HGNC Approved Gene Symbol: G6PD
Cytogenetic location: Xq28 Genomic coordinates (GRCh38): X:154,531,390-154,547,569 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| Xq28 | {Resistance to malaria due to G6PD deficiency} | 611162 | 3 | |
| Hemolytic anemia, G6PD deficient (favism) | 300908 | X-linked | 3 |
Glucose-6-phosphate dehydrogenase (G6PD; EC 1.1.1.49) plays a key role in the production of ribose 5-phosphate and the generation of NADPH in the hexose monophosphate pathway. Because this pathway is the only NADPH-generation process in mature red cells, which lack the citric acid cycle, a genetic deficiency of G6PD (300908) is often associated with adverse physiologic effects (summary by Takizawa et al., 1986).
Takizawa et al. (1986) cloned G6PD from a human hepatoma cDNA library. The deduced 531-amino acid protein has a molecular mass of 58 kD. Cappellini and Fiorelli (2008) stated that the G6PD protein contains 515 amino acids.
Martini et al. (1986) determined that the human G6PD gene has 13 exons and spans 18 kb. The protein-coding region is divided into 12 segments, ranging from 12 to 236 bp, and an intron is present in the 5-prime untranslated region. The major 5-prime end of mature G6PD mRNA in several cell lines is located 177 bp upstream of the translation-initiating codon. Comparison of the promoter region of G6PD and 10 other housekeeping enzyme genes confirmed the presence of common features. In particular, in 8 cases in which a 'TATA' box was present, a conserved sequence of 25 bp was seen immediately downstream.
Chen et al. (1991) determined the sequence of 20,114 bp of human DNA including the G6PD gene. The region included a prominent CpG island, starting about 680 nucleotides upstream of the transcription initiation site, extending about 1,050 nucleotides downstream of the initiation site, and ending at the start of the first intron. The transcribed region from the initiation site to the poly(A) addition site covered 15,860 bp. The sequence of the 13 exons agreed with the published cDNA sequence and, for the 11 exons tested, with the corresponding sequence in a yeast artificial chromosome (YAC). Sixteen Alu sequences constituted 24% of the total sequence tract. Four were outside the borders of the mRNA transcript of the gene; all of the others were found in a large (9,858 bp) intron between exons 2 and 3.
The Japanese pufferfish Fugu rubripes is a useful model for the comparative study of vertebrate genomes because of the compact nature of its genome. Since the Fugu genome is approximately 8 times smaller than that of mammals, most genes should be more compact. To test this hypothesis, Mason et al. (1995) cloned and sequenced the G6PD gene from Fugu and compared it to the corresponding human gene. The intron/exon structure of the 2 genes was identical throughout the protein coding regions. Intron 2 is also the largest intron in both species. However, they found that the Fugu gene was 4 times smaller than the human gene; the difference was accounted for by the fact that the pufferfish gene has smaller introns. Mason et al. (1995) constructed a molecular phylogeny for 10 G6PD protein sequences. The sequences fell in the expected arrangement based on established phylogenetic relationships, with the Plasmodium falciparum sequence diverging most widely.
Fusco et al. (2012) stated that the G6PD gene, which is transcribed in the telomeric direction, partly overlaps the IKBKG gene (300248), which is transcribed in the centromeric direction. The genes share a conserved promoter region that has bidirectional housekeeping activity. In addition, intron 2 of the G6PD gene contains an alternate promoter for the IKBKG gene only. Fusco et al. (2012) determined that the region containing the G6PD gene and the 5-prime end of the IKBKG gene contains Alu elements.
Notaro et al. (2000) showed that an evolutionary analysis is a key to understanding the biology of a housekeeping gene such as G6PD. From the alignment of the amino acid sequence of 52 G6PD species from 42 different organisms, they found a striking correlation between the amino acid replacements that cause G6PD deficiency in humans and the sequence conservation of G6PD. Two-thirds of such replacements were found in highly and moderately conserved (50 to 99%) amino acids; relatively few were located in fully conserved amino acids (where they might be lethal) or in poorly conserved amino acids (where presumably they simply would not cause G6PD deficiency). The findings were considered consistent with the notion that all human mutants have residual enzyme activity and that null mutations are lethal at some stage of development. Comparing the distribution of mutations in the human housekeeping gene with evolutionary conservation is a useful tool for pinpointing amino acid residues important for the stability or the function of the corresponding protein.
Childs et al. (1958) determined that the G6PD gene resides on the X chromosome.
From study of radiation-induced segregants (irradiated human cells 'rescued' by fusion with hamster cells), Goss and Harris (1977) showed that the order of 4 loci on the X chromosome is PGK: alpha-GAL: HPRT: G6PD and that the 3 intervals between these 4 loci are, in relative terms, 0.33, 0.30, and 0.23.
Studying X-autosome translocations in somatic cell hybrids, Pai et al. (1980) showed that a breakpoint at the junction of Xq27-q28 separates HPRT from G6PD. G6PD is distally situated at Xq28. They localized HPRT to the segment between Xq26 and Xq27.
That G6PD is X-linked in the mouse was supported by Epstein's finding (1969) that oocytes of XO females have half as much G6PD as do oocytes of XX female mice. The level of lactate dehydrogenase was the same. Epstein's conclusion was that the G6PD gene is X-linked in the mouse, that synthesis occurs in the oocyte and is dosage-dependent, and that X inactivation does not occur in oocytes.
Ninfali et al. (1995) studied muscle expression of G6PD in normal individuals and in persons with G6PD deficiency of 3 types. They were prompted to undertake these studies because of patients with symptoms such as myalgia, cramps, and muscle weakness under conditions of stress, particularly physical exertion. All 3 variants--Mediterranean (305900.0006), Seattle-like (305900.0010), and G6PD A- (305900.0002)--showed the enzyme defect in muscle. A statistically significant relationship was found in the activity of G6PD in erythrocytes and muscle of male subjects. The results suggested to the authors that, for a given variant, the extent of the enzyme defect in muscle can be determined from the G6PD activity of erythrocytes, using an equation that they derived.
In studies in bovine aortic and human coronary artery endothelial cells, Leopold et al. (2007) demonstrated that aldosterone decreased G6PD expression and activity, resulting in increased oxidant stress and decreased nitric oxide levels, similar to what is observed in G6PD-deficient endothelial cells. Aldosterone decreased G6PD expression by increasing expression of the cAMP-response element modulator (CREM; 123812), thereby inhibiting cAMP-response element binding protein (CREB; 123810)-mediated G6PD transcription. In vivo aldosterone infusion in mice decreased vascular G6PD expression and impaired vascular reactivity; these effects were abrogated by spironolactone or vascular gene transfer of G6pd. Leopold et al. (2007) concluded that aldosterone induces a G6PD-deficient phenotype to impair endothelial function.
Different variants of G6PD are found in high frequency in African, Mediterranean, and Asiatic populations (Porter et al., 1964), and heterozygote advantage vis-a-vis malaria (Luzzatto et al., 1969) has been invoked to account for the high frequency of the particular alleles in particular populations.
The variety of forms of the G6PD enzyme is great (Yoshida et al., 1971; Beutler and Yoshida, 1973; Yoshida and Beutler, 1978). The World Health Organization (WHO (1967, 1967)) gave its attention to problems of nomenclature and standard procedures for study. The demonstrated polymorphism at this X-linked locus rivals that of the autosomal loci for the polypeptide chains of hemoglobin. As in the latter instance, single amino acid substitution has been demonstrated as the basis of the change in the G6PD molecule resulting from mutation (Yoshida et al., 1967).
The G6PD variants have been divided into 5 classes according to the level of enzyme activity: class 1--enzyme deficiency with chronic nonspherocytic hemolytic anemia; class 2--severe enzyme deficiency (less than 10%); class 3--moderate to mild enzyme deficiency (10-60%); class 4--very mild or no enzyme deficiency (60%); class 5--increased enzyme activity. Mutations causing nonspherocytic hemolytic anemia are clustered near the carboxy end of the enzyme, in the region between amino acids 362 and 446, whereas most of the clinically mild mutations are located at the amino end of the molecule. As the intragenic defects have been identified, many variants that were thought to be unique have been found to be identical on sequence analysis. This finding should not be surprising inasmuch as the methods of biochemical characterization are not very accurate, particularly when dealing with mutant enzymes that are unstable. For example, although the patients were unrelated, G6PD Marion, G6PD Gastonia, and G6PD Minnesota had the same val213-to-leu substitution; and G6PD Nashville and G6PD Anaheim were found to have the same arg393-to-his substitution (Beutler et al., 1991).
The frequencies of low-activity alleles of G6PD in humans are highly correlated with the prevalence of malaria (see 611162). These deficiency alleles are thought to provide reduced risk for infection by the Plasmodium parasite and are maintained at high frequency despite the illnesses that they cause. Haplotype analysis of A- (305900.0002) and Mediterranean (Med) (305900.0006) mutations at this locus indicates that they had evolved independently and have increased in frequency at a rate that is too rapid to be explained by random genetic drift. Tishkoff et al. (2001) used statistical modeling to demonstrate that the A- allele arose within a past 3840 to 11,760 years and the Med allele arose within the past 1600 to 6640 years. Tishkoff et al. (2001) concluded that their results support the hypothesis that malaria has had a major impact on humans only since the introduction of agriculture within the past 10,000 years and provide a striking example of the signature of selection on the human genome.
That resistance to severe malaria is the basis of the high frequency of G6PD deficiency and that both hemizygotes and heterozygotes enjoy an advantage was established by Ruwende et al. (1995) in 2 large case-control studies of more than 2,000 African children. They found that the common African form of G6PD deficiency (G6PD A-; 305900.0002) was associated with a 46 to 58% reduction in risk of severe malaria for both female heterozygotes and male hemizygotes. A mathematical model incorporating the measured selective advantage against malaria suggested that a counterbalancing selective disadvantage, associated with this enzyme deficiency, has retarded its rise in frequency in malaria-endemic regions.
Sansone et al. (1981) described 6 G6PD variants in Italian males, all associated with enzyme deficiency and 2 with signs of hemolysis. They provided a useful map of 19 sporadic G6PD variants found in Italy. They mapped to regions where the common forms of G6PD deficiency are frequent.
Hitzeroth and Bender (1981) found an increasing frequency of apparent BB homozygotes with increasing age of groups of South African blacks studied. They suggested that this represents selection against A- cell lines in heterozygotes and speculated further that malaria is the underlying selective agent.
Mohrenweiser and Neel (1981) identified thermolabile variants of lactate dehydrogenase B, glucosephosphate isomerase, and glucose-6-phosphate dehydrogenase. None was detectable as a variant by standard electrophoretic techniques. All were inherited. Beutler (1983) hypothesized that the marked differences in the extent to which various tissues manifest the deficiency state in various enzymopathies including G6PD deficiency may be related to tissue-to-tissue differences in proteases. Mutation may produce changes in susceptibility of the enzyme to proteases.
Data on gene frequencies of allelic variants were tabulated by Roychoudhury and Nei (1988).
Vulliamy et al. (1988) cloned and sequenced 7 mutant G6PD alleles. A single point mutation in the African variant G6PD A (305900.0001) does not result in deficiency of the enzyme. The other 6 mutants were all associated with enzyme deficiency. Single point mutations were identified in G6PD Mediterranean (305900.0006), G6PD Metaponto (305900.0007), G6PD Ilesha (305900.0004), G6PD Chatham (305900.0003), G6PD Santiago de Cuba (305900.0009), and G6PD Matera (an example of A-; 305900.0002).
By use of 14 unique sequence probes and 18 restriction enzymes, D'Urso et al. (1988) found a polymorphic silent mutation in the G6PD gene. A PstI site that maps to exon 10 was monomorphic in all British and Italian subjects studied, but was polymorphic in West African people. Specifically, it was absent from 22% of Nigerian X chromosomes. By sequence analysis, D'Urso et al. (1988) showed that the absence of this PstI site resulted from a G-to-A replacement at position 1116, corresponding to the third base of a glutamine codon (see 305900.0017). No amino acid change was produced in the protein. Yoshida et al. (1988) reported 2 RFLPs of the G6PD locus with high frequency in blacks and showed statistically significant linkage disequilibrium between the A+/B+ types and 1 of the RFLPs at the G6PD locus.
Vulliamy et al. (1988) found a striking predominance of C-to-T transitions among the G6PD mutations, with GC doublets involved in 4 of the 7 cases. It has been found that even in the same population, more than 1 G6PD variant is present. For example, in the island of Sardinia, extensive clinical and biochemical studies identified 4 different G6PD variants. De Vita et al. (1989) cloned and sequenced the 4 G6PD variants and found that at the molecular level there were only 2 mutations. The first mutation had an asp282-to-his change resulting from a GAT-to-CAT change in exon 8. This mutation caused the G6PD Seattle-like phenotype, a relatively mild form of G6PD deficiency (see 305900.0010). The other 3 variants were accompanied by very severe G6PD deficiency. All 3 had a ser188-to-phe change resulting from a TCC-to-TTC transition. This is the same change as that in G6PD Mediterranean (305900.0006). These 3 Sardinian variants also had a silent mutation in exon 11 with a change of TAC-to-TAT, both of which encode tyrosine at amino acid 437. These findings indicate that some G6PD-deficient variants identified only on the basis of their biochemical characteristics may not correspond to different mutations in the G6PD gene. The variations may be due to posttranscriptional or posttranslational modifications of the enzyme; whether the modifications are due to mutations in a tightly linked gene or to noninherited physiologic changes could not be distinguished with the data available. Study of families in which different forms of G6PD Mediterranean segregate suggested that the biochemical characteristics are transmitted in the family along with the enzyme deficiency, thus favoring the first hypothesis.
In a study of an unselected sample of 1,524 schoolboys from the province of Matera (Lucania) in southern Italy, Calabro et al. (1990) found that although the most frequent form of G6PD deficiency was G6PD Mediterranean, an extraordinary number of other forms existed. The overall rate of G6PD deficiency was 2.6%. The frequency ranged from 7.2% on the Ionian coast to zero on the eastern side of the Lucanian Apennines.
Kay et al. (1992) analyzed the evolution of the G6PD gene by examining the DNA samples from 54 male African Americans for G6PD A+ (305900.0001), G6PD A- (305900.0002), and G6PD B and for polymorphisms in intron 5 (PvuII), at nucleotide 1311 (305900.0018), and at nucleotide 1116 (305900.0017). They concluded from these and their previous studies that G6PD B is the most ancient genotype. The nucleotide 1311 mutation, with its worldwide distribution, probably occurred next. The PstI mutation, limited to Africans, probably arose next and is more ancient than the A+ mutation, which occurred in a gene without either the PstI or the 1311 mutation. G6PD A- (202A/376G) is the most recent mutation and is still in linkage disequilibrium with all of the sites. It presumably occurred in an individual with both the A+ and PvuII mutations.
Chiu et al. (1993) reported molecular characterization of the defects in 43 G6PD-deficient Chinese males whose G6PD had been well characterized biochemically. Among the 43 samples, they identified 5 different nucleotide substitutions: 1388G-A (arg to his; 305900.0029); 1376G-T (arg to leu; 305900.0021); 1024C-T (leu to phe; 305900.0046); 392G-T (gly to val; 305900.0045); and 95A-G (his to arg; 305900.0044). The 5 substitutions accounted for 36 of the 43 samples; none of these substitutions had been reported in non-Asians. The substitutions at nucleotides 392 and 1024 were new findings. The substitutions at nucleotides 1376 and 1388 accounted for over one-half of the samples.
Vulliamy et al. (1993) tabulated 58 different mutations in the G6PD gene that account for 97 named G6PD variants. The mutations were almost exclusively missense mutations, causing single amino acid substitutions. They were spread throughout the coding region of the gene, although there appeared to be a clustering of mutations that caused a more severe clinical phenotype towards the 3-prime end of the gene. The absence of large deletions, frameshift mutations, and nonsense mutations was considered consistent with the notion that a total lack of G6PD activity would be lethal.
Miwa and Fujii (1996) listed the mutations responsible for about 78 G6PD variants.
Mason (1996) reviewed information on the G6PD enzyme and on mutations in the gene. A map of 515 amino acids showing the location of mutations, including double mutations, was provided.
Filosa et al. (1996) analyzed fractionated blood cells in 4 heterozygotes for the class 1 G6PD mutations G6PD Portici (305900.0008) and G6PD Bari (1187G-T). In erythroid, myeloid, and lymphoid cell lineages there was a significant excess of G6PD-normal cells, suggesting that a selective mechanism operates at the level of pluripotent blood stem cells. They concluded that their studies provided evidence that severe G6PD deficiency adversely affects the proliferation or survival of nucleated blood cells.
Liu et al. (1997) reported a method of determination of clonality using allele-specific PCR (ASPCR) to detect exonic polymorphisms in p55 (305360) and G6PD. They demonstrated a significant sex difference in allele frequencies in African Americans but not in Caucasians, and linkage disequilibrium for the p55 and G6PD alleles in Caucasians but not in African Americans.
Vulliamy et al. (1998) determined the causative mutation in 12 cases of G6PD deficiency associated with chronic nonspherocytic hemolytic anemia. In 11 cases, the mutation they found had previously been reported in unrelated individuals. These mutations comprised 7 different missense mutations and a 24-bp deletion, G6PD Nara (305900.0052), previously found in a Japanese boy. Repeated findings of the same mutations suggest that a limited number of amino acid changes can produce the chronic nonspherocytic hemolytic anemia phenotype and be compatible with normal development. They found 1 new mutation, G6PD Serres (305900.0051).
Cappadoro et al. (1998) presented evidence suggesting that early phagocytosis of G6PD-deficient erythrocytes parasitized by Plasmodium falciparum may explain malaria protection in G6PD deficiency.
Kwok et al. (2002) described a Web-accessible database of G6PD mutations. The relational database integrates up-to-date mutational and structural data from various databanks with biochemically characterized variants and their associated phenotypes obtained from published literature and a Favism website.
Barisic et al. (2005) identified 5 different mutations in the G6PD gene in 24 unrelated males with G6PD deficiency from the Dalmatian region of southern Croatia. The variants included Cosenza (305900.0059) (37.5% of patients), Mediterranean (305900.0006) (16.6%), Seattle (12.5%), Union (12.5%), Cassano (4.2%), and a novel variant, termed G6PD Split (305900.0059) (4.2%). The variants in 3 patients (12.5%) were uncharacterized.
Ninokata et al. (2006) identified G6PD deficiency in 9.8% of males and 10.4% of females among 345 healthy adults on Phuket island in southern Thailand. Although none of the individuals had molecular evidence of malaria infection, the findings suggested that malaria endemics had occurred in the past and that G6PD deficiency has been maintained as an advantageous genetic trait in this population. At least 5 different G6PD variants were identified, suggesting that several Asian ethnic groups, such as Burmese, Laotian, Cambodian, Thai, and Chinese, participated in establishing the current ethnic identity of the population of Phuket.
Jiang et al. (2006) identified 14 different mutations in the G6PD gene among 1,004 G6PD-deficient Chinese individuals comprising 11 ethnic groups. The variants varied in frequency across the ethnic groups and correlated geographically with historical patterns of malaria. The variants were different from those reported in African, European, and Indian populations. The most common variants in the Chinese population were G6PD Kaiping (R463H; 305900.0029) and G6PD Canton (R459L; 305900.0021), accounting for over 60% of G6PD-deficient individuals, and Gaohe (H32R; 305900.0044). In vitro functional expression studies in E. coli showed significantly decreased enzyme activity for all 3 mutant proteins. All 3 variants showed decreased Km for G6P, but whereas the Canton and Kaiping variants had increased Km for NADP+, the Gaohe variant showed decreased Km for NADP+, likely reflecting compensation in the latter variant. Jiang et al. (2006) concluded that residues arg459 and arg463 play an important role in anchoring NADP+ to the catalytic domain of the enzyme.
Miwa and Fujii (1996) stated that most of the class 1 G6PD variants associated with chronic hemolysis have the mutations surrounding either the substrate- or NADP-binding site.
Costa et al. (2000) pointed out that G6PD mutants causing class 1 variants (the most severe forms of the disease) cluster within exon 10, in a region that, at the protein level, is believed to be involved in dimerization. They identified a class 1 variant mapping to exon 8 (305900.0053).
Longo et al. (2002) crossed mouse chimeras from embryonic stem cells in which the G6pd gene had been targeted with normal females. First-generation G6pd heterozygotes born from this cross were essentially normal; their tissues demonstrated strong selection for cells with the targeted G6pd allele on the inactive X chromosome. When these first-generation heterozygous females were bred to normal males, only normal G6pd mice were born. There were 3 reasons for this: hemizygous G6pd male embryos' development was arrested from embryonic day 7.5, the time of onset of blood circulation, and they died by embryonic day 10.5; heterozygous G6pd females showed abnormalities from embryonic day 8.5, and died by embryonic day 11.5; and severe pathologic changes were present in the placenta of both G6pd hemizygous and heterozygous embryos. Thus, G6PD is not indispensable for early embryonic development; however, severe G6PD deficiency in the extraembryonic tissues (consequent on selective inactivation of the normal paternal G6PD allele) impairs the development of the placenta and causes death of the embryo. Most importantly, G6PD is indispensable for survival when the embryo is exposed to oxygen through its blood supply.
In ischemia-reperfusion experiments on isolated mouse hearts, Jain et al. (2004) demonstrated that G6pd is rapidly activated without a change in G6pd protein levels. G6pd -/- hearts had greatly impaired cardiac relaxation and contractile performance, associated with depletion of total glutathione stores and impaired generation of reduced glutathione, compared to wildtype hearts. Increased ischemia-reperfusion injury was reversed by antioxidant treatment but unaffected by supplementation of ribose stores. Jain et al. (2004) concluded that G6PD is an essential myocardial antioxidant enzyme, required for maintaining cellular glutathione levels and protecting against oxidative stress-induced cardiac dysfunction during ischemia-reperfusion.
Polymorphism at the G6PD locus has made it a useful X-chromosome marker, like the colorblindness and Xg blood group loci; close linkage of the colorblindness loci, the G6PD locus, and the hemophilia A locus (Adam et al., 1967; Boyer and Graham, 1965) has been demonstrated. Also, as a biochemical phenotype identifiable at the cellular level, G6PD variants have been useful in somatic cell genetics, permitting, for example, one of the critical proofs in man of the Lyon hypothesis (Davidson et al., 1963).
The relative stability of the X chromosome during evolution has been shown by the fact that the G6PD locus is X-borne also in a number of other species (Ohno, 1967). G6PD and HPRT are linked in the Chinese hamster (Rosenstraus and Chasin, 1975) and presumably are on the X chromosome as in man. By study of cell hybrids, Shows et al. (1976) found that HPRT and G6PD are closely linked in the Muntjac deer. Smith et al. (1976) found G6PD deficiency in a male Weimaraner dog, but were not able to do genetic studies. Alpha-GAL, HPRT, PGK and G6PD are X-linked in the rabbit, according to mouse-rabbit hybrid cell studies (Cianfriglia et al., 1979; Echard and Gillois, 1979). By comparable methods, Hors-Cayla et al. (1979) found them to be X-linked also in cattle. According to cell hybridization studies, HPRT, G6PD, and PGK are X-linked in the pig (Gellin et al., 1979) and in sheep (Saidi et al., 1979). Using pulsed field gel electrophoresis, Faust et al. (1992) demonstrated that, in the mouse, Gdx (312070), P3 (312090), and G6pd are physically linked to the X-linked visual pigment locus (Rsvp) within a maximal distance of 340 kb, while G6pd and f8 (300841) are approximately 900 kb apart.
Takizawa and Yoshida (1987) reported that the G6PD A+ gene has an A-to-G transition, resulting in the substitution of aspartic acid for asparagine as the 142nd amino acid from the N-terminus of the enzyme.
G6PD Hektoen is characterized by increased red cell enzyme activity. It is, therefore, a class 5 G6PD variant. It was first described by Dern et al. (1969). Yoshida (1970) thought that the variant peptide had replacement of histidine by tyrosine. Later, Yoshida (1996) was uncertain about this conclusion and stated that the basic defect remained to be identified.
See Kirkman et al. (1964) and Yoshida et al. (1967). Vulliamy et al. (1988) found that the G6PD A variant is the same as 1 of the 2 variants identified in G6PD A- (305900.0002), i.e., asn126-to-asp. They noted that G6PD A, which is widely distributed in Africa, is not associated with deficiency of the enzyme.
Hirono and Beutler (1988) showed that a mutation responsible for the G6PD A- phenotype present in enzyme-deficient (300908) West African and American blacks occurred in a gene that produces the G6PD A+ phenotype. A substitution of guanine for adenine at nucleotide 376 (in exon 5) was found in all G6PD A+ and G6PD A- samples but in none of the G6PD B+ samples examined. Substitution of adenine for guanine at nucleotide 202 was found in 4 of 5 G6PD A- samples; this change is apparently responsible for the in vivo instability of the enzyme protein. Thus, the difference distinguishing the A and B forms of G6PD is the amino acid at residue 126 (see 305900.0002). Presumably as the result of alternative splicing, there is considerable heterogeneity among different G6PD cDNAs.
Both the variant A (with enzyme activity in the normal range, also called A) and the variant A- (associated with enzyme deficiency) have a frequency of about 0.2 in several African populations. Two restriction fragment length polymorphisms have also been found in people of African descent but not in other populations, whereas a silent mutation has been shown to be polymorphic in Mediterranean, Middle Eastern, African, and Indian populations. Vulliamy et al. (1991) reported 2 additional polymorphisms detected by sequence analysis, one in intron 7 and one in intron 8. Analysis of 54 African males for the 7 polymorphic sites clustered within 3 kb of the G6PD gene showed only 7 of the 128 possible haplotypes, thus indicating marked linkage disequilibrium. These data enabled Vulliamy et al. (1991) to suggest an evolutionary pathway for the different mutations, with only a single ambiguity. The mutation underlying the A variant is the most ancient and the mutation underlying the A- variant is the most recent. Since it seemed reasonable that the A- allele is subject to positive selection by malaria, whereas the other alleles are neutral, Vulliamy et al. (1991) suggested that G6PD may lend itself to the analysis of the role of random genetic drift and selection in determining allele frequencies within a single genetic locus in human populations.
Babalola et al. (1976) predicted that the A- mutation may have occurred in an individual carrying the A+ mutation. A black individual with the G6PD A- phenotype but no mutation at nucleotide 202 suggested that this individual may have another mutation that caused instability and thus deficiency of the enzyme. Yoshida and Takizawa (1988) presented evidence that the A- gene evolved by stepwise mutations through the A+ gene.
Vulliamy et al. (1988) cloned and sequenced 7 mutant G6PD alleles. A single point mutation in the African variant G6PD A does not result in deficiency of the enzyme. The other 6 mutants, including G6PD A-, were all associated with enzyme deficiency. Two different point mutations were found in G6PD A-, 1 of which was the same as that in G6PD A. See Yoshida et al. (1967). Hirono and Beutler (1988) demonstrated a substitution of methionine for valine at position 68 resulting from a G-to-A change at nucleotide 202 (in exon 4). The in vivo instability of the enzyme is the result of this change. The gene also has the change at amino acid 126 characteristic of G6PD A. See Vulliamy et al. (1988).
Beutler et al. (1989) performed haplotyping with 4 polymorphic restriction sites in the G6PD locus in DNA samples from 29 males with the G6PD A- phenotype and 14 males with a G6PD B phenotype. All G6PD A- subjects with the G6PD A- (202A/376G) genotype, regardless of population origin, shared identical haplotypes. The 5 populations screened were black (16), Puerto Rican (2), Mexican (2), white US (1), and Spanish (3). One G6PD A- male was of the 376G/680T genotype and 2 were of the 376G/968C genotype. One of the restriction sites is uncommon in the populations studied; thus, Beutler and Kuhl (1990) considered it likely that the G6PD A- mutation at nucleotide 202 arose relatively recently and in a single person.
Calabro et al. (1990) found this mutation, regarded as characteristically African, in an unselected sample of 1,524 schoolboys of the province of Matera in Southern Italy.
Beutler et al. (1991) found that 3 previously reported electrophoretically fast Mexican G6PD variants--G6PD Distrito Federal (Lisker et al., 1981), G6PD Tepic (Lisker et al., 1985), and G6PD Castilla (Lisker et al., 1977)--all showed the changes characteristic of G6PD A- (202A/376G) and had the haplotype characteristic of G6PD A- in Africa. G6PD Betica (Vives-Corrons and Pujades, 1982; Vives-Corrons et al., 1980), which is frequent in Spain, also had the same characteristics. Since the PvuII+ genotype is rare in Europe, the G6PD Betica mutation was presumably imported from Africa.
Hirono and Beutler (1988) found 2 other mutations that produced the G6PD A- phenotype: arg227-to-leu and leu323-to-pro. In both cases the mutations existed on the G6PD A background, i.e., the asn126-to-asp substitution.
Town et al. (1992) demonstrated that both the val68-to-met and the asn126-to-asp mutations found in G6PD A- are necessary to produce the G6PD-deficient phenotype (rather than the val68-to-met mutation having happened to arise in an A+ gene in the first instance). They approached the question by introducing G6PD B, A, A-, and G6PD val68-to-met in a bacterial expression system and analyzing their biochemical properties. With each of the 2 mutations alone, they found a slight decrease in both the specific activity and the yield of enzyme protein when compared to G6PD B. When both mutations were introduced together, there was a roughly additive effect on specific activity, but a much more drastic effect on enzyme yield which was reduced to 4% of normal. They inferred that the coexistence of the 2 mutations acted synergistically in causing instability of the enzyme. This would explain why a B- phenotype has only very rarely been observed. (Comparable results were produced when the replacement gln119-to-glu was combined with val68 to met.)
G6PD A- is the most common polymorphic variant associated with deficiency of G6PD in African populations, accounting for 20 to 40% of the affected population in western and central Africa; the most common nondeficient polymorphic variant in Africa is G6PD A. The G6PD A- mutation at position 68 alone has not been detected in any variant; this, together with further haplotyping analyses, led Vulliamy et al. (1992) to suggest that the nondeficient single mutant G6PD A is more ancient than the deficient double mutant G6PD A-.
Gomez-Gallego et al. (2000) performed structural studies on the doubly mutant G6PD A-. The changes they observed did not affect the active site of the mutant protein, since its spatial position was unmodified. The result of the structural changes was a loss of folding determinants, leading to a protein with decreased intracellular stability. Gomez-Gallego et al. (2000) suggested that the resultant protein was the cause of the enzyme deficiency in the red blood cell, which is unable to perform de novo protein synthesis.
Substitution of adenine for guanine at nucleotide 1003 leads to substitution of alanine by threonine at amino acid position 335 (Vulliamy et al., 1988). This mutation has been found in 2 unrelated Asian Indians and in a man from Syria and may be polymorphic. It causes class 2 enzyme derangement. No change in restriction sites has been found.
Mesbah-Namin et al. (2002) reported the first investigation of G6PD deficiency (300908) among the Mazandaranians of northern Iran. They analyzed the G6PD gene in 74 unrelated G6PD-deficient males with a history of favism. Molecular analysis revealed 3 different major polymorphic variants: G6PD Mediterranean (305900.0006) was found in 49 (66.2%), G6PD Chatham in 20 (27%), and G6PD Cosenza in 5 (6.75%) of the patients. The prevalence of G6PD Chatham in this Iranian population was the highest in the world. The distribution of the G6PD variants was more similar to that found in an Italian population than in other Middle Eastern countries.
See Usanga et al. (1977) and Luzzatto et al. (1979). Substitution of adenine for guanine at base 466 (in exon 5) leads to replacement of glutamic acid by lysine (Vulliamy et al., 1988). This sporadic class 3 mutation is associated with loss of a HinfI site.
See Panich et al. (1972). A G-to-A change at base 487 (exon 6) leads to substitution of serine for glycine at amino acid 163 (Vulliamy, 1989). This mutation is polymorphic in Southeast Asia, causes class 2 enzyme derangement, and is associated with a new AluI site (Vulliamy et al., 1989). The same mutation was identified by Tang et al. (1992) in a Taiwanese in Taiwan.
Matsuoka et al. (2004) found that 11% of blood samples from persons in remote areas of Myanmar (former Burma) indicated G6PD deficiency. Taken together with data from a previous report (Iwai et al., 2001), these findings indicated that 91.3% of G6PD variants were G6PD Mahidol. The findings suggested that the Myanmar population is derived from homogeneous ancestries different from those of Thai, Malaysian, and Indonesian populations.
Louicharoen et al. (2009) investigated the effect of the G6PD-Mahidol 487A variant on human survival related to P. vivax and P. falciparum malaria in Southeast Asia. They showed that strong and recent positive selection has targeted the Mahidol variant over the past 1,500 years. The authors found that the G6PD-Mahidol variant reduces vivax, but not falciparum, parasite density in humans, which indicates that P. vivax has been a driving force behind the strong selective advantage conferred by this mutation.
See Kirkman et al. (1964), Ben-Bassat and Ben-Ishay (1969), Lenzerini et al. (1969), Testa et al. (1980), and Morelli et al. (1984). A change from cytosine to thymine at base position 563 (in exon 6) causes a change from serine to phenylalanine in amino acid position 188 (Vulliamy et al., 1988). De Vita et al. (1989) found that G6PD Mediterranean, G6PD Sassari, and G6PD Cagliari have the same mutational change, resulting from a TCC-to-TTC mutation in exon 6. There is a second silent mutation of TAC-to-TAT at codon 437 in exon 11 (C-to-T at nucleotide 1311; see 305900.0018); both codons code for tyrosine. This mutation is a polymorphism, causes class 2 abnormality, and creates a new MboII site.
Beutler and Kuhl (1990) studied the distribution of the nucleotide polymorphism C1311T in diverse populations. Only 1 of 22 male subjects from Mediterranean countries who had the G6PD Mediterranean-563T genotype had a C at nucleotide 1311, which is the more frequent finding in this group. In contrast, both G6PD Mediterranean-563T males from the Indian subcontinent had the usual C at nucleotide 1311. Beutler and Kuhl (1990) interpreted these findings as suggesting that the same mutation at nucleotide 563 arose independently in Europe and in Asia.
Similar studies were done by Kurdi-Haidar et al. (1990) in 21 unrelated individuals with G6PD Mediterranean from Saudi Arabia, Iraq, Iran, Jordan, Lebanon, and Israel. All but 1 had the 563 mutation, and, of these, all but 1 had the C-to-T change at nucleotide 1311. Among another 24 unrelated Middle Eastern persons with normal G6PD activity, 4 had the silent mutation at position 1311 in the absence of the deficiency mutation at position 563. Kurdi-Haidar et al. (1990) concluded that most Middle Eastern subjects with the G6PD Mediterranean phenotype have the same mutation as that found in Italy; that the silent mutation is an independent polymorphism in the Middle East, with a frequency of about 0.13; and that the mutation leading to G6PD Mediterranean deficiency probably arose on a chromosome that already carried the silent mutation.
In Nepal, Matsuoka et al. (2003) tested 300 males for G6PD deficiency and identified 2 (0.67%) who were G6PD deficient. Compared with normal controls, G6PD activity was 12% and 26%, respectively. Both subjects had the 563C-T substitution of G6PD Mediterranean (ser188 to phe), and both had the silent 1311C-T change. A similar second change has been described in persons living in Mediterranean countries and Middle East countries. However, the form of G6PD Mediterranean found in India and Pakistan has no replacement at nucleotide 1311. Thus, the 2 subjects in Kathmandu, Nepal, would be closer to people in Middle East countries than people in India.
Corcoran et al. (1992) described a G6PD mutant biochemically indistinguishable from the common variety due to a C-to-T mutation at nucleotide 563. Instead, a C-to-T transition was found at nucleotide 592 in exon 6, changing an arginine residue to a cysteine residue only 10 amino acids downstream from the Mediterranean mutation. The new variant was named G6PD Coimbra (305900.0031).
Kaplan et al. (1997) presented data suggesting that the coexistence of Mediterranean type G6PD deficiency with the TA insertion polymorphism of the promoter of the UGT1A1 gene (191740.0011), which is associated with Gilbert syndrome (143500) in adults, is responsible for the development of neonatal hyperbilirubinemia. This is the most devastating clinical consequence of G6PD deficiency; it can be severe and result in kernicterus or even death. Kaplan et al. (1997) found that neither G6PD deficiency nor the polymorphism of UDP glucuronosyltransferase alone increased the incidence of neonatal hyperbilirubinemia, but in combination they did. The authors suggested that this gene interaction may serve as a paradigm of the interaction of benign genetic polymorphisms in the causation of disease.
Kaplan et al. (2001) reported 2 premature female neonates heterozygous for the G6PD Mediterranean mutation who presented with severe hyperbilirubinemia requiring exchange transfusions. Both had had normal G6PD biochemical screening tests.
Substitution of adenine for guanine at base 172 (exon IV) leads to a substitution of asparagine for aspartic acid at amino acid 58 (Vulliamy et al., 1988). The mutation was found in a sporadic, class 3 case, and no restriction site change was identified. See Calabro et al. (1990).
G6PD Portici has a G-to-A change at nucleotide 1178 of the G6PD gene, resulting in substitution of histidine for arginine at residue 393 (Filosa, 1989). The mutation was found in a sporadic case of class 1 deficiency (300908) and is not associated with an identified restriction site. In the full report, Filosa et al. (1992) described the kinetic characteristics of this G6PD variant (Portici) which was associated with chronic nonspherocytic hemolytic anemia.
Substitution of adenine for guanine as base number 1339 (exon 11) leads to substitution of arginine for glycine at amino acid position 447 (Vulliamy et al., 1988). This variant is associated with severe chronic hemolytic anemia (class 1; 300908). It was found in a sporadic case. A new PstI site was created, and this was used to show that it was a new mutation.
See Lenzerini et al. (1969) and Rattazzi et al. (1969). De Vita et al. (1989) found that G6PD Seattle-like, which produces a relatively mild phenotype, has substitution of histidine for aspartic acid at amino acid 282, resulting from a GAT-to-CAT change in exon 8. Cappellini et al. (1994) found the same variant in an Italian man from the Po delta and designated it G6PD Modena before finding that it had the same mutation as that in G6PD Seattle-like. They stated that the G-to-C transition was at nucleotide 844 in exon 8.
Town et al. (1990) described G6PD Harilaou in a Greek boy with severe hemolytic anemia. Poggi (1989) found a T-to-G change at nucleotide 648 that leads to substitution of leucine for phenylalanine at residue 216.
See Beutler et al. (1986). Hirono et al. (1989) demonstrated an A-to-G substitution at nucleotide 1156, resulting in substitution of glutamic acid for lysine at amino acid 386. This variant G6PD, as well as G6PD Beverly Hills, Tomah, Riverside, and some others, is unstable in the presence of 10 microM NADP+ (where normal G6PD is stable) but is reactivated by 200 microM NADP+. G6PD Tomah, Iowa and Beverly Hills have amino acid substitutions at positions 385, 386, and 387, respectively; G6PD Riverside, with a substitution at position 410, shows weak reactivation by NADP+. These observations, together with the fact that these amino acids are highly conserved, led Hirono et al. (1989) to propose that they are in the region of the molecule involved in NADP+ binding.
Hirono et al. (1989) demonstrated a G-to-A mutation at nucleotide 1160, causing substitution of histidine for arginine-387. The mutation destroyed an HhaI site.
Hirono et al. (1989) demonstrated a T-to-C transition at nucleotide 1153, causing substitution of arginine for cysteine-385. The mutation created an Fnu4HI restriction site, which was used to confirm the mutation.
Hirono et al. (1989) demonstrated a G-to-T mutation at nucleotide 1228 that caused a change of glycine to cysteine at amino acid 410. The fact that the mutation destroyed an NciI restriction site was used to confirm the mutation.
Viglietto et al. (1990) found a new variant with nearly normal properties, due to a G-to-A transition that caused an arginine-to-histidine substitution at position 285. See Calabro et al. (1990).
D'Urso et al. (1988) found a silent G-to-A change at nucleotide 1116 (in exon 10), generating a PstI site.
De Vita et al. (1989) found a silent C-to-T change at nucleotide 1311 (in exon 11).
Yoshida et al. (1988) found a RFLP resulting from a substitution in intron 5, creating a PvuII site. The probable change was C to G at a position 60 nucleotides upstream from exon 6 (Luzzatto, 1990).
Vives-Corrons et al. (1990) studied a G6PD variant resembling G6PD Mediterranean kinetically but with a slightly rapid electrophoretic mobility. They demonstrated a G-to-A transition at nucleotide 1361, producing an arg-to-his substitution.
G6PD Canton is one of the most common deficient variants in Orientals, reaching a gene frequency of 1.7% in southern China (McCurdy et al., 1966). Stevens et al. (1990) demonstrated that codon 459 in G6PD-B is changed from CGT(arginine) to CTT(leucine). The G-to-T change occurs at nucleotide 1376. Tang et al. (1992) found this mutation in 3 Taiwanese and 1 Hakkanese in Taiwan. They pointed out that the same mutation occurs in 3 other Chinese G6PD variants in Guangdong, China: Taiwan-Hakka (McCurdy et al., 1970), Gifu (Fujii et al., 1984), and Agrigento (Sansone et al., 1975). The G6PD Gifu variant was discovered in a 9-year-old Japanese male with chronic hemolysis and hemolytic crises after upper respiratory infections (Fujii et al., 1984). Enzyme activity was 2.9% of normal. The patient's G6PD showed increased utilization of substrate analog, deamino-NADP, and thermal instability.
Beutler et al. (1991) found a G-to-A transition at nucleotide 1192 causing a substitution of the amino acid lysine for the normal glutamic acid at position 398. This aberrant G6PD associated with nonspherocytic hemolytic anemia (300908) was described by Elizondo et al. (1982).
Beutler et al. (1991) found an A-to-T mutation at nucleotide 542 resulting in an asp-to-val substitution at amino acid 181. The subjects were white with 'some evidence of hemolysis' in one but none in the other. This aberrant G6PD, described by Saenz et al. (1984) in 2 unrelated subjects from Costa Rica, is 1 of 4 polymorphic variants that have 2 point mutations. One of these point mutations in each case is 376A-G (asn126asp), the change characteristic of the nondeficient polymorphic variant G6PD A+ (305900.0001).
Beutler et al. (1991) found that although the patients from whom this variant G6PD was derived were unrelated, all had a G-to-T mutation at nucleotide 637 in exon 6 leading to substitution of leucine for valine-213. The G6PD variants called Gastonia, Marion, and Minnesota were all from patients with nonspherocytic hemolytic anemia (300908).
In 2 unrelated patients with nonspherocytic hemolytic anemia (300908), Beutler et al. (1991) found a G-to-A mutation at nucleotide 1178 in exon 10 producing substitution of histidine for arginine-393.
See Poon et al. (1988). Beutler (1991) reported a G-to-A mutation at nucleotide 871, resulting in substitution of methionine for valine-291. The variant belonged to WHO class 2.
Louicharoen and Nuchprayoon (2005) and Matsuoka et al. (2005) indicated that G6PD Viangchan is the most common mutation in the Cambodian population, similar to Thai and Laotian populations, suggesting a common ancestry for people from these 3 countries. Matsuoka et al. (2005) found that G6PD Viangchan was linked in 8 cases with a 1311C-T transition (305900.0018) in exon 11 and a T-to-C substitution in intron 11, 93 bp downstream of exon 11. The finding was in accordance with studies of G6PD Viangchan in Laos, Thailand, and Malaysia.
In subjects with the G6PD A- phenotype, Hirono and Beutler (1988) found substitution of leucine for arginine-227, resulting from a G-to-T mutation at nucleotide 680 (rather than the val68-to-met mutation as in the usual G6PD A-). The mutation existed on the G6PD A background (asn126 to asp).
In subjects with the G6PD A- phenotype, Hirono and Beutler (1988) found substitution of proline for leucine-323, resulting from a T-to-C mutation at nucleotide 968 (rather than the val68-to-met mutation as in the usual G6PD A-). The mutation existed on the G6PD A background (asn126-to-asp).
Zuo et al. (1990) demonstrated substitution of histidine for arginine-463 resulting from a G-to-A mutation in nucleotide 1388. The G6PD was of the WHO class 2. The Chinese variant G6PD Kaiping was discovered by Du et al. (1988). The same mutation was found in G6PD Anant (Panich and Sungnate, 1973), Dhon (Panich and Na-Nakorn, 1980), Petrich-like (Shatskaya et al., 1980), and Sapporo-like (Fujii et al., 1981).
In a patient with nonspherocytic hemolytic anemia (300908), Beutler et al. (1991) identified a C-to-A mutation at nucleotide 1089 in exon 10, producing substitution of asparagine-363 by lysine.
In the son of a Portuguese woman who had suffered an attack of favism, Corcoran et al. (1992) identified a G6PD mutant with the chemical properties of the Mediterranean type (305900.0006). However, at the DNA level, they demonstrated that the mutation was a C-to-T transition 29 nucleotides downstream from the Mediterranean mutation, resulting in substitution of cysteine for arginine 10 amino acids downstream from the Mediterranean change. The same mutation was found in a patient in southern Italy. The new variant was called G6PD Coimbra.
In 3 individuals with G6PD deficiency from tribal groups in southern India, Chalvam et al. (2008) identified the Coimbra variant and stated that the mutation had a frequency of 7.5% in this population.
Gray et al. (1973) described a unique G6PD variant in a patient with chronic granuloma and hemolytic anemia. G6PD activity was undetectable not only in the patient's red blood cells but also in leukocytes and fibroblasts, and an immunologically crossreacting material was undetectable in these tissues. This is the only variant observed with no measurable activity and lack of crossreacting material, satisfying the definition for a 'null' variant. Maeda et al. (1992) found that the mRNA content and the size of mRNA were normal in the patient's lymphoblastoid cells (maintained as GM7254 in the Coriell repository in Camden, New Jersey). Western blot hybridization indicated that the patient's cells did not produce crossreacting material. Three nucleotide base changes were found in variant cDNA: a C-to-G transversion at nucleotide 317 (counting from adenine of the initiation codon), which should cause a ser-to-cys substitution at the 106th position (counting from the initiation met); a C-to-T transition at nucleotide 544, producing an arg-to-trp substitution at the 182nd position; and a C-to-T transition at nucleotide 592, resulting in an arg-to-cys substitution at the 198th position of the protein. No deletions or frameshift mutations were found, and no nucleotide change was detected in the extended 5-prime region which included the most distal cap site. When the variant cDNA was expressed in E. coli, the G6PD activity was about 2% of normal and crossreacting material was undetectable. However, when the variant mRNA was expressed in the in vitro translation system of rabbit reticulocytes, the variant protein was produced. The results suggested that extremely rapid in vivo degradation or precipitation of the variant enzyme induced by the 3 amino acid substitutions could be the major cause of the molecular deficiency.
Tang et al. (1992) identified an A-to-G transition at nucleotide 493 resulting in an asn165-to-asp amino acid substitution in the G6PD protein. The biochemical features of the mutation were not characterized. This mutation has only been reported in Chinese.
The Chinese population of Taiwan is divided into 4 groups: Taiwanese, mainland Chinese, Hakkanese, and Aborigines. The Taiwanese, the largest group, are descendants from emigrants who left mainland China during the 17th to 19th centuries. Most were from Fuchien Province on the southeast coast of China. The second largest population is mainland Chinese, who resided originally in many provinces throughout mainland China and migrated to Taiwan during the period 1948 to 1950. The third population is Hakkanese (Taiwan-Hakka), originally from Chung Yuan, who immigrated from the Kwangtung and Fuchien provinces on the southern coast of China and who came to Taiwan primarily during the 16th and 17th centuries. The native Taiwan Aborigines are a much smaller group, containing at least 9 distinct tribes whose ancestors are believed to have arrived in Taiwan from mainland Asia several thousand years ago. The frequency of G6PD deficiency varies from 4.52% in the Hakkanese to an average of 0.3% in most of the Aborigines. The Ami tribe of Aborigines shows a frequency of 3.5%, presumably a reflection of founder effect.
In a Chilean patient with nonspherocytic hemolytic anemia (300908), Beutler et al. (1992) identified a G-to-C transversion at nucleotide 593 leading to an arg198-to-pro substitution. They suggested G6PD Santiago as the designation. (G6PD Santiago de Cuba is a different mutation; see 305900.0009.)
In a Mexican individual with no clinical features attributable to the G6PD variant, Beutler et al. (1992) described a G-to-A transition at nucleotide 680 leading to an arg227-to-gln substitution. They suggested the designation G6PD Mexico City. (There is a G6PD Mexico; see under 305900.9999.) Nucleotide 680 is the same base that is altered from G-to-T in one type of G6PD A- (arg227-to-leu).
In a Greek person with no clinical abnormalities that could be related to the G6PD variant, Beutler et al. (1992) identified a C-to-T transition at nucleotide 1057 resulting in a pro353-to-ser substitution.
See Vaca et al. (1982). In a Mexican patient with nonspherocytic hemolytic anemia (300908), Beutler et al. (1992) identified an arg387-to-cys substitution resulting from a C-to-T transition at nucleotide 1159.
See Beutler and Rosen (1970). Beutler et al. (1992) indicated that the mutation in this G6PD variant found in a US white patient with nonspherocytic hemolytic anemia (300908) involved a G-to-C transversion at nucleotide 1180 resulting in a val394-to-leu substitution.
In a Japanese patient with nonspherocytic hemolytic anemia (300908), Beutler et al. (1992) identified a G-to-A transition at nucleotide 1229 resulting in a gly410-to-asp substitution.
In a US white patient with nonspherocytic hemolytic anemia (300908), Beutler et al. (1992) identified a G-to-C transition at nucleotide 1316 leading to an arg439-to-pro substitution.
Using a PCR-based technique, MacDonald et al. (1991) determined the nucleotide sequence of the entire coding region of the G6PD gene from a person with severe red cell G6PD deficiency and chronic hemolytic anemia (300908). The only abnormality found was a 3-bp deletion in exon 2, which predicted the loss of 1 of 2 adjacent isoleucine residues (amino acid 35 or 36), just upstream of the methionine residue called 'junctional' by Kanno et al. (1989). This part of exon 2 lies in a region that was thought by Kanno et al. (1989) to be encoded by a gene on chromosome 6, an idea subsequently disproved. The observations of MacDonald et al. (1991) demonstrated that a mutation in this X-linked amino-terminal region of G6PD caused deficiency in red cells. The deletion was within a 3-fold CAT repeat and had presumably resulted from misalignment at meiosis, with conservation of the reading frame.
G6PD Kerala (Azevedo et al., 1968) and G6PD Kalyan (Ishwad and Naik, 1984), 2 variants discovered in India, were thought to be distinct on the basis of their biochemical properties. Ahluwalia et al. (1992) demonstrated that the molecular defect is identical. Both have a glu317-to-lys mutation which causes a loss of 2 negative charges; this is in keeping with the very slow electrophoretic mobility of G6PD Kerala-Kalyan. Both are accompanied by only mild enzyme deficiency. In both, the mutation is a C-to-T transition in the CpG dinucleotide. The mutations were found in 2 populations that are entirely distinct linguistically and culturally with no known historical links. However, in light of the traditional occupation of the Koli tribal group inhabiting the Kalyan district of Bombay, namely, marine fishing, victims of bad weather may have found their way to distant places where they were forced to live for some period, thus creating the possibility of gene flow.
In an Algerian boy who presented to the hospital with acute hemolytic anemia associated with 7 to 10% of G6PD residual activity, Nafa et al. (1993) identified a T-to-C transition at nucleotide 143 converting codon 48 from ATC (ile) to ACC (thr). The mutation was associated with favism.
In Saudi Arabia, Niazi et al. (1996) described G6PD Aures in 7 of 20 children (35%) with severe G6PD deficiency and in a 16-year-old boy with a history of passing dark urine after eating fava beans at the age of 5 years. Of the 20 children, 12 were positive for G6PD Mediterranean (305900.0006), and the mutation in 1 child remained unidentified.
This G6PD variant was described by Du et al. (1985). Its biochemical characterization was reviewed by Chiu et al. (1993), who demonstrated that the mutant is frequent in Chinese and consists of a change in cDNA nucleotide 95 from A to G (his to arg).
In an analysis of the molecular defect in 43 G6PD-deficient Chinese, Chiu et al. (1993) found 3 with a G-to-T transversion in cDNA nucleotide 392 (exon 5) resulting in a gly-to-val substitution. They reviewed the biochemical characteristics of this previously unidentified variant.
In a study of the molecular defect in 43 G6PD-deficient Chinese, Chiu et al. (1993) identified a 'new' variant due to a C-to-T transition at cDNA nucleotide 1024 resulting in a leu-to-phe substitution. Chiu et al. (1993) listed the biochemical characteristics of G6PD Mahidol-like.
To determine the extent of heterogeneity of G6PD in India, Kaeda et al. (1995) studied several different Indian populations by screening for G6PD deficiency, followed by molecular analysis of deficient alleles. The frequency of G6PD deficiency varied between 3% and 15% in different tribal and urban groups. Remarkably, a previously unreported deficient variant, G6PD Orissa (ala44-to-gly), was found to be responsible for most of the G6PD deficiency in tribal Indian populations but was not found in urban populations where most of the G6PD deficiency was due to the G6PD Mediterranean (ser188-to-phe) variant (305900.0006). The distribution of G6PD alleles in India is reminiscent of the situation found with beta-globin (141900), as reviewed by Nagel and Ranney (1990). In that case, sickle cell anemia is almost entirely restricted to the tribal groups, whereas urban populations have a predominance of beta-thalassemia mutations. Kaeda et al. (1995) noted that the Km(NADP) of G6PD Orissa was 5-fold higher than that of the normal enzyme. This was thought to be due to the fact that the alanine residue that is replaced by glycine is part of a putative coenzyme-binding site. Surprisingly, the enzyme appeared to the authors to be more stable than normal G6PD, whereas most deficient variants have lowered stability.
In a Chinese newborn with neonatal jaundice, Chen et al. (1996) identified a novel G6PD mutation, G6PD NanKang, caused by a T-to-C transition at nucleotide 517, producing a phe173leu substitution in the G6PD protein.
In a study of G6PD-deficient patients who presented with clinical favism in Spain, Vulliamy et al. (1996) found a new polymorphic variant they called G6PD Malaga, whose only abnormality was an A-to-T transversion at nucleotide 542 resulting in an asp181-to-val amino acid substitution. This was the same mutation previously found in association with the mutation of G6PD A-, namely asn126asp (305900.0001) in the double mutant G6PD Santamaria (305900.0023). G6PD Malaga was associated with enzyme deficiency class 3, and the enzymic properties of G6PD Malaga and G6PD Santamaria were quite similar. Vulliamy et al. (1996) speculated that G6PD Santamaria might have been produced by recombination between G6PDA and G6PD Malaga; however, haplotype analysis, including the use of a new silent polymorphism, suggested that the same 542A-T mutation had taken place independently in a G6PD B gene to give G6PD Malaga and in a G6PD A gene to give G6PD Santamaria.
In a study of 31 unrelated G6PD-deficient males in the Campania region of Southern Italy, Alfinito et al. (1997) found 9 different G6PD variants, 8 of which had already been described. The new variant, G6PD Neapolis, was found to have a pro467-to-arg substitution in the G6PD protein.
In a study of the causative mutation in 12 cases of G6PD deficiency associated with chronic nonspherocytic hemolytic anemia (300908), Vulliamy et al. (1998) found 1 patient to have a novel mutation, which they called G6PD Serres: a 1082C-T change, causing an ala361-to-val substitution in the dimer interface where most other severe G6PD mutations are found.
In a Japanese boy with severe G6PD deficiency (300908), Hirono et al. (1993) identified a 24-bp deletion (nucleotides 953-976) in exon 9 of the G6PD gene, which predicted an 8-amino acid deletion at residue 319.
In a boy born in Aveiro, Portugal with severe chronic hemolytic anemia (300908) present from birth, Costa et al. (2000) found that the undetectable G6PD activity was caused by a G-to-A transition at nucleotide position 806 of the G6PD gene resulting in a cys269-to-tyr (C269Y) amino acid substitution. This mutation, which was designated G6PD Aveiro, was not detected in his mother or sister. By the age of 5 years, the patient had had 6 episodes of severe acute intravascular hemolysis that required hospitalization and erythrocyte transfusion. The spleen was palpable 6 cm below the left costal margin. Costa et al. (2000) pointed out that G6PD mutants causing class 1 variants (the most severe forms of the disease) cluster within exon 10, in a region that, at the protein level, is believed to be involved in dimerization. The mutation in this new class 1 variant maps to exon 8. Mutant and normal alleles were found in both hematopoietic and buccal cells, indicating mosaicism.
G6PD A- is a common G6PD variant among Africans that may cause acute hemolysis triggered by infections and certain drugs, as well as by fava beans. This class 3 phenotype can be caused by a combination of the common 376A-G (asn126 to asp) mutation and either of 3 additional mutations that include 202G-A (val68 to met); see 305900.0002. The missense mutation 376A-G (asn126 to asp) by itself causes an asymptomatic class 4 variant G6PD A with normal enzyme activity, whereas the other mutation, 202G-A, had not been found in humans by itself. Hirono et al. (2002) described an asymptomatic G6PD-deficient patient with the missense mutation 202G-A but not the 376A-G. This was a 3-year-old Japanese boy who was noted to have jaundice and anemia on admission to the Asahi General Hospital. This was the only mutation found and it must have arisen separately from those common in Africans, because the patient had none of the silent mutations closely linked to the African mutation, while he had an intronic single base deletion common in Mongoloids. Town et al. (1992) had found in an in vitro study using recombinant human G6PD mutants expressed in E. coli that 202G-A, as well as 376A-G, does not cause enzyme deficiency by itself, and the synergistic action of these 2 mutations is necessary to produce the class 3 phenotype of G6PD A-. Synergistic interaction was also supported by the fact that val68 and asn126 are closely located in a 3-dimensional model of human G6PD. The results of Hirono et al. (2002) seem inconsistent with the idea that 202G-A cannot produce acute hemolysis by itself.
In 3 brothers and their carrier mother of Jewish Ethiopian descent, Iancovici-Kidon et al. (2000) found a T-to-C transition at nucleotide 964 in exon 9 of the G6PD gene, resulting in a tyr322-to-his (Y322H) mutation. All 3 sibs showed hereditary nonspherocytic hemolytic anemia (300908), but the severity of hemolysis and the transfusion requirement varied markedly. One brother had severe congenital neutropenia (SCN; 202700), a condition not previously described in association with G6PD deficiency. Levels of white blood cell G6PD activity of the 3 sibs was 0 to 5% of normal controls. Neutrophil oxidative and bactericidal activities were impaired in the brother with SCN, but were well preserved in the other 2 sibs.
In a study of blood cells of 4 male patients from 2 unrelated families with nonspherocytic anemia (300908) and recurrent bacterial infections, van Bruggen et al. (2002) discovered that the activity of G6PD in red blood cells and in granulocytes was below detection level. Moreover, their granulocytes displayed a decreased respiratory burst upon activation. Sequencing of genomic DNA revealed a novel 3-bp (TCT) deletion in the G6PD gene, predicting the deletion of a leucine at position 61. The mutant G6PD protein was undetectable by Western blotting in red blood cells and granulocytes of these patients. In phytohemagglutinin-stimulated lymphocytes, the G6PD protein was present, but the amount of the protein was greatly diminished in the patients' cells. Purified mutant protein from an E. coli expression system showed decreased heat stability and decreased specific activity. Furthermore, van Bruggen et al. (2002) demonstrated that mRNA of the mutant G6PD was unstable, which may contribute to the severe G6PD deficiency observed in these patients. They proposed the name 'G6PD Amsterdam' for the new variant.
One family reported by van Bruggen et al. (2002) was Caucasian, the second was Hindustani. The Caucasian patient had an unremarkable medical history until he was admitted to the hospital at age 15 years with recurrent episodes of fever, jaundice, gastroenteritis, and coughing. He was found to have invasive disseminated aspergillosis (see 614079) in the lungs, brain, and soft tissues of the leg. Aspergillosis was successfully treated. Thereafter, hemoglobin level was normal but reticulocytosis was persistent. One of his brothers also had G6PD deficiency and presented with prolonged neonatal jaundice and episodes of acute hemolysis but had no known disposition to infections.
The Hindustani proband reported by van Bruggen et al. (2002) was healthy until the age of 3.5 years, when he was admitted to the hospital with pneumonia caused by Chromobacterium violaceum, an uncommon human pathogen that can cause serious infections in patients with neutrophil dysfunction. He was anemic. He responded well to chemotherapy, although the anemia persisted. With relapse he developed osteomyelitis but again responded to therapy.
In a 33-year-old Swiss male with G6PD deficiency, designated G6PD Zurich, Efferth et al. (2004) identified a single nucleotide mutation that altered position -2 of intron 10 of the G6PD gene from the consensus A to G. The mutation resulted in alternative splicing that removed the first 9 nucleotides of exon 11, which code for amino acids asparagine, valine, and lysine at positions 430-432, respectively. Efferth et al. (2004) estimated that 400 million people worldwide are affected by G6PD deficiency, the most common hereditary enzymopathy, with some 140 known molecular G6PD defects. They pointed out that most mutations in the G6PD gene are missense mutations. To the best of their knowledge, there was only 1 missplicing mutation previously described: G6PD Varnsdorf (305900.0058), which is caused by destruction of the same obligate splice site as that destroyed in G6PD Zurich. In G6PD Varnsdorf, the invariant 3-prime AG dinucleotide has been deleted, whereas in G6PD Zurich, a point mutation has changed AG to GG. In both G6PD Zurich and G6PD Varnsdorf, the next available downstream consensus splice sequence is used, resulting in deletion of 3 amino acids. Efferth et al. (2004) suggested that it was no coincidence that the only 2 splicing mutations of G6PD identified to that time both affected the same splice site. Since null mutations of G6PD appear to be incompatible with life, a functional alternative splice site that does not cause a frameshift is required for viability. The 3-prime splice site of intron 10 offers this opportunity.
See 305900.0057 and Efferth et al. (2004).
Calabro et al. (1993) identified a novel G6PD variant, which they called Cosenza, in patients with G6PD deficiency from the Calabria region of southern Italy. The arg459-to-pro (A459P) substitution results from a 1376G-C transversion. The mutant protein retains less than 10% enzyme activity and belongs to the group of severe disorders often associated with hemolysis.
Barisic et al. (2005) identified G6PD Cosenza in 9 (37.5%) of 24 unrelated patients with G6PD deficiency from the Dalmatian region of southern Croatia. Seven of the 9 patients had favism.
In a male with G6PD deficiency from the Dalmatian region of southern Croatia, Barisic et al. (2005) identified a 1442C-G transversion in the G6PD gene, resulting in a pro481-to-arg (P481R) substitution. The mutant protein retained approximately 30% enzyme activity (class 3).
Chalvam et al. (2007) identified a 208T-C transition in exon 4 of the G6PD gene, resulting in a his70-to-tyr (H70Y) substitution, as the basis of G6PD deficiency in Indian patients with the disorder. The H70Y mutation was detected in 28 (70.4%) of 40 affected Indian males from 3 tribal groups from the Nilgiri district of Tamil Nadu in southern India. The variant was termed G6PD Namoru.
In 4 individuals with G6PD deficiency from tribal groups of the Nilgiri district in southern India, Chalvam et al. (2008) identified a 593G-A transition in exon 6 of the G6PD gene, resulting in an arg198-to-his (R198H) substitution, which they designated G6PD Nilgiri. The authors stated that the mutation had a frequency of 10.0% in this population.
The following list of G6PD variants which have not been characterized at the molecular level is in alphabetic order. Quotation marks surround the name of each G6PD variant about which there is insufficient information for certainty of its uniqueness.
G6PD AACHEN. See Kahn et al. (1976).
G6PD AARAU. See Gahr et al. (1976).
G6PD 'ABEOKUTA'. See Usanga et al. (1977).
G6PD ABRAMI. See Kahn et al. (1975).
G6PD 'ADAME'. See Usanga et al. (1977).
G6PD ADANA. See Aksoy et al. (1987).
G6PD AKITA. See Miwa et al. (1978).
G6PD ALABAMA. Prchal et al. (1988) described a 6-year-old black boy who had transient hemolysis after a viral infection and was found to have mildly decreased red cell G6PD activity. The unusual finding was the presence of 2 G6PD bands in him and in his maternal grandfather despite normal XY karyotype. Two bands were seen only in reticulocytes. Prchal et al. (1988) postulated that there were 2 transcriptional products of the mutant G6PD gene, 1 of which had a short half-life and was detectable only in young red blood cells.
G6PD ALBUQUERQUE. See Beutler et al. (1968).
G6PD ALESSANDRIA. Similar to G6PD Alexandra. See Sansone et al. (1981).
G6PD ALEXANDRA. This was found in Australia in a male of Italian extraction who suffered severe neonatal jaundice following maternal ingestion of fava beans prenatally and postnatally. Retesting in adolescence showed milder expression of the enzyme defect (Harley et al., 1978).
G6PD ALGER. See Benabadji et al. (1978).
G6PD AMBOIN. See Chockkalingam et al. (1982).
G6PD AMMAN-1. See Karadsheh et al. (1986).
G6PD AMMAN-2. See Karadsheh et al. (1986).
G6PD ANGORAM. See Chockkalingam et al. (1982).
G6PD ANKARA. See Kahn et al. (1975).
G6PD ARLINGTON HEIGHTS. See Honig et al. (1979).
G6PD ASAHIKAWA. This variant was discovered in a 6-year-old Japanese boy with chronic hemolytic anemia and hemolytic crises after upper respiratory infections (Takizawa et al., 1984).
G6PD ASHDOD. See Ramot et al. (1969).
G6PD ATHENS. See Stamatoyannopoulos et al. (1967).
G6PD 'ATHENS-LIKE'. See Stamatoyannopoulos et al. (1971).
G6PD ATLANTA. See Beutler et al. (1976).
G6PD 'ATTICA'. See Rattazzi et al. (1969).
G6PD AVENCHES. See Pekrun et al. (1989).
G6PD 'AVVOCATA'. See Colonna-Romano et al. (1985).
G6PD AYUTTHAYA. See Panich (1980).
G6PD AZERBAIJAN. See Shatskaya et al. (1975).
G6PD B. The so-called normal, this form predominates in all populations greater than a few hundred (Yoshida et al., 1971).
G6PD 'BAGDAD'. See Geerdink et al. (1973).
G6PD BAKU. See Shatskaya et al. (1980).
G6PD 'BALCALI'. See Aksoy et al. (1987).
G6PD BALI. See Chockkalingam et al. (1982).
G6PD BALTIMORE-AUSTIN. See Porter et al. (1964) and Long et al. (1965).
G6PD BANGKOK. See Talalak and Beutler (1969).
G6PD BARBIERI. See Marks et al. (1962).
G6PD BARCELONA. See Vives-Corrons et al. (1982). This is one of the rare G6PD variants associated with granulocyte dysfunction and increased susceptibility to infections. Hemolysis in this form of chronic nonspherocytic hemolytic anemia is exaggerated by infection.
G6PD 'BASH-KUNGUT I AND II'. See Shatskaya et al. (1980).
G6PD 'BASH-KUNGUT IV'. See Shatskaya et al. (1980).
G6PD BAT-YAM. See Ramot et al. (1969).
G6PD BAUDELOCQUE. See Junien et al. (1974).
G6PD 'BEAUJON'. See Boivin and Galand (1968).
G6PD BEAUMONT. Mamlok et al. (1985) reported a new molecular variant associated with severe enzyme deficiency and chronic nonspherocytic hemolytic anemia. The characteristics were marked heat lability, a normal rate constant value for glucose-6-phosphate, a nearly normal pH activity curve, and increased use of 2-deoxyglucose-6-phosphate. Mamlok et al. (1987) described a fatal case of Chromobacterium violaceum sepsis in a 3-year-old boy with this variant. The child was an identical twin; the surviving twin subsequently had a severe episode of Campylobacter jejuni gastroenteritis. Patients with severe deficiency of G6PD and polymorphonuclear leukocytes have increased susceptibility to infections and abnormal phagocyte function that resembles that of patients with chronic granulomatous disease, but such had not hitherto been reported during the first decade of life. Infections with C. violaceum are rare; most of the 20 or so infections have occurred in Louisiana or Florida and have been associated with warm, stagnant water sources.
G6PD BENEVENTO. See McCurdy et al. (1973).
G6PD BERLIN. See Helge and Borner (1966).
G6PD BIDEIZ. See Krasnopolskaya et al. (1977).
G6PD BIELEFELD. See Gahr et al. (1977).
G6PD BIRMINGHAM. See Prchal et al. (1980).
G6PD BLIDA. See Benabadji et al. (1978).
G6PD BNEI BRAK. See Sidi et al. (1980).
G6PD BODENSEE. See Benohr et al. (1971).
G6PD BOGIA. See Chockkalingam and Board (1980).
G6PD BOLUO. See Du et al. (1988).
G6PD BOLUO-2. See Du et al. (1988).
G6PD BOSTON. See Necheles et al. (1971).
G6PD BUKITU. See Chockkalingam and Board (1980).
G6PD BUTANTAN. In Brazil, Stocco dos Santos et al. (1991) described a Gd(+) variant which was characterized by normal activity and electrophoretic mobility, increased Km, and increased activity for 2-deoxy-G6P. The variant, which they called G6PD Butantan, was present in 3, and perhaps a fourth, cousin; the 4 mothers were sisters. All 4 males had severe mental retardation, bilateral congenital hip luxation, and short stature. Five uncles of these males may have been affected. In this family, Stocco dos Santos et al. (2003) found linkage of the X-linked mental retardation syndrome (300434) to the pericentric region, Xp11.3-q21.1.
G6PD 'CAGLIARI II' (CAGLIARI-LIKE). See Frigerio et al. (1987) and Calabro et al. (1990).
G6PD 'CALTANISSETTA'. See Sansone et al. (1981) and Perroni et al. (1982).
G6PD 'CAMALDOLI'. See Colonna-Romano et al. (1985).
G6PD CAMPBELLPORE. See McCurdy et al. (1970).
G6PD CAMPERDOWN. Harley et al. (1978) found this variant in Australia in a boy of Maltese extraction in whom lamellar cataracts were found at age 4. The enzyme deficiency was detected in a screening of children of Mediterranean extraction with lamellar cataracts. The boy had no excessive hemolysis. Previous descriptions of cataracts were in patients with hemolytic anemia.
G6PD CAPETOWN. See Botha et al. (1969).
G6PD CARSWELL. See Siegel and Beutler (1971).
G6PD CASTILLA-LIKE. See Chockkalingam et al. (1982).
G6PD CAUJERI. See Gutierrez et al. (1987).
G6PD CENTRAL CITY. See Csepreghy et al. (1988).
G6PD CHAINAT. See Panich and Na-Nakorn (1980).
G6PD CHAO PHYA. See Panich (1980).
G6PD CHARLESTON. See Beutler et al. (1972).
G6PD CHIAPAS. See Lisker et al. (1978).
G6PD CHIBUTO. See Reys et al. (1970).
G6PD CHICAGO. See Kirkman et al. (1964) and Fairbanks et al. (1980). Fairbanks et al. (1980) demonstrated that G6PD Chicago and G6PD Cornell are the same variant; they had been described previously in different members of a single large kindred.
G6PD CHINESE. See Chan et al. (1972).
G6PD CIUDAD DE LA HABANA. See Gonzalez et al. (1980).
G6PD 'CLICHY'. See Boivin and Galand (1968).
G6PD CLINIC. In a young patient with chronic nonspherocytic hemolytic anemia and familial amyloidotic polyneuropathy, Vives-Corrons et al. (1989) identified a new variant with a markedly acidic pH optimum. It bore some similarity in its molecular characteristics to G6PD Bangkok and G6PD Duarte.
G6PD COLOMIERS. See Vergnes et al. (1981).
G6PD COLUMBUS. See Pinto et al. (1966).
G6PD CORINTH. Yoshida, A.: unpublished, 1975.
G6PD CORNELL. See Miller and Wollman (1974) and Fairbanks et al. (1980). Fairbanks et al. (1980) demonstrated that G6PD Chicago and G6PD Cornell are the same variant; they had been described previously in different members of a single large kindred.
G6PD CUIABA. In a 33-year-old male of Portuguese extraction who developed hemolytic anemia after acetaminophen and acetylsalicylic acid ingestion, Barretto and Nonoyama (1987) found a variant G6PD which had normal activity and normal electrophoretic mobility, but unusually high K(m) for glucose-6-phosphate, high K(i) for NADPH, and decreased thermal stability.
G6PD 'DAKAR'. See Kahn et al. (1971, 1973).
G6PD DALLAS. Beutler, E.; Frenkel, E. P.; Forman, L.: unpublished, 1987.
G6PD DEBROUSSE (G6PD CONSTANTINE, FORMERLY). See Kissin and Cotte (1970) and Sansone et al. (1975).
G6PD DJYNET. See Krasnopolskaya and Bochkov (1982).
G6PD DOTHAN. See Prchal et al. (1979).
G6PD DUARTE. See Beutler et al. (1968).
G6PD DUBLIN. See McCann et al. (1980).
G6PD DUSHANBA I. See Krasnopolskaya and Bochkov (1982).
G6PD DUSHANBA II. See Krasnopolskaya and Bochkov (1982).
G6PD DUSHANBA III. See Krasnopolskaya and Bochkov (1982).
G6PD EAST AFRICAN. See Othieno-Obel (1972).
G6PD EAST HARLEM. See Feldman et al. (1977).
G6PD 'EKITI'. See Usanga et al. (1977).
G6PD EL-FAYOUM. See McCurdy et al. (1974).
G6PD EL-KHARGA. See McCurdy et al. (1974).
G6PD EL MORRO. See McCurdy et al. (1973).
G6PD ENGLEWOOD. See Rattazzi et al. (1971).
G6PD 'ENSLEY'. See Nsouly and Prchal (1981).
G6PD 'ESPOO'. See Vuopio et al. (1975).
G6PD FERRANDINA. See Calabro et al. (1990).
G6PD FERRARA. See Carandina et al. (1976).
G6PD FERRARA II. See De Flora et al. (1981) and Sansone et al. (1981).
G6PD 'FERRARA III'. See Perroni et al. (1982).
G6PD FORT PIERCE. Phyliky, R. L.; Nishimura, R. A. and Beutler, E.: unpublished, 1983.
G6PD FORT WORTH. See Mills et al. (1975).
G6PD 'FRANKFURT'. Nowicki et al. (1974).
G6PD FREIBURG. See Weinreich et al. (1968) and Busch and Boie (1970).
G6PD FUKUOKA. This variant was found in a 77-year-old male with drug-induced hemolysis (Fujii et al., 1984). Enzyme activity was 6.4% of normal and the patient's G6PD had abnormal electrophoretic mobility and thermal instability.
G6PD FUKUSHIMA. Miwa et al. (1978) described this 'deficiency' mutant, which leads to chronic hemolytic anemia. It was slow-moving electrophoretically, like G6PD Kurume, from which it differed by low utilization of deamino-NADP and normal pH curve. The proband, a 33-year-old male, had 2.8% of normal enzyme activity and mild hemolytic anemia. Miwa et al. (1978) stated that 46 variants had previously been classified as class 1, with severe enzyme deficiency leading to chronic nonspherocytic hemolytic anemia.
G6PD GABROVIZZA. See Ventura et al. (1984).
G6PD 'GALLIERA'. See Perroni et al. (1982).
G6PD GALLURA. See Sansone et al. (1975).
G6PD 'GALVESTON'. See Alperin and Mills (1972).
G6PD 'GAMBIA'. Welch et al. (1978) found a gene frequency of 0.024 among 1,109 persons examined in The Gambia. This is a slow electrophoretic variant with reduced enzyme activity.
G6PD GAOMIN. See Du et al. (1988).
G6PD GAOZHOU. See Du et al. (1988).
G6PD GENOVA. See Gaetani et al. (1990).
G6PD GOODENOUGH. See Chockkalingam et al. (1982).
G6PD GOTZE DELCHEV. See Shatskaya et al. (1980). G6PD GRAND PRAIRIE. See Cederbaum and Beutler (1975).
G6PD GREAT LAKES. Beutler, E. and Maurer, H. S.: unpublished, 1984.
G6PD GUANGZHOU. See Du et al. (1988).
G6PD GUANTANAMO. See Gutierrez et al. (1987). G6PD 'GUIBA'. See Weimer et al. (1981).
G6PD HAAD YAI. See Panich and Na-Nakorn (1980).
G6PD 'HAMBURG'. See Gahr and Schroter (1974).
G6PD HAMM. See Gahr et al. (1976).
G6PD 'HANOI'. See Toncheva (1986).
G6PD HAWAII. Beutler, E. and Matsumoto, F.: unpublished, 1975.
G6PD HAYEM. See Kahn et al. (1974). G6PD HEIAN. See Nakai and Yoshida (1974).
G6PD HEKTOEN. Substitution of tyrosine for histidine (Dern et al., 1969).
G6PD HELSINKI. See Vuopio et al. (1973) and Harkonen and Vuopio (1974). Cohn et al. (1979) described severe hemolytic anemia in 2 Danish boys, who showed deficiency of G6PD. The enzyme had characteristics possibly identical to those of G6PD Helsinki.
G6PD HILLBROW. See Cayanis et al. (1975).
G6PD 'HIROSHIMA-1'. See Kageoka et al. (1985).
G6PD 'HIROSHIMA-2'. See Kageoka et al. (1985).
G6PD 'HIROSHIMA-3'. See Kageoka et al. (1985).
G6PD HOFU. See Miwa et al. (1977).
G6PD HONG KONG. See Wong et al. (1965) and Chan et al. (1972).
G6PD HONG KONG POKFULAM. See Chan et al. (1972).
G6PD HOTEL DIEU. See Kahn et al. (1977).
G6PD HUALIEN. McCurdy, P. R.: unpublished, 1975.
G6PD HUALIEN-CHI. McCurdy, P. R.: unpublished, 1975.
G6PD HUAZHOU. See Du et al. (1988).
G6PD HUIYANG. See Du et al. (1988).
G6PD HUNTSVILLE. See Hall et al. (1988).
G6PD HURON. See Ravindranath and Beutler (1987).
G6PD IBADAN-AUSTIN. See Long et al. (1965).
G6PD IJEBU-ODE. See Luzzatto and Afolayan (1968).
G6PD INDIANAPOLIS. Beutler, E.; Forman, L.; Gelbart, T.: unpublished, 1985.
G6PD INDONESIA. See Kirkman and Eng (1969).
G6PD INHAMBANE. See Reys et al. (1970).
G6PD INTANON. See Panich (1974).
G6PD ISERLOHN. Unstable enzyme. See Eber et al. (1985).
G6PD ITA-BALE. See Long et al. (1965).
G6PD IWATE. See Kanno et al. (1987).
G6PD JACKSON. See Thigpen et al. (1974).
G6PD JALISCO. See Vaca et al. (1985).
G6PD JOHANNESBURG. See Balinsky et al. (1973).
G6PD 'JUNUT'. See Shatskaya et al. (1980).
G6PD KABYLE. See Kaplan et al. (1967).
G6PD KALUAN. See Chockkalingam and Board (1980).
G6PD KALUGA. See Shatskaya et al. (1976).
G6PD KAMIUBE. See Nakatsuji and Miwa (1979).
G6PD KAN. See Panich (1973).
G6PD KANAZAWA. This variant, found by Kitao et al. (1982) in a Japanese male with chronic nonspherocytic hemolytic anemia, has normal electrophoretic mobility, normal Km for glucose-6-phosphate and NADP, and normal utilization of the substrate 2-deoxyglucose-6-phosphate and deamino-NADP. It shows decreased thermal stability and a biphasic pH curve. G6PD KAR KAR. See Chockkalingam et al. (1982).
G6PD KARDISTA. Stamatoyannopoulos, G.: unpublished, 1975.
G6PD KEPHALONIA. See Rattazzi et al. (1969).
G6PD KEROVOGRAD. See Krasnopolskaya and Bochkov (1982). G6PD 'KHARTOUM'. See Samuel et al. (1981).
G6PD 'KILGORE'. See Alperin and Mills (1972).
G6PD KING COUNTY. Yoshida, A.: unpublished, 1975.
G6PD KIROVOGRAD. See Shatskaya et al. (1976).
G6PD KIWA. See Nakatsuji and Miwa (1979).
G6PD KOBE. See Fujii et al. (1981).
G6PD KONAN. See Nakatsuji and Miwa (1979).
G6PD KREMENCHUNG. See Cherniak et al. (1977) and Tokarev et al. (1978).
G6PD KUANYAMA. See Balinsky et al. (1974).
G6PD KURUME. A 'deficiency' mutation, this variant leads to chronic hemolytic anemia. It is electrophoretically slow-moving. The proband was a 17-year-old male whose red cells had only 0.8% normal enzyme activity (Miwa et al., 1978). The enzyme showed normal KmG6P, normal KmNADP, low KiNADP, normal utilization of 2-deoxy-G6P and deamino-NADP, very low heat stability, and a biphasic pH curve.
G6PD 'KYOTO'. See Kojima (1972). G6PD LAGHOUAT. See Benabadji et al. (1978).
G6PD LAGUNA. Although the proband was anemic, the absence of anemia in relatives with the same G6PD variant suggested that the association was coincidental (Weimer et al., 1984). The characteristics of the mutant enzyme, including slower electrophoretic mobility, were described.
G6PD 'LANLATE'. See Usanga et al. (1977).
G6PD LAOS. Smith, J. W. and Beutler, E.: unpublished, 1981.
G6PD LAWNDALE. See Grossman et al. (1966).
G6PD LEVADIA. See Stamatoyannopoulos et al. (1970).
G6PD LIFTA. See Ramot et al. (1969).
G6PD LINCOLN PARK. See Honig et al. (1979).
G6PD LINDA VISTA. Smith, J. W. and Beutler, E.: unpublished, 1981.
G6PD 'LIZU-BAISHA'. See Du (1981).
G6PD LONG PRAIRIE. See Johnson et al. (1977).
G6PD LONG XUYEN. See Panich et al. (1980).
G6PD LOS ANGELES. See Beutler and Matsumoto (1977).
G6PD LOURENZO MARQUES. See Reys et al. (1970). G6PD LOZERE. See Vergnes et al. (1976).
G6PD LUBLIN. See Pawlak et al. (1970).
G6PD LUZ-SAINT SAUVEUR. See Vergnes et al. (1973).
G6PD LYNN (G6PD YUGOSLAVIA, FORMERLY). Beutler, E. and Lind, S.: unpublished, 1987.
G6PD MADANG. See Chockkalingam et al. (1982).
G6PD MADISON. See Shows et al. (1964).
G6PD MADRONA. See Hook et al. (1968).
G6PD MAINOKI. See Chockkalingam et al. (1982).
G6PD 'MALI'. See Kahn et al. (1971).
G6PD MAMMOLA. See Perroni et al. (1982).
G6PD MANCHESTER. See Milner et al. (1974).
G6PD MANDANG. See Chockkalingam et al. (1982).
G6PD MANJACAZE. See Reys et al. (1970).
G6PD MANUS. See Chockkalingam et al. (1982).
G6PD MARKHAM. See Kirkman et al. (1968).
G6PD 'MARTINIQUE'. See Kahn et al. (1971).
G6PD MARTINIQUE-LIKE. See Krasnopolskaya et al. (1977).
G6PD MATAM. See Kahn et al. (1975).
G6PD MELISSA. Stamatoyannopoulos, G.: unpublished, 1975.
G6PD MENORCA. See Vives-Corrons and Pujades (1982).
G6PD MERCURY. Beutler, E. and Taylor, G. P.: unpublished, 1982.
G6PD MEXICO. See Lisker et al. (1972).
G6PD MIAOZU-BAISHA. See Du et al. (1984).
G6PD MILWAUKEE. See Westring and Pisciotta (1966).
G6PD MINAS GERAIS. See Azevedo and Yoshida (1969).
G6PD MINNEAPOLIS. Johnson, G. J. and Beutler, E.: unpublished, 1980.
G6PD 'MISENO'. See Colonna-Romano et al. (1985).
G6PD MISSOULA. See Wilson (1976).
G6PD MOOSBURG. See Pekrun et al. (1989).
G6PD MORELIA. Class 4. First in class with a high Km for NADP and a low Ki for NADPH. See Vaca et al. (1985).
G6PD MOSCOW. See Batischev et al. (1977).
G6PD MURET. See Vergnes et al. (1981).
G6PD MUSASHINO. See Kumakawa et al. (1987).
G6PD NAGANO. This variant is associated with infection-induced hemolysis and chronic hemolytic anemia due to markedly impaired enzyme activity and thermal instability (Takahashi et al., 1982).
G6PD 'NAGASAKI-1'. See Kageoka et al. (1985).
G6PD 'NAGASAKI-2'. See Kageoka et al. (1985).
G6PD 'NAGASAKI-3'. See Kageoka et al. (1985).
G6PD 'NANCY'. See Streiff and Vigneron (1971).
G6PD NANHAI. See Du et al. (1988).
G6PD NAPOLI. See De Flora et al. (1981).
G6PD NEDELINO. See Toncheva and Tzoneva (1984).
G6PD NEW GUINEA-II. See Rattazzi et al. (1971).
G6PD NEW YORK. See Rattazzi et al. (1971).
G6PD N-PATHOM. See Panich (1974) and Panich and Na-Nakorn (1980).
G6PD N-SAWAN. See Panich and Na-Nakorn (1980).
G6PD NUCUS. See Yermakov et al. (1981).
G6PD NUHA. See Krasnopolskaya and Bochkov (1982).
G6PD 'NUKHA'. See Shatskaya et al. (1980).
G6PD OGIKUBO. See Miwa et al. (1978).
G6PD OGORI. See Lisker et al. (1977). G6PD OHIO. See Pinto et al. (1966).
G6PD OKHUT I. See Krasnopolskaya et al. (1977).
G6PD OKHUT II. See Krasnopolskaya et al. (1977).
G6PD OKLAHOMA. See Kirkman and Riley (1961) and Nance (1964).
G6PD ONODA. Nakashima, K.: unpublished, 1978.
G6PD ORCHOMENOS. See Stamatoyannopoulos et al. (1971).
G6PD PADREW. See Panich and Na-Nakorn (1980).
G6PD PALAKAU. See Chockkalingam et al. (1982).
G6PD 'PALEPOLI'. See Colonna-Romano et al. (1985).
G6PD 'PALLONETTO'. See Colonna-Romano et al. (1985).
G6PD 'PALMI I'. See Perroni et al. (1982).
G6PD 'PALMI II'. See Perroni et al. (1982).
G6PD PANAMA. See Beutler et al. (1974).
G6PD PANAY. See Fernandez and Fairbanks (1968).
G6PD PANAY-LIKE.
G6PD 'PARIS'. See Boivin and Galand (1968).
G6PD PEA RIDGE. See Fairbanks et al. (1980).
G6PD 'PETILIA'. See Sansone et al. (1981) and Perroni et al. (1982).
G6PD PETRICH. See Shatskaya et al. (1980).
G6PD PINAR DEL RIO. See Gonzalez et al. (1977).
G6PD PISTICCI. See Viglietto et al. (1990) and Calabro et al. (1990).
G6PD POMPTON PLAINS. Beutler, E.; Davis, S.; Forman, L. and Gelbart, T.: unpublished, 1985.
G6PD POPONDETTA. See Chockkalingam et al. (1982).
G6PD PORBANDAR. See Cayanis et al. (1977).
G6PD 'PORDENONE'. See Sansone et al. (1981) and Perroni et al. (1982).
G6PD PORT ELIZABETH. See Balinsky et al. (1973).
G6PD PORT-ROYAL. See Kaplan et al. (1971).
G6PD PORTO ALEGRE. See Hutz et al. (1977).
G6PD 'POSILIPPO'. See Colonna-Romano et al. (1985).
G6PD POZNAN. See Pawlak et al. (1975).
G6PD 'POZZALLO'. See Perroni et al. (1982).
G6PD PUERTO RICO. See McCurdy et al. (1973).
G6PD QING-BAILJIANG. See Du et al. (1988).
G6PD RAMAT-GAN. See Ramot et al. (1969).
G6PD REGAR. See Ermakov et al. (1983).
G6PD REGENSBURG. See Eber et al. (1985).
G6PD 'RENNES'. See Picat et al. (1980).
G6PD ROTTERDAM. See Rattazzi et al. (1971).
G6PD RUDOSEM. See Toncheva and Tzoneva (1984).
G6PD RUSSIAN-MOSCOW. See Krasnopolskaya and Bochkov (1982).
G6PD SALATA. See Chockkalingam and Board (1980).
G6PD SAMANDAG. See Aksoy et al. (1987).
G6PD SAN DIEGO. See Howell et al. (1972).
G6PD SAN FRANCISCO. See Mentzer et al. (1980).
G6PD SAN JOSE. See Castro and Snyder (1974).
G6PD SAN JUAN. See McCurdy et al. (1973).
G6PD SANTA BARBARA. Kidder, W. R. and Beutler, E.: unpublished, 1979.
G6PD SAPPORO. See Fujii et al. (1981).
G6PD 'SCHWABEN'. See Benohr et al. (1971).
G6PD 'S.DONA'. See Perroni et al. (1982).
G6PD SEATTLE. See Kirkman et al. (1965).
G6PD SELIM. See Shatskaya et al. (1975).
G6PD SENDAGI. This variant was associated with chronic nonspherocytic hemolytic anemia in a 2-year-old Japanese male in whom upper respiratory infection precipitated a hemolytic crisis (Morisaki et al.,1983).
G6PD SHEKII. See Krasnopolskaya et al. (1977).
G6PD SHIRIN-BULAKH. See Krasnopolskaya et al. (1977).
G6PD SIRIRAJ. See Panich et al. (1972).
G6PD SIWA. See McCurdy et al. (1974).
G6PD SONGKHLA. See Panich and Na-Nakorn (1980).
G6PD S-SAKORN. See Panich (1980).
G6PD ST. LOUIS. See Kahn et al. (1974).
G6PD STEILACOM. Yoshida, A.; Baur, E. and Voigtlander, B.: unpublished, 1975.
G6PD 'STELLA'. See Colonna-Romano et al. (1985).
G6PD 'STRASBOURG'. See Waitz et al. (1970).
G6PD SWIT. See Chockkalingam et al. (1982).
G6PD TACOMA. Yoshida, A. and Baur, E.: unpublished, 1975.
G6PD TACOMA-LIKE. See Vergnes et al. (1975).
G6PD TAHTA. See McCurdy et al. (1974).
G6PD TAIPEI-HAKKA. See McCurdy et al. (1970).
G6PD 'TAIWAN-AMI 5'. See McCurdy et al. (1970).
G6PD 'TAIWAN-AMI 6'. See McCurdy et al. (1970).
G6PD TARSUS. See Gahr et al. (1976).
G6PD TASHKENT. See Yermakov et al. (1981).
G6PD TEHERAN. McCurdy, P. R.: unpublished, 1965.
G6PD TEL HASHOMER. See Ramot and Brok (1964) and Kirkman et al. (1969).
G6PD TENGANAN. See Chockkalingam et al. (1982).
G6PD THENIA. See Benabadji et al. (1978).
G6PD THESSALONIKI. Koliakos et al. (1989) found a new variant in a 70-year-old patient with idiopathic myelofibrosis. This disorder, formerly called agnogenic myeloid metaplasia, is a myeloproliferative disease with clonal origin in a malignant pluripotent stem cell. Bone marrow fibrosis is a secondary process. The patient was thought to be heterozygous since her only son had normal G6PD. That she showed severe G6PD deficiency was taken to indicate that the normal X chromosome was active in the original cell that underwent malignancy.
G6PD THESSALY. See Stamatoyannopoulos et al. (1970).
G6PD TITTERI. See Benabadji et al. (1978).
G6PD TITUSVILLE. Csepreghy et al. (1989) described a new G6PD variant in a 7-month-old black male and his mother. The proband had had a transient hemolytic episode.
G6PD TOKUSHIMA. See Miwa et al. (1976).
G6PD TOKYO. See Miwa et al. (1976).
G6PD TORONTO. See Crookston et al. (1973).
G6PD TORRANCE. See Tanaka and Beutler (1969).
G6PD TOULOUSE. See Vergnes et al. (1974).
G6PD 'TRAPANI'. See Sansone et al. (1981) and Perroni et al. (1982).
G6PD TRINACRIA. See Sansone et al. (1977).
G6PD TRIPLER. See Engstrom and Beutler (1970).
G6PD TSUKUI. See Ogura et al. (1988).
G6PD TUBINGEN. See Benohr and Waller (1970).
G6PD TURSI. See Viglietto et al. (1990) and Calabro et al. (1990).
G6PD UBE. See Nakashima et al. (1977).
G6PD UNION. See Yoshida et al. (1970).
G6PD 'UNION-MARKHAM'. See Stamatoyannopoulos et al. (1971).
G6PD 'UNNAMED'. See Othieno-Obel (1972).
G6PD 'VARADERO'. See Estrada et al. (1982).
G6PD VELLETRI. See Mandelli et al. (1977).
G6PD VIENTIANE. See Kahn et al. (1978).
G6PD 'VIN FU'. See Toncheva (1986).
G6PD WAKAYAMA. This variant was found in a 16-month-old boy with 4.5% of normal enzyme activity and mild hemolytic anemia (Miwa et al., 1978). Electrophoretically, it is slow-moving like G6PD Kurume, from which it differs by a normal pH curve. In addition to the 4 slow variants reported by Miwa et al. (1978), 5 had previously been reported: Alhambra, Atlanta, Hong Kong Pokfulam, Manchester, and Tokyo. G6PD WASHINGTON. McCurdy, P. R.: unpublished, 1975.
G6PD WATERLOO. Beutler, E. and Phyliky, R. L.: unpublished, 1978.
G6PD WAYNE. See Ravindranath and Beutler (1987).
G6PD WEST BENGAL. See Azevedo et al. (1968).
G6PD WEST TOWN. This variant causes chronic nonspherocytic anemia which is compensated except following infections or exposure to an oxidant drug (Honig et al., 1979).
G6PD WESTERN. Yoshida, A. and Baur, E.: unpublished, 1975.
G6PD WEWAK. See Chockkalingam et al. (1982).
G6PD WORCESTER. Snyder et al. (1970) described a family in which a new variant form of G6PD was associated with congenital nonspherocytic hemolytic anemia and optic atrophy in 3 males related as first cousins once removed. Blindness developed rapidly in the teens.
G6PD 'WROCLAW'. See Kwiatkowska and Kacprzak-Bergman (1971).
G6PD YAMAGUCHI. This variant was found in an 8-year-old boy who had 3.5% of normal enzyme activity and moderate hemolytic anemia (Miwa et al., 1978). Electrophoretically, it is slow-moving, like G6PD Kurume, from which it differs by high Km NADP, high deamino-NADP utilization, and an abnormal pH curve of a different type (with narrow peak at pH 8.76).
G6PD YANGORU. See Chockkalingam et al. (1982).
G6PD YOKOHAMA. See Miwa et al. (1978).
G6PD 'ZAEHRINGEN'. See Witt and Yoshioka (1972).
G6PD ZAKATALY. See Krasnopolskaya et al. (1977).
G6PD ZHITOMIR. See Shatskaya et al. (1976).
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