Genetic heterogeneity in acatalasemia

Góth, László; Páy, Anikó

doi:10.1002/elps.1150170805

Cited by 8 publications

(3 citation statements)

References 12 publications

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“…In contrast, none of the 66 normocatalasemic family members suffered from diabetes mellitus [13,14]. Genetic analysis of these families showed that the known types of Japanese acatalasemia (2) were not found in the Hungarian families [15,16].…”

Section: Introductionmentioning

confidence: 76%

Detection of a novel familial catalase mutation (Hungarian type D) and the possible risk of inherited catalase deficiency for diabetes mellitus

Góth

Vitai

Rass³

et al. 2005

ELECTROPHORESIS

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The enzyme catalase is the main regulator of hydrogen peroxide metabolism. Recent findings suggest that a low concentration of hydrogen peroxide may act as a messenger in some signalling pathways whereas high concentrations are toxic for many cells and cell components. Acatalasemia is a genetically heterogeneous condition with a worldwide distribution. Yet only two Japanese and three Hungarian syndrome-causing mutations have been reported. A large-scale (23 130 subjects) catalase screening program in Hungary yielded 12 hypocatalasemic families. The V family with four hypocatalasemics (60.6 +/- 7.6 MU/L) and six normocatalasemic (103.6 +/- 23.5 MU/L) members was examined to define the mutation causing the syndrome. Mutation screening yielded four novel polymorphisms. Of these, three intron sequence variations, namely G-->A at the nucleotide 60 position in intron 1, T-->A at position 11 in intron 2, and G-->T at position 31 in intron 12, are unlikely to be responsible for the decreased blood catalase activity. However, the novel G-->A mutation in exon 9 changes the essential amino acid Arg 354 to Cys 354 and may indeed be responsible for the decreased catalase activity. This inherited catalase deficiency, by inducing an increased hydrogen peroxide steady-state concentration in vivo, may be involved in the early manifestation of type 2 diabetes mellitus for the 35-year old proband.

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Section: Introductionmentioning

confidence: 76%

Detection of a novel familial catalase mutation (Hungarian type D) and the possible risk of inherited catalase deficiency for diabetes mellitus

Góth

Vitai

Rass³

et al. 2005

ELECTROPHORESIS

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“…We have reported on two acatalasemic sisters in the first Hungarian acatalasemic family [9] and nine hypocatalasemic families [10] with 37 hypocatalasemics including the biochemical markers of lipid and carbohydrate metabolism in acatalasemia and hypocatalasemia [11]. In Hungarian acatalasemic and hypocatalasemic patients, we could not detect the mutations responsible for the defect catalase synthesis in Japanese patients [12,13]. For the acatalasemic and three hypocatalasemic families, we found a GA insertion at position 138 of exon 2.…”

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confidence: 83%

A novel catalase mutation detected by polymerase chain reaction-single strand conformation polymorphism, nucleotide sequencing, and Western blot analyses is responsible for the type C of Hungarian acatalasemia

2001

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Polymerase chain reaction-single strand conformation polymorphism (PCR-SSCP) screening was used for searching mutations of the catalase gene in two Hungarian hypocatalasemic families. A syndrome-causing mutation was found in a PCR product containing exon 7 and its boundaries. Nucleotide sequence analyses detected a G to T substitution at position 5 of intron 7. The effect of this splice site mutation was confirmed by Western blot analyses demonstrating a decreased catalase protein level in these patients. These findings represent a novel type (C) of catalase mutations in the Hungarian acatalasemic/hypocatalasemic patients.

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“…The biochemical characterization of their catalase protein revealed a difference from the Swiss type and similarity to the Japanese type of this syndrome [8]. In contrast to this similarity, the lack of G to A mutation at the fifth position of intron four for Hungarian acatalasemic patients revealed genetic heterogeneity in acatalasemia between Caucasians and Japanese [9]. Heterozygotes of Hungarian acatalasemia showed half the normal blood catalase (hypocatalasemia) activity, similar to the Japanese patients [lo].…”

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confidence: 99%

Further genetic heterogeneity in acatalasemia

Góth

1997

Electrophoresis

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A T-deletion at position 10 of exon 4 for catalase gene was reported as a novel mutation, causing a new genetic type of acatalasemia in Japan. This mutation, destroying a Hinf1 recognition site, was searched for in Hungarian acatalasemic (2) and hypocatalasemic (22) patients and in controls (27) by Hinf1 digestion and sequence analyses of a 203 bp polymerase chain reaction (PCR) product containing the entire exon 4. The Hinf1 polymorphism did not reveal any difference between controls and hypocatalasemic as well as acatalasemic patients. These results were confirmed by sequence analyses showing the T nucleotide for the two acatalasemic and for one unrelated hypocatalasemic patient, as well as for two controls. These findings represent further evidence that acatalasemia is heterogeneous at the DNA level.

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Genetic heterogeneity in acatalasemia

Cited by 8 publications

References 12 publications

Detection of a novel familial catalase mutation (Hungarian type D) and the possible risk of inherited catalase deficiency for diabetes mellitus

Detection of a novel familial catalase mutation (Hungarian type D) and the possible risk of inherited catalase deficiency for diabetes mellitus

A novel catalase mutation detected by polymerase chain reaction-single strand conformation polymorphism, nucleotide sequencing, and Western blot analyses is responsible for the type C of Hungarian acatalasemia

Further genetic heterogeneity in acatalasemia

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