroid cells. The authors suggested that this model may be relevant to heme-containing globins in a broad range of NOS-containing somatic cells.
Crystal Structure
Andersen et al. (2012) presented the crystal structure of the dimeric porcine haptoglobin (140100)-hemoglobin complex determined at 2.9-angstrom resolution. This structure revealed that haptoglobin molecules dimerize through an unexpected beta-strand swap between 2 complement control protein (CCP) domains, defining a new fusion CCP domain structure. The haptoglobin serine protease domain forms extensive interactions with both the alpha- and beta-subunits of hemoglobin, explaining the tight binding between haptoglobin and hemoglobin. The hemoglobin-interacting region in the alpha-beta dimer is highly overlapping with the interface between the 2 alpha-beta dimers that constitute the native hemoglobin tetramer. Several hemoglobin residues prone to oxidative modification after exposure to heme-induced reactive oxygen species are buried in the haptoglobin-hemoglobin interface, thus showing a direct protective role of haptoglobin. The haptoglobin loop previously shown to be essential for binding of haptoglobin-hemoglobin to the macrophage scavenger receptor CD163 (605545) protrudes from the surface of the distal end of the complex, adjacent to the associated hemoglobin alpha-subunit. Small-angle x-ray scattering measurements of human haptoglobin-hemoglobin bound to the ligand-binding fragment of CD163 confirmed receptor binding in this area, and showed that the rigid dimeric complex can bind 2 receptors.
Wilson et al. (1977) described a possible nucleotide polymorphism in the untranslated 3-prime region of the alpha-globin gene and suggested that the heterogeneity is related to the existence of 2 alpha gene loci.
Musumeci et al. (1978) pointed out that the combination of alpha-thalassemia and beta-thalassemia leads to less severe clinical expression of homozygous beta-thalassemia. The rarity of a chromosome 16 with both alpha loci deleted (as demonstrated by the restriction endonuclease mapping technique of Southern) explains the rarity of severe forms of alpha-thalassemia in Africans, e.g., Hb H disease, which requires loss of 3 alpha loci and homozygous alpha-thalassemia which requires loss of 4 alpha loci (Dozy et al., 1979).
By restriction endonuclease mapping, Goossens et al. (1980) identified 12 persons heterozygous for a chromosome carrying 3 alpha genes. There were no hematologic abnormalities. The frequency was 0.0036 in American Blacks and 0.05 in Greek Cypriots. They had previously shown a frequency of 0.16 for the single alpha-globin locus in black Americans. The single locus had a frequency of 0.18 in Sardinians, but none of 125 Sardinians had a triple alpha locus, suggesting that the former had a selective advantage. Greek Cypriots have a frequency of 0.07 for the single alpha locus. Among 645 Japanese subjects studied, Nakashima et al. (1990) found 10 persons heterozygous for a chromosome with the triplicated alpha-globin locus. Thus, the frequency of the triplicate alpha locus was 0.008 in this population, while that of the single alpha-locus, i.e., the alpha-thalassemia-2 gene, may be lower than 0.0008. Analysis of haplotypes suggested that the triple alpha loci may have had multiple origins. Nakashima et al. (1990) commented on the fact that in Melanesia the frequency of the triplicated genotype is about the same (Flint et al., 1986) as in Japan, whereas the frequency of the single alpha gene is much higher, compatible with a selective advantage vis-a-vis malaria. Liebhaber et al. (1981) found identity of the alpha-1-globin genes from an Asian and a Caucasian. Furthermore, the alpha-1 and alpha-2 genes have a much higher degree of homology than would be predicted from the timing of the duplication before the bird-mammal divergence (about 300 Myr ago). Liebhaber et al. (1981) presented this as evidence for the existence of mechanisms for suppression of allelic polymorphisms and for exchange of genetic information within the alpha-globin gene complex. See 142200 for a discussion of gene conversion in relation to a comparably surprising homology of the 2 gamma-globin genes.
Lehmann and Carrell (1984) suggested the use of the following nomenclature for alpha-thalassemias based on the number of alpha-globin genes that are missing or abnormal: 1-alpha-thalassemia (silent type); 2-alpha-thalassemia, trans or cis (thalassemia trait); 3-alpha-thalassemia (Hb H disease); and 4-alpha-thalassemia (Hb Bart hydrops fetalis). In this scheme, homozygous Hb Constant Spring is a 2-alpha-thalassemia which, if combined with a cis 2-alpha-thalassemia heterozygous Hb Constant Spring, gives a 3-alpha-thalassemia and results in Hb H disease. Lehmann and Carrell (1984) also proposed that the 2 alpha-globin genes be designated as 5-prime (now alpha-2) and 3-prime (now alpha-1). Liebhaber and Cash (1985) described a method for identifying whether the alpha-1 or alpha-2 locus is the site of particular alpha-globin mutations. Rubin and Kan (1985) described a sensitive method for determining how many alpha-globin genes are present. It had the advantages of not requiring restriction enzyme digestion and gel electrophoresis and using the much more stable isotope (35)S rather than 32(P) for labeling. Only a small sample of DNA is needed. Application of the approach to diagnosis of Down syndrome was proposed. Assum et al. (1985) added a fourth restriction site polymorphism in the alpha-globin gene cluster. Compared to the beta-globin cluster, the alpha-globin cluster seemed to show a poverty of DNA polymorphism; however, Higgs et al. (1986) demonstrated a remarkable degree of DNA polymorphism in the alpha-globin gene cluster. In addition, the RFLP haplotype is associated with hypervariable regions of DNA.
Pseudo-alpha-1 (HBAP1), a pseudogene, is defective in several respects, including splice junction mutations and premature termination codons. Hardison et al. (1986) identified a previously undetected pseudogene in the alpha-globin cluster. It was not detected by hybridization studies but was found only on sequence analysis. Hardison et al. (1986) suggested that 'divergent copies of a large number of genes may comprise a substantial fraction of the slowly renaturing DNA of mammalian genomes.' The newly detected pseudogene, which will be symbolized HBAP2, is only 65 bp 3-prime to the polyadenylation site of zeta-1 (HBZP). The sequence is: 5-prime--HBZ--HBZP--HBAP2--HBA2--HBA1--3-prime. (The functional Hba gene of the mouse is on chromosome 11, but pseudogenes are dispersed to other chromosomes (e.g., Hba-ps3 to mouse chromosome 15) (Popp et al., 1981; Leder et al., 1981; Eicher and Lee, 1991).)
Vandenplas et al. (1987) described a new form of alpha-0 thalassemia in a South African family ascertained through a case of Hb H disease. A novel deletion of 22.8-23.7 kb of DNA removed 3 pseudogenes as well as the alpha-2 and alpha-1 genes. Since the alpha-2-globin gene encodes the majority of alpha-globin, a thalassemic mutation of the alpha-1-globin gene would be expected to result in a less severe loss of alpha-chain synthesis.
Moi et al. (1987) described an initiation codon mutation, AUG-to-GUG, in the alpha-1-globin gene. As predicted, the degree of interference with alpha-globin synthesis was less in this mutation than in the mutation in the initiation codon of the alpha-2-globin gene (see 141850).
Hill et al. (1987) described a unique nondeletion form of Hb H disease in Papua New Guinea: all 4 alpha genes were intact. Hill et al. (1987) commented on the striking difference in the hemoglobinopathies that occur in Southeast Asia and in Melanesia. In the former area, Hb E, Hb Constant Spring, and the Southeast Asian form of deletion alpha-0-thalassemia are all common, whereas these forms have never been found in Melanesians or Polynesians.
Jarman and Higgs (1988) identified a highly polymorphic region approximately 100 kb upstream of the alpha-globin genes and referred to it as 5-prime HVR. This is a valuable genetic marker for 16p. Higgs et al. (1989) gave a comprehensive review of the molecular genetics of the alpha-globin gene cluster, including its diseases.
Hatton et al. (1990) presented evidence for the existence of an alpha-locus control region (LCRA; 152422). This would be comparable to the beta-LCR which controls expression of the beta-like genes; see 152424. Liebhaber et al. (1990) identified an individual with alpha-thalassemia in whom structurally normal alpha-globin genes were inactivated in cis by a discrete de novo 35-kb deletion located about 30 kb 5-prime to the alpha-globin gene cluster. They concluded that the deletion inactivates expression of the alpha-globin genes by removing one or more of the previously identified upstream regulatory sequences that are critical to expression of the alpha-globin genes.
Hemoglobinopathies of alpha-globin can result from missense mutations at either of the 2 alpha-globin loci, HBA1 or HBA2. Since the normal HBA1 and HBA2 genes encode an identical alpha globin, these mutants cannot be assigned to their specific loci on the basis of protein structural analysis. A clue to the encoding locus, HBA1 versus HBA2, is provided by the relative concentration of the alpha-globin mutant in the erythrocyte based on the 2- to 3-fold higher level of expression of the HBA2 gene (Liebhaber et al., 1986). However, since variables such as protein stability, efficiency of hemoglobin tetramer formation, and other factors can affect the steady-state levels of globin mutants, a definitive locus assignment must be directly determined. Cash et al. (1989) quantitated the expression of 2 alpha-globin structural mutants found in the Caribbean basin, Fort de France and Spanish Town, and showed that they are HBA1 and HBA2 mutants, respectively, on the basis of low or high expression.
Wilkie et al. (1991) described major polymorphic length variation in the terminal region of 16p (16p13.3) by physically linking the alpha-globin locus with probes to telomere-associated repeats. They found 3 alleles in which the alpha-globin genes lie 170 kb, 350 kb, or 430 kb from the telomere. The 2 most common alleles were found to contain different terminal segments, starting 145 kb distal to the alpha-globin genes. Beyond this boundary these alleles are nonhomologous, yet each contains sequences related to other, different chromosome termini. This chromosome-size polymorphism probably arose by occasional exchanges between the subtelomeric regions of nonhomologous chromosomes. Wilkie et al. (1991) raised the possibility that the high frequency of trisomy 16 may be related to this nonhomology of the 2 common 16pter alleles in their subtelomeric region.
Huisman et al. (1996) found that of the 141 codons of the alpha-globin genes (there are no sequence differences between the coding regions of the alpha-2 and alpha-1 genes), as many as 99 have been found to be mutated; for several, 3 or 4 mutations have been discovered, while 5 mutations are known for codons 23, 75, and 94, and 6 for codon 141. The mutations appear to occur at random; thus, either one of the 3 bases are replaced in the 199 known alpha-globin gene mutants.
The suggestion that alpha(+)-thalassemia has achieved a high frequency in some populations as a result of selection by malaria is based on a number of epidemiologic studies. In the southwest Pacific region, there is a striking geographic correlation between the frequency of alpha(+)-thalassemia and the endemicity of Plasmodium falciparum. Allen et al. (1997) undertook a prospective case-control study of children with severe malaria on the north coast of Papua New Guinea, where malaria transmission is intense and alpha(+)-thalassemia affects more than 90% of the population (homozygotes comprise approximately 55% and heterozygotes 37% of the population). Compared with normal children, the risk of having severe malaria was 0.40 in alpha(+)-thalassemia homozygotes and 0.66 in heterozygotes. Unexpectedly, the risk of hospital admission with infections other than malaria also was reduced to a similar degree in homozygotes (0.36) and heterozygotes (0.63). This clinical study demonstrated that a malaria resistance gene protects against disease caused by infections other than malaria. A reduction in mortality greater than that attributable directly to malaria had been observed after the prevention of malaria by insecticides, chemoprophylaxis, and insecticide-impregnated bed nets. Previous observations that direct malaria mortality cannot account for observed hemoglobin S gene frequencies suggest that the findings of this study may apply equally to other malaria resistance genes.
Fung et al. (1999) reported 3 cases of homozygous alpha-thalassemia who survived beyond the newborn period, all with hypospadias. Review of the literature identified 2 additional cases. Fung et al. (1999) suggested that the hypospadias may have been secondary to the in utero edema leading to failure of fusion of urogenital folds or due to defect or deletion of another gene at 16p13.3.
For a review of hydrops fetalis caused by alpha-thalassemia, see Chui and Waye (1998).
From work on the mouse model of alpha-thalassemia, Leder et al. (1999) demonstrated that a normal beta-globin allele can act as a modifying gene ameliorating the severity of alpha-thalassemia. They found that the phenotype of alpha-thalassemia was strongly influenced by the genetic background in which the mutation resided; when both mutant genes were on a chromosome derived from strain 129, the phenotype was severe, whereas it was mild when the gene was on a 129 chromosome and a C57BL/6 chromosome. Linkage mapping indicated that the modifying gene is very tightly linked to the beta-globin locus (lod score = 13.3). Furthermore, the severity of the phenotype correlated with the size of beta-globin-containing inclusion bodies, which accumulate in red blood cells and likely accelerate their destruction. The beta-major globin chains encoded by the 2 strains differed by 3 amino acids, one of which is a glycine-to-cysteine substitution at position 13. The cys13 should be available for interchain disulfide bridging and consequent aggregation between excess beta chains. This normal polymorphic variation between murine beta-globin chains could account for the modifying action of the unlinked beta-globin locus. Here, the variation in severity of the phenotype would not depend on a change in the ratio between alpha and beta chains but on the chemical nature of the normal beta chain, which is in excess. This work also indicated that modifying genes can be normal variants that, absent an apparent physiologic rationale, may be difficult to identify on the basis of structure alone.
De Gobbi et al. (2006) identified a pathogenetic mechanism underlying a variant form of the inherited blood disorder alpha-thalassemia. Association studies of affected individuals from Melanesia localized the disease trait to the telomeric region of human chromosome 16, which includes the alpha-globin gene cluster, but no molecular defects were detected by conventional approaches. After resequencing and using a combination of chromatin immunoprecipitation and expression analysis on a tiled oligonucleotide array, De Gobbi et al. (2006) identified a gain-of-function regulatory single-nucleotide polymorphism (rSNP) (141800.0218) in a nongenic region between the alpha-globin genes and their upstream regulatory elements. The rSNP creates a new promoter-like element that interferes with normal activation of all downstream alpha-like globin genes. De Gobbi et al. (2006) concluded that their work illustrates a strategy for distinguishing between neutral and functionally important rSNPs, and it also identifies a pathogenetic mechanism that could potentially underlie other genetic diseases.
Schoenfelder et al. (2010) found that mouse Hbb and Hba associated with hundreds of active genes from nearly all chromosomes in nuclear foci that they called 'transcription factories.' The 2 globin genes preferentially associated with a specific and partially overlapping subset of active genes. Schoenfelder et al. (2010) also noted that expression of the Hbb locus is dependent upon Klf1 (600599), while expression of the Hba locus is only partially dependent on Klf1. Immunofluorescence analysis of mouse erythroid cells showed that most Klf1 localized to the cytoplasm and that nuclear Klf1 was present in discrete sites that overlapped with RNAII foci. Klf1 knockout in mouse erythroid cells specifically disrupted the association of Klf1-regulated genes within the Hbb-associated network. Klf1 knockout more weakly disrupted interactions within the specific Hba network. Schoenfelder et al. (2010) concluded that transcriptional regulation involves a complex 3-dimensional network rather than factors acting on single genes in isolation.
N.B.: Alpha-globin variants for which it is unknown whether HBA1 or HBA2 is involved have arbitrarily been included in this entry. Carver and Kutlar (1995) listed 191 alpha-globin variants as of January 1995. The syllabus by Huisman et al. (1996) listed 199 alpha-chain hemoglobin variants as of January 1996. These included single-base mutations in the alpha-2 and alpha-1 genes as well as 2-base mutations. Not included in their syllabus were deletions in mutations that result in alpha-thalassemia, even if such a change (point mutation or frameshift) occurred in one of the coding regions of the gene. Information about the alpha-thalassemias was provided by Higgs et al. (1989).
Gandini et al. (1977) concluded, incorrectly as it turned out, that the alpha loci are on the long arm of chromosome 4 (4q28-q34). The conclusion was based on a finding of excessive synthesis of alpha chains in patients with duplication of this region.
See Harano et al. (1984) and Baudin et al. (1987).
This was found in a clinically normal black female in Albany, Georgia (Webber et al., 1983). See also Shimasaki et al. (1983).
See Pootrakul et al. (1975).
See Adams et al. (1972) and Adams (1974).
See Rahbar et al. (1975).
See Fujiwara (1970) and Fujiwara et al. (1971).
See McDonald et al. (1990).
See Shelton et al. (1985).
See Marinucci et al. (1980).
See Liang et al. (1982).
See Kleihauer et al. (1968). (This is actually an allelic variant of the HBA2 gene; see 141850.0030.)
See Dahmane-Arbane et al. (1987).
See de Traverse et al. (1966), Yanase et al. (1968), Vella et al. (1970), and Fleming et al. (1978).
See Virshup et al. (1988). Moo-Penn et al. (1989) identified insertion of a glutamic acid residue between proline-37 and threonine-38 in an unstable hemoglobin variant. The PCR-amplified fragment of the variant gene showed insertion of a GAA codon. In the normal alpha-globin gene cluster, GAG is the codon for glutamic acid. Moo-Penn et al. (1989) suggested that this mutation may have resulted from nonhomologous nonallelic gene conversion.
See Boyer et al. (1968).
See Orringer et al. (1976).
See Clegg et al. (1966) and Harano et al. (1983). Polycythemia (ECYT7; 617981) is the only clinical feature. This was the first polycythemia-producing variant to be described (Charache et al., 1966).
See Jones et al. (1968).
See Bowman et al. (1986).
See Zeng et al. (1984).
Unstable hemoglobin due to disruption of hydrogen bond between alpha 103 (his) and beta 108 (asn) (Sciarratta et al., 1984).
See Nakatsuji et al. (1984).
See Spivak et al. (1981) and Lacombe et al. (1987).
See Rahbar et al. (1973) and de Weinstein et al. (1985).
See Wiltshire et al. (1972).
See Liang et al. (1981, 1988).
See Jue et al. (1979) and Baklouti et al. (1988).
See Crookston et al. (1969) and Headlee et al. (1983).
Honig et al. (1982) first described Hb Evanston in 2 black families. See also Moo-Penn et al. (1983).
Harteveld et al. (2004) found this rare variant alone and in the presence of common alpha-thalassemia deletions in 3 independent Asian cases.
See Lee-Potter et al. (1981).
Wajcman et al. (1989) found this substitution in an Italian family. The substitution produced no change in the stability or oxygen binding properties of the hemoglobin molecule. The electrophoretic properties were, furthermore, identical to those of Hb A, with the exception of isoelectric focusing in which the variant migrated like Hb A1c. Hb J(Nyanza), another substitution at position alpha-21, likewise causes no hematologic disorder.
See Braconnier et al. (1977). Cash et al. (1989) confirmed that this is a mutant of the HBA1 gene.
See Marengo-Rowe et al. (1968).
This variant was described in 2 black families. Unusually low (5%) concentration was found in heterozygotes, perhaps because of decreased ability of the abnormal alpha chain to form dimers with beta chains. See Schneider et al. (1971) and Carstairs et al. (1985).
See Huisman et al. (1970).
See Cohen-Solal et al. (1975) and Lorkin et al. (1975).
Hb G (Pest) and Hb J (Buda) (141850.0008), both alpha-chain mutants, occurred together in a Hungarian male with erythrocytosis. The occurrence of some normal Hb A in this man showed the existence of at least 2 alpha loci. See Brimhall et al. (1970, 1974) and Hollan et al. (1972). Using polymerase chain reaction (PCR) to amplify selectively alpha-1 and alpha-2-globin cDNAs, Mamalaki et al. (1990) then hybridized the cDNAs to synthetic oligonucleotides specific for either the normal or the mutated sequence. Using this approach, the alpha-globin structural mutants J-Buda and G-Pest were found to be encoded by the alpha-2 and the alpha-1-globin genes, respectively. The substitution in G-Pest was a change from GAC to AAC at codon 74.
See Vella et al. (1958), Gammack et al. (1961), Lie-Injo et al. (1966, 1979); Blackwell and Liu (1970), Pootrakul and Dixon (1970), Lorkin et al. (1970), Iuchi et al. (1978), and Higgs et al. (1980). Zeng et al. (1992) demonstrated that the mutation is due to a GAC-to-CAC change in codon 74 of the HBA1 gene. They developed a simple and accurate method for diagnosis of the Hb Q (Thailand) variant based on restriction enzyme analysis.
See Blackwell et al. (1973) and Bunn et al. (1978). Schiliro et al. (1991) found this variant in a Filipino mother and child living in Sicily. They showed no hematologic abnormalities.
See Winter et al. (1978).
At the time it was first studied by Huisman et al. (1974), hemoglobin Grady was unique in having an insertion of threonine-glutamic acid-phenylalanine between amino acids 118 and 119 of the alpha chain. Several hemoglobins with deletions were then known (Leiden, Lyon, Freiburg, Niteroi, Tochigi, St. Antoine, Tours and Gun Hill). Scott et al. (1981) found no evidence of an extra (fifth) alpha gene. They argued, therefore, that if, as supposed, Hb Grady arose by unequal crossing over, the event occurred between alleles rather than between the separate alpha-1 and alpha-2 loci. The glu-phe-thr insertion is a repeat of normal residues 116, 117 and 118. See Cleek et al. (1983). Substitution of glutamine for histidine at alpha 112 was thought to be the change in hemoglobin Dakar; however, on restudy the hemoglobin was found to be identical to Hb Grady (Garel et al., 1976).
See Jen and Liu (1987), Zhou et al. (1987), and Li et al. (1990).
See Hattori et al. (1985).
See Harano et al. (1982) and Sugihara et al. (1983).
See Griffiths et al. (1977), Chih-chuan et al. (1981), and Al-Awamy et al. (1985).
See Zeng et al. (1984).
See Harano et al. (1988). Using dot-blot analysis of amplified DNA with (32)p-labeled probes, Zhao et al. (1990) located the mutation in codon 27 of the minor alpha-1 globin gene and showed that the change involved a GAG (glutamic acid)-to-GAT (aspartic acid) mutation. Their patients were 3 Chinese women from Macau.
In Thailand, Ngiwsara et al. (2004) described 2 unrelated cases of compound heterozygosity for Hb Hekinan and alpha-thalassemia.
See Ohba et al. (1975, 1978).
See Fleming et al. (1987).
Fast hemoglobin. See Smith and Torbert (1958), Itano and Robinson (1960), Bradley et al. (1961), Ostertag et al. (1972), Clegg and Charache (1978).
Fast hemoglobin. Substitution of aspartic acid for lysine at alpha 16 was first reported by Murayama (1962). However, Crick pointed out that this substitution could not be accomplished by change in one base. Restudy by Beale and Lehmann (1965) and by Schneider et al. (1966) showed substitution of glutamic acid for lysine. Hemoglobin I was thought to show sickling but this has been shown to be due to faulty technique (Schneider et al., 1967). See Rucknagel et al. (1955), Schwartz et al. (1957), Itano and Robinson (1959, 1960), Ranney et al. (1962), O'Brien et al. (1964), Thompson et al. (1965), Schneider et al. (1966), Bowman and Barnett (1967), Baur (1968), Labossiere and Vella (1971), Fleming et al. (1978), and Liebhaber et al. (1984). The hemoglobin I mutation is curious in that the mutation is present in HBA2 (141850.0011) as well as in HBA1.
See Shibata et al. (1980) and Liu et al. (1983).
See Cabannes et al. (1972).
See Giordano et al. (1990).
See Kamuzora and Lehmann (1974) and Blackwell et al. (1974).
See Martinez et al. (1978). Romero et al. (1995) found this hemoglobin variant in 3 Spanish families. The original description by Martinez et al. (1978) was in a Cuban family of Spanish ancestry.
See Botha et al. (1966), Harano et al. (1983), and Lambridis et al. (1986). Erythrocytosis (ECYT7; 617981) is a clinical feature.
See Saenz et al. (1977) and Moo-Penn et al. (1981).
See Colombo et al. (1974) and Ohba et al. (1983).
See Rahbar et al. (1976).
See Gottlieb et al. (1964).
See Kendall et al. (1973).
See Rosa et al. (1966), Trincao et al. (1968), and Marinucci et al. (1979).
See Hyde et al. (1971).
See Alberti et al. (1974) and Moo-Penn et al. (1978).
See Wong et al. (1984).
Since no simple frameshift mechanism could be imagined, the possibility of 2 separate mutations was favored by Blackwell et al. (1972), who suggested that 2 separate hemoglobins, appropriately called Hb J (Singa) and Hb J (Pore), will be discovered eventually. Double mutation on the same chromosome would seem more likely than crossing-over in a compound heterozygote since the 2 codons involved are contiguous.
See Houjun et al. (1984). Li et al. (1990) found this variant in populations in the Silk Road region of China.
See Gajdusek et al. (1967) and Beaven et al. (1972). A homozygous individual had only anomalous hemoglobin suggesting the existence of only one alpha locus in Melanesians (Abramson et al., 1970).
See Crookston et al. (1965).
See Moo-Penn et al. (1976).
See Ahmed et al. (1986).
See Harano et al. (1983) and Imai et al. (1989).
See Harano et al. (1982).
Not a genetic change. The C-terminal amino acid, 141, of the alpha chain (arginine) is missing, probably from the action of a carboxypeptidase present in normal plasma. This unusual fast hemoglobin is observed in persons with hemolysis. The change can occur in fetal hemoglobin also (Kohne et al., 1977). See Marti et al. (1967) and Schiliro et al. (1982).
See Yamaoka et al. (1960), Ooya et al. (1961), Sumida (1975), and Ohba et al. (1982). The change is in TP IV (DeVries et al., 1963).
See Rahbar et al. (1969).
See Mavilio et al. (1978). Erythrocytosis (ECYT7; 617981) is a clinical feature.
See Sellaye et al. (1982), Harano et al. (1983), and Malcorra-Azpiazu et al. (1988).
See Djoumessi et al. (1981) and Lu et al. (1984).
This variant was discovered in a 10-year-old Algerian boy born in Loire. The child had erythrocytosis (ECYT7; 617981) and microcytosis, the latter being due to iron deficiency (Baklouti et al., 1988).
Groff et al. (1989) found this substitution in association with mild hemolytic anemia and increased indirect bilirubinemia in a family originating from the Netherlands.
The aberrant hemoglobins associated with methemoglobinemia (see 617973) are referred to as hemoglobin M. Most of the hemoglobin M variants have substitutions of histidine at alpha 58, alpha 87, beta 63, or beta 92. These 4 amino acids are critical to the binding of the heme group. The exception is hemoglobin M (Milwaukee-1). See Gerald et al. (1957), Hansen et al. (1960), Gerald and Efron (1961), Betke (1962), Hayashi et al. (1964), Shimizu et al. (1965), Suzuki et al. (1965), Hollan et al. (1967), and Pulsinelli et al. (1973).
Hb Iwate was the first variant hemoglobin found in Japan (Shibata et al., 1960). Familial cyanosis had been recognized for about 200 years in the prefecture of Iwate in Honshu, where about 70 affected persons were identified in the 1950s. It was called 'kuchikuro,' or 'blackmouth.' In each form of methemoglobinemia (see 617973), the heme iron is stabilized in the ferric form. Patients with the Hb M alpha forms are cyanotic at birth; those with the Hb M beta forms are usually not cyanotic until they are 3 months of age. Horst et al. (1987) showed that the Iwate mutation involves the alpha-1 globin gene. Specifically, they demonstrated a CAC-to-TAC mutation in codon 87 of that gene. They showed that the Iwate mutation can be identified directly on RsaI digestion. See Meyering et al. (1960), Shibata et al. (1961), Gerald and Efron (1961), Miyaji et al. (1962), Heller (1962), Heller et al. (1962), Tonz et al. (1962), Shibata (1964), Tamura (1964), Shimizu et al. (1965), Pik and Tonz (1966), Maggio et al. (1981), and Mayne et al. (1986).
Ameri et al. (1999) likewise determined that the molecular defect in 2 patients with Hb M (Kankakee) was his87 to tyr in the HBA1 gene. The proportion of Hb M (Kankakee) observed was higher than that predicted for an alpha-1-globin variant. They presented evidence suggesting that the greater-than-expected proportion of Hb M (Kankakee) results from preferential association of the electronegative beta-globin chains with the alpha-(M)-globin chains that are more electropositive than normal alpha-globin chains.
See Ohba et al. (1977) and Yi-Tao et al. (1982).
Substitution of glutamine for glutamic acid at alpha 23. A hemoglobin S homozygote who also carries this abnormal hemoglobin has a mild form of sickle cell anemia. See Kraus et al. (1965, 1967) and Cooper et al. (1973).
Fast hemoglobin. See Jones et al. (1963, 1968), Beckman et al. (1966), Labie and Rosa (1966), Quattrin and Ventruto (1967), Fessas et al. (1969), and Trabuchet et al. (1982).
See Honig et al. (1980). Erythrocytosis (ECYT7; 617981) is a clinical feature.
See Ohba et al. (1989).
No hematologic abnormality. See Iuchi et al. (1980).
See Knuth et al. (1979).
This variant was detected by chromatography in the course of screening diabetics for Hb A1c (Wajcman et al., 1980).
See Honig et al. (1978).
See Shibata et al. (1981).
Fast hemoglobin. See Ager et al. (1958), Baglioni (1962), Huntsman et al. (1963), Hanada et al. (1964), Imamura (1966), and Lehmann and Carrell (1969).
See Wajcman et al. (1989).
This hemoglobin showed an extremely high oxygen affinity. The patient, who had 'marginal erythrocytosis' (ECYT7; 617981), was shown to have 13.1% Hb Nunobiki (Shimasaki, 1985).
See Lie-Injo and Sadono (1958), Baglioni and Lehmann (1962), and Sansone et al. (1970).
Daud et al. (2001) investigated the occurrence of hemoglobin O (Indonesia) in related ethnic populations of the Indonesian archipelago. Nineteen individuals heterozygous for this variant were identified in 4 ethnic populations. The level of Hb O (Indonesia) in 17 of the individuals was 11.6 +/- 1.0%, significantly lower than the expected 17 to 22%, indicating the instability of Hb O (Indonesia).
See Vettore et al. (1974), Kilinc et al. (1985), and Martin et al. (1990). Schnedl et al. (1997) showed that the silent hemoglobin O Padova mutation causes an additional peak on high performance liquid chromatography (HPLC) and falsely low HbA(1c) values (glycated hemoglobin) when measured by HPLC. HPLC is the gold standard for evaluation of glycated hemoglobin in diabetes mellitus.
See Sugihara et al. (1982), Moo-Penn et al. (1982), and Yongsuwan et al. (1987). This has been shown to be a mutation of the HBA1 gene (Cash et al., 1989).
See Schneider et al. (1982).
See Vella et al. (1974) and Pootrakul et al. (1974).
Yodsowan et al. (2000) studied this variant in a 21-year-old Thai female and her mother. Turbpaiboon et al. (2002) reported a fourth case of Hb Siam in a healthy Thai female and concluded that there is no alpha-thalassemic effect of the variant.
This is a neutral-to-neutral change; it was detected in the course of mass screening by isoelectric focusing (Harano et al., 1986).
See Rahbar et al. (1976).
See Honig et al. (1981).
See Thillet et al. (1977) and Gonzalez Redondo et al. (1987).
See Brennan et al. (1977).
See Sukumaran et al. (1972) and Schmidt et al. (1976).
See Lorkin et al. (1970), Lie-Injo et al. (1979), and Higgs et al. (1980).
See Bardakdjian-Michau et al. (1989).
See Huisman and Sydenstricker (1962) and Reynolds and Huisman (1966). This has been shown to be a mutation of the HBA1 gene (Cash et al., 1989).
Masala et al. (1987) first described this variant as an electrophoretically slow-moving hemoglobin in 2 brothers affected by erythrocytosis (ECYT7; 617981) with slight microcytosis. In a large screening program involving 20,000 people in the city of Sassari and its surrounding area in Sardinia, Masala (1992) found the variant in 3 other apparently unrelated subjects. A male of German origin was identified by Bardakdjian-Michau et al. (1990) as a carrier of the same mutation. Sanna et al. (1994) demonstrated that the adult variant has increased oxygen affinity, a dramatic reduction of homotropic interactions, and a significant decrease of the effect of 2,3-diphosphoglycerate (35% lower than that observed for Hb A). The fetal variant also showed increased oxygen affinity compared with normal Hb F and an almost abolished heme-heme interaction.
Paglietti et al. (1998) demonstrated that Hb Sassari results from a GAC (asp)-to-CAC (his) mutation in the HBA1 gene.
See Szelenyi et al. (1980), Juricic et al. (1985), Ojwang et al. (1985), and Suarez et al. (1985).
No pathologic effects were observed (Sumida et al., 1973; Sumida, 1975).
See Wajcman et al. (1972), Nozari et al. (1977), Al-Awamy et al. (1985), and Abdo (1989). Schiliro et al. (1991) found this hemoglobin variant in Sicily.
Dincol et al. (2003) stated that Hb Setif was first described in an Algerian family (Wajcman et al., 1972) and subsequently in Iranian, African, Saudi Arabian, and Maltese populations. They identified the variant in a Turkish family. Heterozygotes were asymptomatic.
See Abramov et al. (1980).
See Zeng et al. (1982) and Yi et al. (1989).
See Yamaoka et al. (1960) and Hanada and Rucknagel (1964).
See Liang et al. (1981).
See Clegg et al. (1969).
See Vella et al. (1974).
See Bannister et al. (1972).
Felice (2003) cited evidence that Hb St. Luke's is a mutation of the HBA1 gene.
See Van Ros et al. (1968), North et al. (1980), and Rhoda et al. (1983). Costa et al. (1991) described a family with 1 homozygote and 3 heterozygotes for Hb Stanleyville II. The pattern of restriction fragments demonstrated an associated 3.7-kb alpha-globin gene deletion.
See Niazi et al. (1975) and Beksedic et al. (1975).
See Schroeder et al. (1979).
See Poyart et al. (1976) and Saenz et al. (1978). Erythrocytosis (ECYT7; 617981) is a clinical feature.
See Moo-Penn et al. (1987). Harano et al. (1996) observed this variant in a Japanese man with mild polycythemia (ECYT7; 617981).
See Pootrakul et al. (1977).
See Schneider et al. (1975).
See Harano et al. (1983).
See Beretta et al. (1968) and Prato et al. (1970).
See Nakatsuji et al. (1981).
This hemoglobin variant is associated with congenital Heinz body anemia (Ohba et al., 1987).
See Guis et al. (1985). This has been shown to be a mutation of the HBA1 gene (Cash et al., 1989).
See Miyaji et al. (1967). In Turkey, Bilginer et al. (1984) found the first instance of Hb Ube-2 outside Japan. It occurred in other members of the family.
Cotton et al. (2000) found this rare variant during universal neonatal screening. The patients had normal hematologic parameters. The variant was found in twins and an older sister and in the father; both parents were of Belgian ancestry.
Shin et al. (2002) described the disorder in a Taiwanese subject.
See Ohba et al. (1978).
This variant was found in a Chinese woman (Fleming et al., 1980). See Liang et al. (1988).
See Vella et al. (1973) and Nakatsuji et al. (1983). This has been shown to be a mutation of the HBA1 gene (Cash et al., 1989).
Since alpha-6 asp is involved in salt linkage with alpha-127 lys of the same chain, the increased oxygen affinity of hemoglobin variants at this position probably reflects loss of this salt bridge in the deoxy state. Similar changes have been observed for Hb St. Claude which also cannot form the salt bridge because of substitution of threonine for lysine at alpha-127. See Como et al. (1986).
See Zeng et al. (1981). Qualtieri et al. (1995) found this fast-migrating hemoglobin variant in a pregnant woman living in Italy.
See Barclay et al. (1969).
See Wajcman et al. (1990).
In the course of measuring hemoglobin A1c by automated cation exchange high performance liquid chromatography, Ohba et al. (1990) detected a new alpha-chain variant: substitution of alanine by threonine at position 110. The abnormal alpha chain comprised about 14% of the total alpha chain.
This hemoglobin, which has a high affinity for oxygen, was detected in a Japanese male during a screening survey. The proband was a 53-year-old man with liver cirrhosis and hemorrhagic gastritis (Hidaka et al., 1990).
Zwerdling et al. (1991) investigated the structural abnormality of a putative Hb E detected in an African American family with no apparent Asian ancestry. The tryptic peptide map formed by high performance liquid chromatography showed that the electrophoretic variant was indeed the beta glu26-to-lys mutation of Hb E. In addition, however, the tryptic map showed an abnormal alpha peptide. The second mutation was a substitution of arginine for lysine at residue 56 of the alpha chain. The variant was clinically silent.
See Wajcman et al. (1990).
See Wajcman et al. (1990, 1993).
See Vasseur et al. (1990). Substitution of glutamic acid for valine as the first residue in the mature protein is accompanied by retention of the initiator methionine residue. This may be the only known hemoglobin variant with an NH2-extension in the alpha-globin chain. Hb Marseille (141900.0171), Hb Doha (141900.0069), and Hb South Florida (141900.0266) are examples of hemoglobin variants with an NH2-extension due to retention of the initiator methionine in the beta-globin chain. Each is due to mutation in the first or second residue of the mature protein. Vasseur et al. (1992) found that elongation of the NH2-terminus of the alpha-chain, due to inhibition of cleavage of the initiator methionine which is then acetylated, modifies the 3-dimensional structure of hemoglobin at a region that is known to have an important role in the allosteric regulation of oxygen binding. Hb Thionville has a lowered affinity for oxygen. In contrast, response to 2,3-diphosphoglycerate is normal.
This variant was numbered based on the first amino acid of the mature protein. In the gene-based system of counting, this variant is VAL2GLY.
In the course of a high performance liquid chromatography survey of Hb A1c, Miyashita et al. (1992) detected a new hemoglobin in a 70-year-old Japanese male with cerebral infarction and erythremia (ECYT7; 617981). Further studies revealed a lys40-to-met mutation. The variant showed increased oxygen affinity, decreased heme-heme interaction, and a lowered 2,3-diphosphoglycerate effect.
(Erythremia, a now almost obsolete synonym for polycythemia and erythrocytosis, means increased red blood cell mass.)
In a diabetic woman of Scottish ancestry, Langdown et al. (1992) detected a new hemoglobin variant in the course of determining Hb A1c by high performance liquid chromatography. The abnormal hemoglobin chromatographed with the Hb A1c fraction. Family studies showed that a lys99-to-glu mutation, which was not associated with any hematologic disturbance, had occurred de novo. An AAG-to-GAG mutation was presumed and was not assigned to either the alpha-2- or alpha-1-globin chain.
The Hb A(1c) level in the patient of Langdown et al. (1992) was found to be very high. In a Japanese individual, Harano et al. (2003) likewise found an unexpectedly high Hb A(1c) level as measured by an automatic Hb A(1c) analyzer and found by DNA sequencing a change in the first nucleotide of codon 99 (AAG-GAG) of the Hb A1 gene.
Hemoglobin Zaire was found in a 36-year-old patient from Zaire during a systematic hemoglobin study. Wajcman et al. (1992) demonstrated that the abnormality was the insertion of 5 amino acids--his, leu, pro, ala, glu--between glu116 and phe117 of the alpha-globin chain. This sequence represented a tandem repeat of the 5 amino acid residues from 112 through 116, located at the end of the GH corner of the molecule. Hemoglobin Grady (141800.0045) involves the insertion of 3 amino acids as repeats of residues 116, 117 and 118. Unequal crossing over between alleles rather than between the separate alpha-1 and alpha-2 loci was thought to be the mechanism in that case and possibly in the case of Hb Zaire as well.
In a newborn infant and the father, a 35-year-old Pakistani man, Williamson et al. (1992) described a new hemoglobin with high oxygen affinity. The high affinity hemoglobin mutation was identified by HPLC peptide mapping and amino acid sequencing; leucine was substituted for histidine at amino acid position 89. The mutation occurred at the end of the F helix (FG1), a part of the hemoglobin structure critical in determining oxygen affinity since it is directly linked to the heme iron through the proximal histidine residue F8. This was the first example of a mutation at this position of the alpha chain of hemoglobin, although there were 2 high affinity mutants that involved the structurally equivalent amino acid (beta94 asp) of the beta chain: Hb Barcelona (beta94 his; 141900.0016) and Hb Bunbury (beta94 asn; 141900.0035). The new hemoglobin was called Hb Luton for the name of the hospital where the proband was originally treated. The proband was a neonate in whom 2 abnormal hemoglobin bands were found, the 2 bands being the mutant forms of fetal and adult hemoglobins containing the anomalous alpha globin. The father had microcytosis as well as mild polycythemia and was shown to have an accompanying alpha-thalassemia trait due to deletion of a single alpha-globin gene.
During a screening for hemoglobinopathies in Sardinia, Ferranti et al. (1993) found a new 'silent' hemoglobin variant in 5 apparently unrelated newborn babies. The variant was detected by means of isoelectric focusing (IEF), and further study revealed a valine for alanine substitution at position 71 of the alpha-globin chain. The substitution indicated that a C-to-T transition had occurred in the GCG codon for alanine which contains one of the 35 unmethylated CpG dinucleotides of the HBA1 gene. This observation brought to 13 the number of variants due to mutation in the CpGs of the HBA1 gene and raised the possibility that unmethylated CpGs, like methylated ones, may be hotspots for mutations.
In 3 Turkish children with severe thalassemia, Curuk et al. (1992) found a GGC-to-GAC mutation in codon 59 of the HBA1 gene resulting in a replacement of glycine by aspartic acid. The combination of an alpha-thal-1 deletion with the unstable Hb Adana resulted in a severe type of Hb H disease (613978).
During a routine program of hemoglobin screening performed in the United Arab Emirates, Abbes et al. (1992) found an electrophoretically fast-moving variant in a 9-month-old girl and in several members of her family. Amino acid sequencing demonstrated that the new variant had a gly18-to-asp substitution. Its functional properties were normal.
Hb Poitiers was discovered by Bardakdjian et al. (1994) in a 9-year-old French Caucasian boy who suffered from chronic anemia. The molecular defect consists of a missense mutation at codon 45 of the HBA1 gene, changing histidine to aspartate. Hb Poitiers displays a 2-fold increased oxygen affinity, a slightly decreased heme-heme interaction, and a slightly faster autooxidation rate. In adult hemoglobin (Hb A), the histidine residue at position 45 of the alpha-globin gene is the only polar contact between the heme group and globin. This position, however, seems to allow for moderate variation without dramatic consequences on the function of hemoglobin. His45 is replaced by glutamine in Hb Bari (141800.0009) and by arginine in Hb Fort de France (141800.0034).
Wajcman et al. (1993) discovered the Hb Caen variant in a 25-year-old French Caucasian woman suffering from a mild chronic hemolytic anemia. Trypsin degradation of the isolated hemoglobin alpha chain followed by high performance liquid chromatography indicated that the valine residue at position 132 was replaced by glycine.
Hb Yuda was discovered in a 65-year-old Japanese female with noninsulin-dependent diabetes mellitus (Fujisawa et al., 1992). Gas phase Edman degradation indicated that the abnormal hemoglobin alpha chain has a substitution of aspartic acid for alanine at residue 130. Hb Yuda has a very low oxygen affinity and slightly decreased cooperative subunit interaction.
Hb Capa was discovered in a 28-year-old female in Turkey who was being treated for chronic iron deficiency anemia. The hemoglobin showed abnormal electrophoretic mobility and was mildly unstable in a heat denaturation test. The molecular change was a GAC-to-GGC transition in codon 94, resulting in substitution of glycine for aspartic acid. Three other substitutions of asp-94 are known: Hb Setif (141800.0130), Hb Titusville (141800.0148), and Hb Sunshine Seth (141800.0143). All 4 variants exhibit mild instability.
Wajcman et al. (1992) demonstrated an asp126-to-tyr change in the HBA1 gene in an individual of Puerto Rican descent. At physiologic pH (7.4), the oxygen binding of the patient's red blood cells revealed a 40% reduction. Hb Montefiore appears to have lower cooperativity than other characterized alpha-126 mutants: aspartic acid is replaced by asparagine in Hb Tarrant (141800.0146), by histidine in Hb Sassari (141800.0126), and by valine in Hb Fukutomi (141800.0163).
A tyr140-to-his mutation in the HBA1 gene was discovered and characterized in a French patient with polycythemia (ECYT7; 617981) by Wajcman et al. (1992) and in a newborn baby of Ethiopian descent by Webber et al. (1992). This mutation provides an example of an alteration of the C terminus of the alpha chain, a region involved in the mechanisms of allosteric regulation. Hb Rouen has increased oxygen affinity and decreased cooperativity. A complementary tyr145-to-his mutation (Hb Bethesda; 141900.0022) in the hemoglobin beta chain has more dramatic effects, suggesting that the alpha and beta chains play unequal roles in the overall function of hemoglobin.
Hb Melusine was found in an Algerian patient during a systematic screening for hemoglobinopathies in Luxembourg. Using isoelectric focusing and reverse phase high performance liquid chromatography (RP-HPLC), Wajcman et al. (1993) determined that the molecular mutation at amino acid position 114 of the HBA1 gene changed the residue from proline to serine.
Girodon et al. (1992) reported the characterization of Hb Taybe, a hemoglobin variant discovered in a young Arabic woman suffering since birth from a severe and highly regenerative hemolytic anemia. DNA amplification and sequencing of the HBA1 gene indicated a 3-bp deletion (encoding threonine) at amino acid position 38 or 39. This variant increases the hydrophobicity of the amino acid chain, and it is quite unstable.
Wajcman et al. (1994) described a missense mutation involving the same codon as that involved in Hb Chesapeake (141800.0018), the first high oxygen affinity hemoglobin variant to be described in association with polycythemia (Charache et al., 1966). Hb Chesapeake has an arg92-to-leu substitution; Hb Cemenelum has an arg92-to-trp substitution. Hb J (Cape Town) (141800.0063) has a substitution (arg92-to-gln) in the same codon. Hb Cemenelum was discovered in a French diabetic patient with no hematologic abnormalities. The purified abnormal hemoglobin, like Hb J (Cape Town), displayed only a 1.5- to 2-fold increased oxygen affinity. The findings demonstrate that the degree to which the functional properties are altered by changes in key residues at the alpha-beta interface depends upon the specific residue occupying this position.
Hb Ramona was accidentally detected by isoelectrofocusing in a pregnant woman of part Spanish descent; its mobility was slightly faster than that of Hb A. A TAT-to-TGT change was found at codon 24, corresponding to a replacement of tyrosine by cysteine.
In a 72-year-old woman born in Czechoslovakia, Wajcman et al. (1994) found a lys7-to-asn mutation when investigating the basis for an abnormal level of Hb A1c. No abnormal hematologic features were observed.
In a 31-year-old man of Portuguese origin who had suffered from diabetes mellitus since the age of 15 years, Wajcman et al. (1994) found an abnormal hemoglobin during measurement of Hb A1c by an isoelectrofocusing study. There were no abnormal hematologic features.
Kister et al. (1995) described a new hemoglobin variant in a 73-year-old woman from Roanne in central France. She suffered from mild chronic hemolytic anemia. An asp94-to-glu substitution was found in the alpha-1 chain. Aspartate-94 is involved in several contacts, both in the deoxy- and oxy-structures of the hemoglobin.
Kazanetz et al. (1995) observed this variant hemoglobin in an adult male in Granada, Spain, who was evaluated because of severe iron deficiency anemia. Sequencing of the HBA1 gene showed 2 nucleotide changes. One was a simple polymorphism, as both GCG and GCT code for alanine (at codon 120). The second mutation was a GCC-to-TCC change at codon 123 resulting in replacement of alanine by serine. The replacement caused slight differences in the IEF and reversed-phase HPLC experiments, but the stability of the hemoglobin was normal. Family studies were not performed; thus, whether the 2 mutations were in coupling or repulsion was not known.
In 3 members of a Tunisian family, Darbellay et al. (1995) identified a leu129-to-pro substitution in the HBA1 gene by sequencing the entirety of the HBA2 and HBA1 genes. In the heterozygous state, the variant was manifested by microcytosis, whereas the homozygous state showed moderate anemia with marked microcytosis.
By tiny abnormalities observed during isoelectrofocusing, Wajcman et al. (1995) identified this electrophoretically silent variant in 3 members of a Caucasian-French family. This hemoglobin was the first alpha-chain variant that involved position 64. In the beta chain, the corresponding position, E14, is also occupied by an alanine residue; in Hb Seattle (141900.0256), it is replaced by aspartic acid (ala70-to-asp).
Wajcman et al. (1995) found this variant hemoglobin during a systematic study of the iron status in a 6-month-old baby and his mother who originated from Chad in North Central Africa.
Wajcman et al. (1995) found this variant in a 35-year-old pregnant woman of Caucasian origin who lived in Luxembourg. The abnormal Hb was also found in one of her daughters.
At the Fuchu Municipal Medical Center in Tokyo, Harano et al. (1995) identified 2 Hb variants in the course of assaying glycated hemoglobin, Hb A(1c), of the peripheral blood by cation exchange HPLC. Structural analyses demonstrated that 1 patient had a his72-to-tyr substitution and the other an asn97-to-his substitution (141800.0197) of the alpha-globin chain. These were named Hb Fuchu-I and Hb Fuchu-II, respectively. Both were healthy adults.
See 141800.0196.
In a 54-year-old Dutch woman under treatment for diabetes mellitus, Giordano et al. (1996) incidentally found a silent alpha-chain variant on testing for glycated hemoglobin. A CAC-to-CAA transversion was predicted to result in substitution of glutamine for histidine at residue 72 in the HBA1 gene.
Wajcman et al. (1998) described Hb J-Biskra, a variant hemoglobin consisting of deletion of 24 nucleotides from the HBA1 gene and 8 amino acid residues from the alpha-globin chain: residues 50-57, 51-58, or 52-59. This variant was mildly unstable in vitro only, and there was no hematologic or biochemical evidence of hemolysis in affected family members. Wajcman et al. (1998) stated that this was the largest deletion reported to that time in a hemoglobin molecule that is expressed at an almost normal level in the red blood cell.
Hb Godavari is the fourth example of a substitution involving neutral residues at position 95 of the alpha-1 chain. In all of these variants, the electrophoretic pattern suggested that the structural modification unmasks a charged residue in the alpha-1/beta-2 contact area. The other examples are Hb Denmark Hill, pro95 to ala (141800.0027); Hb G (Georgia), and pro95 to leu (141800.0038). Hb Godavari shared the same electrophoretic properties as these variants, but displayed minimal alterations of the oxygen-binding properties. Wajcman et al. (1998) identified Hb Godavari in 2 families of different ethnic origin. The first case, found in the Netherlands, involved an Indian patient. The second case was identified a few months later in an African family from Mali, living in France.
Hamaguchi et al. (1998) reported a neutral (silent) hemoglobin variant, designated Hb Oita, in which a change from CAC to CCC caused a his45-to-pro substitution. In Hb Bari (141800.0009), his45 is replaced by gln. In Hb Fort de France (141800.0034), his45 is replaced by arg. In Hb Portiers (141800.0176), his45 is replaced by asp.
In a Greek child with Hb H disease (613978), Traeger-Synodinos et al. (1999) found deletion of codon 62 of the alpha-1 gene, leading to alpha-plus-thalassemia. Codon 62 encodes a valine residue at the E11 alpha helix, which is located in the interior of the heme pocket. Substitutions of this valine with other amino acid residues in the alpha as well as beta polypeptide chains lead, in the heterozygous carrier, either to Hb M disease or to congenital nonspherocytic hemolytic anemia. Traeger-Synodinos et al. (1999) assumed that deletion of val at position 62 disrupted the conformation of the alpha chain to such an extent that the mutated subunit was rapidly removed by proteolysis. The final result was an alpha-thalassemia phenotype rather than an unstable hemoglobin syndrome. This conclusion was supported by the apparent absence of an abnormal alpha chain in the peripheral blood of the patient. Hb Evans (141850.0006) is a val62-to-met mutation of the HBA2 gene and was found in a patient with mild hemolytic anemia. Four amino acid substitutions at position 67(E11)val of the beta chain lead to instability of the Hb tetramer and an anemia of variable degrees in the heterozygotes. One of these substitutions, val67 to glu (141900.0163), results in the stable Hb M-Milwaukee-I.
Lacan et al. (1999) detected Hb Charolles in a 46-year-old patient who presented with microcytosis and hypochromia. It was easily detected by isoelectrofocusing and high performance liquid chromatography. It accounted for 11% of the total hemoglobin. The amino acid change resulted from a CAC-to-TAC change in codon 103.
In a French family from the north of France, Prehu et al. (1999) found a new HBA1 variant in 5 members. The variant was initially detected during measurement of glycated hemoglobin in a woman originating from Roubaix. Codon 55 in exon 2 was found to have a heterozygous change from GTT (val) to CTT (leu). This was a neutral variant.
In a woman from Cameroon, Prehu et al. (2001) identified a new hemoglobin variant, designated Hb Douala, with a C-to-T transition (TCT-TTT) in the HBA1 gene, resulting in a ser3-to-phe (S3F) amino acid substitution. The patient was also heterozygous for Hb S (141900.0243) and for a 3.7-kb deletional alpha-thalassemia.
In a patient of Iranian descent with the hematologic profile of alpha-plus-thalassemia characterized by mild microcytosis, Waye et al. (2001) found a 21-bp insertion/duplication that gave rise to a predicted alpha-globin chain containing a duplication of amino acid residues 93-99.
In a patient of Greek descent with the hematologic profile of alpha-plus-thalassemia characterized by mild microcytosis, Waye et al. (2001) found a 33-bp deletion in the HBA1 gene resulting in a predicted alpha-globin chain missing amino acid residues 64-74.
Harteveld et al. (2002) reported a 69-year-old Dutch woman monitored for diabetes mellitus in whom Hb A(L1c) analysis revealed a clinically silent hemoglobin variant, asn9 to lys (N9K), due to an AAC-to-AAG transversion in heterozygous state. The mutation was identical to that found at the same position in the HBA2 gene that leads to a variant named Hb Park Ridge (141850.0048).
In a 34-year-old Caucasian male of Swedish ancestry who lived in Saratoga Springs, New York, Hoyer et al. (2003) identified a hemoglobin variant with abnormal oxygen affinity, designated Hb Saratoga Springs. There was no family history of erythrocytosis. The patient had no smoking history. A change of codon 40 of the HBA1 gene from AAG to AAC resulted in a lys40-to-asn (K40N) change. Lys40 is replaced by glu in Hb Kariya (141800.0081), and by met in Hb Kanagawa (141800.0169).
In a 7-year-old girl living near the town of Die in southeast France, Lacan et al. (2004) identified a val93-to-ala (V93A) mutation in the HBA1 gene. The family was of French Caucasian origin.
In a 72-year-old woman of French Caucasian origin living in the city of Beziers in the south of France, Lacan et al. (2004) identified a lys99-to-asn (K99N) mutation in the HBA1 gene. The variant was found during the determination of Hb A(1c) by high performance liquid chromatography (HPLC) in this diabetic patient. Hematologic data were normal, without hepatomegaly or splenomegaly.
In a 32-year-old Somali male living in the Netherlands who was being monitored for diabetes mellitus, Harteveld et al. (2004) identified Hb S (141900.0243) in heterozygous state and a heterozygous C-to-G transversion in the HBA1 gene, resulting in a his89-to-gln (H89Q) substitution. The H89Q mutation had previously been described in a Yemenite woman and 2 apparently unrelated Somali males (Hoyer et al., 2002), and had been designated Hb Buffalo. No hematologic abnormality had been associated with the allelic variant in this or other cases. In addition to Hb Buffalo, 4 amino acid substitutions had been reported at codon 89: Hb Luton (his89 to leu; 141800.0172), Hb Villeurbanne (his89 to tyr; 141800.0213), Hb Tokyo (his89 to pro; 141800.0214), and Hb Tamano (his89 to arg; 141800.0215).
Deon et al. (1997) identified a his89-to-tyr (H89Y) mutation in the HBA1 gene as the defect in Hb Villeurbanne.
Harteveld et al. (2004) stated that Hb Tokyo carries a his89-to-pro (H89P) mutation in the HBA1 gene.
Harteveld et al. (2004) stated that Hb Tamano carries a his89-to-arg (H89R) mutation in the HBA1 gene.
In a 4-year-old Caucasian boy investigated for fatigue and microcytosis, Brennan et al. (2005) found a GGC-to-AGC transition at codon 51 in the HBA1 gene, resulting in a gly51-to-ser substitution (G51S). The mutation was thought not to be the cause of the microcytosis as it was detected also in the boy's father who had normal red cell indices.
In an 8-year-old black female of Surinamese origin with a mild alpha-thalassemia phenotype, Harteveld et al. (2005) identified homozygosity for a TGC-to-AGC transversion in the HBA1 gene, resulting in a cys104-to-ser substitution. Cysteine-104 is involved in alpha/beta globin contact and had been described as a critical amino acid of the HBA2 chain when substituted by a tyrosine (cys104 to tyr) in Hb Sallanches (141850.0031).
De Gobbi et al. (2006) studied 148 individuals from Melanesia with alpha-thalassemia, including 5 with HbH disease, in whom none of the theretofore described molecular defects could be found. The pattern of inheritance suggested that individuals with HbH disease were homozygous for a codominant defect, referred to as (alpha-alpha)T, causing alpha-thalassemia with a predicted genotype of (alpha-alpha)T/(alpha-alpha)T. In situ RNA hybridization in erythroid cells from an affected individual from Lamen Island (Vanuatu) detected substantially fewer nuclear transcripts from the alpha-globin genes than from the beta-globin genes. DNA FISH in 2 affected individuals showed that the alpha-globin cluster was present at its normal location of chromosome 16, and no deletions or chromosomal rearrangements were detected in any of these individuals. Linkage analysis showed that the disease phenotype in individuals was derived from telomeric chromosome 16 T. Only the C allele of SNP195 (C or T, located at coordinate 149709) segregated with thalassemia in the affected families and showed complete association with the (alpha-alpha)T haplotype. This allele was not found in a separate analysis of 131 nonthalassemic Melanesian individuals. SNP195 changes the sequence 5-prime-TAATAA-3-prime (T allele) to 5-prime-TGATAA-3-prime (C allele), potentially creating a new binding site for the key erythroid transcription factor GATA1. GATA1 binds at the C allele of SNP195 in vivo. SNP195 creates a new promoter-like element between the upstream regulatory elements and their cognate promoters. This element, when activated, causes significant downregulation of the alpha-D, alpha-2, and alpha-1 genes that lie downstream, thereby causing alpha-thalassemia.
In a newborn of mixed black and Chinese descent who carried the Southeast Asian alpha-0-thal deletion, Eng et al. (2006) also found a 1-bp deletion of cysteine from codon 78 in exon 2 of the HBA1 gene, resulting in a frameshift and premature termination at codon 83.
In a 27-year-old woman with mild compensated hemolytic anemia, Brennan and Matthews (1997) identified Hb Auckland, a his87-to-asn substitution in the HBA1 gene.
HEMOGLOBIN J (INDIA). See Raper (1957).
HEMOGLOBIN J (MALAYA). See Lehmann (1962).
HEMOGLOBIN K (CALCUTTA). Fast hemoglobin. See Lehmann (1962).
HEMOGLOBIN K (MADRAS). See Ager and Lehmann (1957).
HEMOGLOBIN KARAMOJO. See Allbrook et al. (1965).
HEMOGLOBIN L (BOMBAY). See Sukumaran and Pik (1965).
HEMOGLOBIN M (RESERVE). Reduced oxygen affinity and decreased reversible oxygen-binding capacity (Overly et al., 1967).
HEMOGLOBIN N, ALPHA TYPE. An alpha chain anomaly was deduced from molecular hybridization experiments with canine hemoglobin (Silvestroni et al., 1963). Other hemoglobin N variants have a beta change.
HEMOGLOBIN NICOSIA. See Fessas et al. (1965).
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