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

L. Góth, Márta Vitai, Péter Rass, Eszter Sükei, Anikó Páy

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1646-1649
Number of pages4
JournalElectrophoresis
Volume26
Issue number9
DOIs
Publication statusPublished - May 2005

Fingerprint

Acatalasia
Medical problems
Catalase
Introns
Diabetes Mellitus
Hydrogen Peroxide
Mutation
Screening
Essential Amino Acids
Hungary
Poisons
Cellular Structures
Type 2 Diabetes Mellitus
Exons
Polymorphism
Nucleotides
Metabolism
Blood
Enzymes

Keywords

  • Blood catalase activity
  • Catalase mutation
  • Diabetes mellitus

ASJC Scopus subject areas

  • Clinical Biochemistry

Cite this

Detection of a novel familial catalase mutation (Hungarian type D) and the possible risk of inherited catalase deficiency for diabetes mellitus. / Góth, L.; Vitai, Márta; Rass, Péter; Sükei, Eszter; Páy, Anikó.

In: Electrophoresis, Vol. 26, No. 9, 05.2005, p. 1646-1649.

Research output: Contribution to journalArticle

Góth, L. ; Vitai, Márta ; Rass, Péter ; Sükei, Eszter ; Páy, Anikó. / Detection of a novel familial catalase mutation (Hungarian type D) and the possible risk of inherited catalase deficiency for diabetes mellitus. In: Electrophoresis. 2005 ; Vol. 26, No. 9. pp. 1646-1649.
@article{10dc74bef09f4b2cb5351a6d7e50a5a6,
title = "Detection of a novel familial catalase mutation (Hungarian type D) and the possible risk of inherited catalase deficiency for diabetes mellitus",
abstract = "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.",
keywords = "Blood catalase activity, Catalase mutation, Diabetes mellitus",
author = "L. G{\'o}th and M{\'a}rta Vitai and P{\'e}ter Rass and Eszter S{\"u}kei and Anik{\'o} P{\'a}y",
year = "2005",
month = "5",
doi = "10.1002/elps.200410384",
language = "English",
volume = "26",
pages = "1646--1649",
journal = "Electrophoresis",
issn = "0173-0835",
publisher = "Wiley-VCH Verlag",
number = "9",

}

TY - JOUR

T1 - Detection of a novel familial catalase mutation (Hungarian type D) and the possible risk of inherited catalase deficiency for diabetes mellitus

AU - Góth, L.

AU - Vitai, Márta

AU - Rass, Péter

AU - Sükei, Eszter

AU - Páy, Anikó

PY - 2005/5

Y1 - 2005/5

N2 - 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.

AB - 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.

KW - Blood catalase activity

KW - Catalase mutation

KW - Diabetes mellitus

UR - http://www.scopus.com/inward/record.url?scp=18844424909&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=18844424909&partnerID=8YFLogxK

U2 - 10.1002/elps.200410384

DO - 10.1002/elps.200410384

M3 - Article

C2 - 15800961

AN - SCOPUS:18844424909

VL - 26

SP - 1646

EP - 1649

JO - Electrophoresis

JF - Electrophoresis

SN - 0173-0835

IS - 9

ER -