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Other entities represented in this entry:
HGNC Approved Gene Symbol: PGK1
Cytogenetic location: Xq21.1 Genomic coordinates (GRCh38): X:78,104,248-78,129,295 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| Xq21.1 | Phosphoglycerate kinase 1 deficiency | 300653 | X-linked recessive | 3 |
The PGK1 gene encodes phosphoglycerate kinase-1, also known as ATP:3-phosphoglycerate 1-phosphotransferase (EC 2.7.2.3), which catalyzes the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate during glycolysis, generating one molecule of ATP.
PGK1 is distinguished from testicular PGK2 (172270), which maps to chromosome 6p21.
Michelson et al. (1983) isolated a full-length cDNA clone of PGK from a human fetal liver cDNA library using synthetic oligonucleotide mixtures as hybridization probes. The deduced protein contains 417 amino acid residues. Southern blot analysis of human genomic DNAs showed a complex pattern of hybridizing fragments, 2 of which were non-X in origin. The results were interpreted as reflecting the existence of a small family of dispersed PGK or PGK-like genes.
Using a mixture of synthetic oligodeoxyribonucleotides, Singer-Sam et al. (1983) isolated a cDNA encoding amino acids 291-296 of PGK.
The human PGK1 gene contains 11 exons and spans approximately 23 kilobases (Michelson et al., 1985).
Disulfide bonds in secreted proteins are considered to be inert because of the oxidizing nature of the extracellular milieu. An exception to this rule is a reductase secreted by tumor cells that reduces disulfide bonds in the serine proteinase plasmin. Reduction of plasmin initiates proteolytic cleavage in the kringle 5 domain and release of the tumor blood vessel inhibitor angiostatin. New blood vessel formation or angiogenesis is critical for tumor expansion and metastasis. Lay et al. (2000) showed that the plasmin reductase isolated from conditioned medium of fibrosarcoma cells is the glycolytic enzyme phosphoglycerate kinase. Recombinant phosphoglycerate kinase had the same specific activity as the fibrosarcoma-derived protein. Plasma of mice bearing fibrosarcoma tumors contained several-fold more phosphoglycerate kinase, as compared with mice without tumors. Administration of phosphoglycerate kinase to tumor-bearing mice caused an increase in plasma levels of angiostatin, and a decrease in tumor vascularity and rate of tumor growth. Lay et al. (2000) concluded that phosphoglycerate kinase not only functions in glycolysis but is secreted by tumor cells and participates in the angiogenic process as a disulfide reductase.
By somatic cell hybridization, Grzeschik et al. (1972) concluded that the PGK locus was on the long arm of the X chromosome. From the study of chromosomal aberrations in cell hybridization systems, Ricciuti and Ruddle (1973) concluded that the order on the X chromosome was centromere--PGK--HPRT (308000)--G6PD (305900). The conclusion was based on their own work with the KOP 14-X translocation, and on Park Gerald's with a 19-X translocation and Bootsma's with a 3-X translocation. All 3 had breaks involving the long arm of the X chromosome, each at a different site. From study of radiation-induced segregants in which irradiated human cells are rescued by fusion with hamster cells, Goss and Harris (1977) showed that the order of the 4 loci is PGK: alpha-GAL (300644): HPRT: G6PD and that the 3 intervals between these 4 loci are, in relative terms, 0.33, 0.30, and 0.23.
Willard et al. (1985) used a cDNA for human PGK to map the functional PGK1 gene to Xq13. Evidence reported by Verga et al. (1991) suggested that PGK1, which is distal to the Menkes disease gene (309400), may be located in Xq13.3.
PGK is X-linked in the kangaroo (Cooper et al., 1971). Alpha-GALA, 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).
Pseudogenes
One pseudogene of PGK1 (PGK1P1) is on Xq at Xq11-Xq13, proximal to the expressed PGK1 gene at Xq13 (Michelson et al., 1985; Willard et al., 1985). The pseudogene was mapped by somatic hybrid cell and in situ hybridization methods using a cloned DNA probe in each case.
Willard et al. (1985) identified a 10-kb PGK-related DNA sequence on human chromosome 19, which the authors suggested could represent a pseudogene, the putative testes-specific PGK gene, or some other related gene. Gartler et al. (1986) mapped a 1-kb PGK sequence to chromosome 19, which represents the second pseudogene PGK1P2.
Chen et al. (1971) described an electrophoretic variant of PGK with enzyme activity in the normal range. Using a PGK cDNA probe, Hutz et al. (1984) identified a common DNA polymorphism with the restriction enzyme PstI. About 48% of females in all ethnic groups were found to be heterozygous. Data on gene frequencies of allelic variants were tabulated by Roychoudhury and Nei (1988).
Phosphoglycerate Kinase-1 Deficiency
In a patient with chronic hemolytic anemia associated with deficiency of PGK1 activity (300653), Fujii and Yoshida (1980) used peptide mapping analysis to identify an arg206-to-pro (R206P; 311800.0002) substitution in the PGK1 protein. The PGK1 variant was referred to as 'Uppsala.'
Sugie et al. (1998) described an 837T-C mutation (311800.0009) in the PGK gene of a patient with PGK Hamamatsu and the myopathic form of PGK1 deficiency.
In 2 unrelated boys of Spanish origin with severe lifelong chronic hemolytic anemia and progressive neurologic impairment, Noel et al. (2006) identified 2 different mutations in the PGK1 gene (311800.0011 and 311800.0012, respectively).
Spiegel et al. (2009) reported an 18-year-old man of Arab Bedouin descent with PGK1 deficiency confirmed by genetic analysis (T378P; 311800.0015). He had a purely myopathic phenotype, with onset of muscle cramps and exercise-induced pigmenturia at age 7 years. He had no evidence of hemolytic anemia or neurologic involvement; serum creatine kinase was increased. Biochemical studies showed decreased PGK1 activity in muscle (0.9% of control values) and erythrocytes (1.6%). The patient's unaffected mother and 2 sisters were heterozygous for the mutation.
By peptide mapping analysis, Fujii et al. (1980) found an asp268-to-asn (D268N) substitution in the PGK1 enzyme that was associated with mild enzymatic deficiency (21% of normal activity) and was heat-unstable. There was no hemolytic anemia or accumulation of intermediate metabolites. Krietsch et al. (1977, 1980) described a large German kindred with PGK Munchen. Although the variant showed decreased activity, none of the carriers had overt clinical symptoms.
In a patient with chronic hemolytic anemia associated with deficiency of PGK activity (300653), Fujii and Yoshida (1980) used peptide mapping analysis to identify an arg206-to-pro (R206P) substitution in the PGK1 protein.
In a patient with chronic nonspherocytic hemolytic anemia and neurologic disturbances due to PGK1 deficiency (300653), Fujii et al. (1981) used peptide mapping analysis to identify a val266-to-met (V266M) substitution in the PGK1 enzyme. The variant enzyme had 16% activity compared to controls.
Chen et al. (1971) found an electrophoretic polymorphism of PGK in a New Guinea population, where the frequency of a variant enzyme, termed 'PGK II,' showed a gene frequency of about 0.014. In starch gel electrophoresis, the variant enzyme moved toward the anode faster than the normal enzyme. Yoshida et al. (1972) found that the PGK II variant had a substitution of threonine to asparagine. The same substitution was found in a Samoan male. Fujii et al. (1981) stated that the thr-to-asn change was at position 352. The variant was not associated with enzyme deficiency.
PGK Matsue is an electrophoretic variant associated with severe enzyme deficiency, congenital nonspherocytic anemia, and mental disorders (300653) (Miwa et al., 1972). In a cell line from a patient who died at age 9 from complications of pneumonia, Maeda and Yoshida (1991), who found a T/A-to-C/G transition in exon 3 of the PGK gene, resulting in a leu88-to-pro (L88P) substitution. The nucleotide change created an additional NciI cleavage site. Because the substitution was expected to induce serious perturbation and instability in the protein structure, Maeda and Yoshida (1991) suspected that the severe enzyme deficiency was caused mainly by more rapid in vivo denaturation and degradation of the variant enzyme.
Tani et al. (1985) found that PGK Matsue enzyme activity was about 5% of control values. PGK Matsue mRNA was present in normal amounts in fibroblasts, suggesting the enzyme deficiency was due to a 7- to 10-fold increase in degradation of the mutant enzyme.
In a 27-year-old Japanese male with PGK1 deficiency (300653), Fujii et al. (1992) identified a 473G-T transversion in the PGK1 gene, resulting in a gly157-to-val (G157V) substitution The mutation created a new BstXI cleavage site in exon 5. The patient had chronic hemolytic anemia and myoglobinuria, manifested by nausea, anorexia, and muscle weakness after exercise, beginning at the age of 10. There was no family history of anemia or neuromuscular disease.
In a 14-year-old boy with mental retardation, a behavior disorder, and episodic hemolytic anemia due to PGK1 deficiency (300653), Maeda et al. (1992) identified a T-to-C transition in exon 9 of the PGK1 gene, resulting in a cys315-to-arg (C315R) substitution. The nucleotide substitution created an additional AvaII cleavage site in the variant gene. Since the variant gene was not detected in the proband's mother and sibs, it must have originated by de novo mutation during oogenesis. Because the variant was found in Michigan, it was designated 'PGK Michigan.'
In a 37-year-old white male school teacher with PGK1 deficiency (300653), Yoshida et al. (1995) identified a 3-bp deletion in exon 7 of the PGK gene, resulting in a deletion of lys191 in a highly conserved region within alpha-helix 7 of the protein. The patient had had infrequent episodes of jaundice prompting a diagnosis of hepatitis. The authors noted that deletion of lysine could cause molecular instability, as suggested by the rapid in vitro inactivation of the variant PGK in this patient.
In an 11-year-old boy with PGK1 deficiency (300653), Sugie et al. (1998) identified an 837T-C transition in the PGK1 gene, resulting in an ile252-to-thr (I252T) substitution. The boy was mentally retarded and had had recurrent episodes of convulsions followed by generalized myalgia, muscle weakness, and pigmenturia.
Bischof et al. (2006) demonstrated that the I252T mutation originates by gene conversion from a processed pseudogene. A PGK1 pseudogene (PGK1P1) carries the 837T-C transition that produces the I252T substitution associated with phosphoglycerate kinase deficiency.
In a Danish patient with PGK1 deficiency (300653), Valentin et al. (1998) identified an asp285-to-val (D285V) substitution in the PGK1 gene. The patient had isolated hemolytic anemia without neurologic or muscular disorders. The mutated gene was expressed only partially; both normal and substituted nucleotides were found at the same position in a ratio of approximately 1:9. Valentin et al. (1998) presumed that somatic mutation with mosaicism was the likely explanation for the relatively mild phenotype.
In a Spanish boy with PGK1 deficiency (300653), Noel et al. (2006) identified a 140T-A transversion in the PGK1 gene, resulting in an ile46-to-asn (I46N) substitution. He had a long history of chronic hemolytic anemia and progressive neurologic impairment leading to mental deterioration. No muscular dystrophy could be demonstrated. The mutation was present in heterozygous state in the patient's mother. Based on the crystal structure of porcine PGK, the I46N mutation did not modify any of the PGK binding sites for ATP or 3PG, so the consequences must be related to a loss of the enzyme stability rather than a decrease of enzyme catalytic function. Noel et al. (2006) noted that the first report of PGK Barcelona was published in an abstract (Ramirez et al., 2002).
In a boy from Murcia with PGK1 deficiency (300653), Noel et al. (2006) identified a 958G-A transition in the PGK1 gene, resulting in a ser319-to-asn (S319N) substitution. He had severe hemolytic anemia, encephalopathy, and seizures, and died at age 7 years. His mother and sister were heterozygous for the mutation. Based on the crystal structure of porcine PGK, the S319N mutation did not modify any of the PGK binding sites for ATP or 3PG, so the consequences must be related to a loss of the enzyme stability rather than a decrease of enzyme catalytic function.
In 2 affected boys of a white American family with PGK1 deficiency (300653), Flanagan et al. (2006) identified a 491A-T transversion in exon 5 of the PGK1 gene, resulting in an asp164-to-val (D164V) substitution. The 2 boys presented with hemolytic anemia, seizures, and developmental delay. The diagnosis of PGK deficiency was based on an erythrocyte PGK enzyme activity level of less than 5% of normal and identification of the D164V mutation. This mutation had previously been designated PGK-Amiens and described in a French PGK patient (Cohen-Solal et al., 1994) and in a large family of Chinese extraction living in New York (Valentine et al., 1969; Turner et al., 1995). The proband in the family reported by Flanagan et al. (2006) also had hemiplegic migraines, retinal dystrophy, and muscle fatigue. The 3 families in which this mutation had been described appeared to represent recurrent mutations.
This variant has also been referred to as PGK NEW YORK.
In a 33-year-old Japanese man with PGK1 deficiency (300653), Shirakawa et al. (2006) identified a G-to-A transition in intron 7 of the PGK1 gene, resulting in aberrant splicing and a catalytically inactive protein. The patient had mental retardation and exertional myoglobinuria, but no evidence of hemolytic anemia. PGK1 enzyme activity was 8.9% and 13.6% of control values in muscle and red blood cells, respectively.
In an 18-year-old man of Arab Bedouin descent with PGK1 deficiency (300653), Spiegel et al. (2009) identified a 1132A-C transversion in exon 10 of the PGK1 gene, resulting in a thr378-to-pro (T378P) substitution in a highly conserved residue. The patient had a myopathic phenotype, with onset of muscle cramps and exercise-induced pigmenturia at age 7 years. He had no evidence of hemolytic anemia or neurologic involvement; serum creatine kinase was increased. Protein structural analysis predicted that the mutation would destabilize an alpha-helix and interfere with the contact of domains responsible for proper catalytic interactions with nucleotide phosphates. Biochemical studies showed decreased PGK1 activity in muscle (0.9% of control values) and erythrocytes (1.6%). The patient's unaffected mother and 2 sisters were heterozygous for the mutation.
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