DNA sequence abnormalities in human glucose 6-phosphate isomerase deficiency

Walker, James I. H.; Layton, D. M.; Bellingham, A. J.; Morgan, Michael J.; Faik, Pelin

doi:10.1093/hmg/2.3.327

Cited by 31 publications

(9 citation statements)

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“…The c1039 C 3 T mutation found in exon 12 of the GPI gene of this patient as well as in her father has been described recently by Xu and Beutler [30]. It causes an Arg 347 3 Cys substitution and is closely located to Asp 342, which is according to Walker et al [28] a putative catalytic site in the pig protein. Interestingly in the same paper the authors described an adjacent mutation c1040 G 3 A that results in an Arg 346 3 His substitution.…”

Section: Discussionsupporting

confidence: 53%

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Glucose phosphate isomerase deficiency: biochemical and molecular genetic studies on the enzyme variants of two patients with severe haemolytic anaemia

Huppke

Wünsch

Pekrun

et al. 1997

European Journal of Pediatrics

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Section: Discussionsupporting

confidence: 53%

“…Since the ®rst description of DNA sequence abnormalities in 1993 [28] the analysis of the GPI gene performed with 12 patients ± 6 homozygotes and 6 compound heterozygotes suering from GPI de®ciency ± resulted in the discovery of 14 missense mutations, 1 nonsense mutation and a 4 nucleotide deletion [1,9,28,30].…”

Section: Introductionmentioning

confidence: 99%

Glucose phosphate isomerase deficiency: biochemical and molecular genetic studies on the enzyme variants of two patients with severe haemolytic anaemia

Huppke

Wünsch

Pekrun

et al. 1997

European Journal of Pediatrics

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“…This mutation seems to induce the enzyme instability, resulting in chronic hemolysis. In addition, two homozygous missense mutations and four compound heterozygous missense mutations have been determined [76,77]. Phosphofructokinase (PFK) deficiency is associated with a heterogenous group of clinical symptoms characterized by myopathy (Tarui disease) and/or hemolysis, or an asymptomatic state.…”

Section: Other Enzyme Deficiencies With Defined Molecular Defectsmentioning

confidence: 99%

Molecular basis of erythroenzymopathies associated with hereditary hemolytic anemia: Tabulation of mutant enzymes

Shiro¹,

Fujii²

1996

American J Hematol

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Molecular abnormalities of erythroenzymopathies associated with hereditary hemolytic anemia have been determined by means of molecular biology. Pyruvate kinase (PK) deficiency is the most common and well-characterized enzyme deficiency in the glycolytic pathway, and it causes hereditary hemolytic anemia. To date, 47 gene mutations have been identified. We identified one base deletion, one splicing mutation, and six distinct missense mutations in 12 unrelated families with a homozygous PK deficiency. Mutations located near the substrate or fructose-1,6- diphosphate binding site may change the conformation of the active site, resulting in a drastic loss of activity and severe clinical symptoms. Glucose-6-phosphate dehydrogenase (G6PD)deficiency is the most common metabolic disorder, and it is associated with chronic hemolytic anemia and/or drug- or infection-induced acute hemolytic attack. An estimated 400 million people are affected worldwide. The mutations responsible for about 78 variants have been determined. Some have polymorphic frequencies in different populations. Most variants are produced by one or two nucleotide substitutions. Molecular studies have disclosed that most of the class 1 G6PD variants associated with chronic hemolysis have the mutations surrounding either the substrate or the NADP binding site. Among rare enzymopathies, missense mutations have been determined in deficiencies of glucosephosphate isomerase, (TPI), phosphoglycerate kinase, and adenylate kinase. Compound heterozygosity with missense mutation and base deletion has been determined in deficiencies of hexokinase and diphosphoglyceromutase. Compound heterozygosity with missense and nonsense mutations has been identified in TPI deficiency. One base junction mutations resulting in abnormally spliced PFK-M mRNA have been identified in homozygous PFK deficiency. An exception is hemolytic anemia due to increased adenosine deaminase activity. The basic abnormality appears to result from the overproduction of a structurally normal enzyme.

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“…In some cases, GPI deficiency is associated with splenomegaly and, in a few cases, neurologic impairment. Recently, we studied (Repiso et al, 2005) the enzymatic and familial characterization of a GPI homozygous mutation p.Arg346His, previously reported in a double heterozygote patient (Walker et al, 1993). In the current study, three new GPI mutations in two Spanish patients with GPI deficiency and CNSHA are reported.…”

Section: Introductionmentioning

confidence: 99%

Red cell glucose phosphate isomerase (GPI): a molecular study of three novel mutations associated with hereditary nonspherocytic hemolytic anemia

et al. 2006

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Molecular characteristics of red blood cell (RBC) glucose phosphate isomerase (GPI) deficiency are described in two Spanish patients with chronic nonspherocytic hemolytic anemia. One patient, with residual GPI activity in RBCs of around 7% (GPI-Catalonia), is homozygous for the missense mutation c.1648A>G (p.Lys550Glu) in exon 18. The other patient, with residual activity in RBCs of around 20% (GPI-Barcelona), was found to be a compound heterozygote for two different missense mutations: c.341A>T (p.Asp113Val) in exon 4 and c.663T>G (p.Asn220Lys) in exon 7. Molecular modeling using the human crystal structure of GPI as a model was performed to determine how these mutations could affect enzyme structure and function.

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DNA sequence abnormalities in human glucose 6-phosphate isomerase deficiency

Cited by 31 publications

References 0 publications

Glucose phosphate isomerase deficiency: biochemical and molecular genetic studies on the enzyme variants of two patients with severe haemolytic anaemia

Glucose phosphate isomerase deficiency: biochemical and molecular genetic studies on the enzyme variants of two patients with severe haemolytic anaemia

Molecular basis of erythroenzymopathies associated with hereditary hemolytic anemia: Tabulation of mutant enzymes

Red cell glucose phosphate isomerase (GPI): a molecular study of three novel mutations associated with hereditary nonspherocytic hemolytic anemia

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