@article{MTMT:2817325,
	title = {Further acatalasemia mutations in human patients from Hungary with diabetes and microcytic anemia},
	url = {https://m2.mtmt.hu/api/publication/2817325},
	author = {Nyesténé Nagy, Teréz and Paszti, Erika and Káplár, Miklós and Bhattoa Harjit, Pál and Góth, László},
	doi = {10.1016/j.mrfmmm.2014.12.008},
	journal-iso = {MUTAT RES-FUND MOL M},
	journal = {MUTATION RESEARCH-FUNDAMENTAL AND MOLECULAR MECHANISMS OF MUTAGENESIS},
	volume = {772},
	unique-id = {2817325},
	issn = {0027-5107},
	abstract = {Abstract In blood, the hydrogen peroxide concentration is regulated by catalase. Decreased activity of catalase may lead to increased hydrogen peroxide concentration, which may contribute to the manifestation of age-related disease. The aim of this study is to examine association of decreased blood catalase activity and catalase exon mutations in patients (n = 617) with diabetes (n = 380), microcytic anemia (n = 58), beta-thalassemia (n = 43) and presbycusis (n = 136) and in controls (n = 295). Overall, 51 patients (8.3%) had less than half of normal blood catalase activity. Their genomic DNA was used for mutation screening of all exons and exon/intron boundaries with polymerase chain reaction-single-strand conformation polymorphism (PCR-SSCP) and PCR-heteroduplex analyses, and mutations were verified with nucleotide sequencing. Seven patients (type 2 diabetes (n = 3), gestational diabetes (n = 1), microcytic anemia (n = 2)) had four novel catalase exon mutations namely, c.106_107insC, p.G36Afs*5(n = 3, Hungarian type G1), c.379C>T, p.R127Y (n = 2, Hungarian type H1), c.390T>C, p.R129L, (n = 1, Hungarian type H2) and c.431A>T, p.N143V (n = 1, Hungarian type H3). In patients with decreased blood catalase, the incidence of acatalasemia mutations was significantly high (P < 0.0002) in microcytic anemia, type 2 and gestational diabetes. The four novel mutations were probably responsible for low blood catalase activity in 7/51 patients. In the remainder of the cases, other polymorphisms and epigenetic/regulatory factors may be involved.},
	keywords = {Aged; Adult; Adolescent; Female; Middle Aged; Male; DNA; ARTICLE; GENOMICS; human; diabetes mellitus; Hungary; Child; Incidence; polymerase chain reaction; nucleotide sequence; frameshift mutation; major clinical study; controlled study; DNA sequence; enzyme activity; insulin dependent diabetes mellitus; preschool child; Catalase; pregnancy diabetes mellitus; intron; exon; non insulin dependent diabetes mellitus; missense mutation; mutational analysis; microcytic anemia; heteroduplex analysis; beta thalassemia; catalase deficiency; mutation screening; Blood catalase; Presbyacusis; Novel catalase exon mutations; Catalase decrease; Hungarian (citizen); single stranded conformation polymorphism},
	year = {2015},
	eissn = {1873-135X},
	pages = {10-14},
	orcid-numbers = {Bhattoa Harjit, Pál/0000-0002-4909-0065}
}

@article{MTMT:2393863,
	title = {A simple method for examination of polymorphisms of catalase exon 9: Rs769217 in Hungarian microcytic anemia and beta-thalassemia patients},
	url = {https://m2.mtmt.hu/api/publication/2393863},
	author = {Nyesténé Nagy, Teréz and Csordás, M and Kósa, Z and Góth, László},
	doi = {10.1016/j.abb.2012.01.004},
	journal-iso = {ARCH BIOCHEM BIOPHYS},
	journal = {ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS},
	volume = {525},
	unique-id = {2393863},
	issn = {0003-9861},
	abstract = {Catalase decreases the high, toxic concentrations of hydrogen peroxide but it lets the physiological, low concentrations in the cells mainly for signaling purposes. Its decreased activity may contribute to development of several pathological conditions. Catalase mutations occur frequently in exon 9, these were examined with different, complicated and costly methods. The aim of the current study was to evaluate a method for screening of polymorphisms in catalase exon 9. We used the slab gel electrophoresis of PCR amplicons without denaturation and silver staining for visualization of the DNA bands. We detected extra DNA bands in the 400-800 bp region of the catalase exon 9. Their single stranded nature was proved with nucleotide sequence analyses, comparison with the standard SSCP, staining with Sybr Green II and Sybr Green I, ethidium bromide, no digestion with RFLP (BstX I), and digestion with plant nuclease. We used this method for examination of polymorphisms of catalase exon 9 in microcytic anemia and beta-thalassemia patients. The lowest blood catalase activities were detected in microcytic anemia and beta-thalassemia patients with the TT genotypes of the C111T polymorphism. This method was sensitive for detection of G113A acatalasemia mutation, but poorly detected C37T and G5A acatalasemia mutations. © 2012 Elsevier Inc. All rights reserved.},
	keywords = {Adult; Adolescent; Female; Middle Aged; Male; Humans; MUTATION; ARTICLE; Polymorphism, Genetic; human; Hungary; Genotype; restriction fragment length polymorphism; polymerase chain reaction; nucleotide sequence; genetic screening; genetic association; Polymorphism, Restriction Fragment Length; priority journal; major clinical study; gene mutation; controlled study; Sequence Analysis, DNA; sequence analysis; base pairing; enzyme activity; Exons; Models, Genetic; ANEMIA; Catalase; human tissue; gene sequence; exon; Polymorphism, Single-Stranded Conformational; BETA-THALASSEMIA; Silver Staining; single stranded DNA; gel electrophoresis; amplicon; DNA polymorphism; single strand conformation polymorphism; gene structure; microcytic anemia; nuclease; genetic procedures; beta thalassemia; DNA denaturation; molecular diagnosis; Ethidium bromide; SSCP; catalase deficiency; Acatalasemia; Catalase gene mutations screening},
	year = {2012},
	eissn = {1096-0384},
	pages = {201-206}
}

@article{MTMT:1993025,
	title = {Detection of a novel familial catalase mutation (Hungarian type D) and possible risk of inherited catalase deficiency for diabetes mellitus},
	url = {https://m2.mtmt.hu/api/publication/1993025},
	author = {Góth, László and Vitai, Márta and Rass, P and Sükei, E and Páy, Anikó},
	doi = {10.1002/elps.200410384},
	journal-iso = {ELECTROPHORESIS},
	journal = {ELECTROPHORESIS},
	volume = {26},
	unique-id = {1993025},
	issn = {0173-0835},
	abstract = {The enzyme catalase is the main regulator of hydrogen peroxide metabolism. Recentfindings suggest that a low concentration of hydrogen peroxide may act as a messengerin 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 syndromecausing
		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 (60.667.6MU/L) and six normocatalasemic (103.6623.5MU/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 atposition 11 in intron 2, and G?Tat 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 = {Female; Middle Aged; Male; Humans; MUTATION; ARTICLE; genetic polymorphism; human; diabetes mellitus; Hungary; polymerase chain reaction; Pedigree; amino acid substitution; risk assessment; gene mutation; sequence analysis; clinical article; enzyme activity; DNA Mutational Analysis; Spectrophotometry; Mass Screening; GENOME ANALYSIS; hydrogen peroxide; Diabetes Mellitus, Type 2; Catalase; enzyme blood level; gene identification; intron; Electrophoresis, Capillary; agar gel electrophoresis; mutational analysis; nucleic acid base substitution; steady state; DNA extraction; Acatalasia; catalase deficiency; Catalase mutation; Blood catalase activity},
	year = {2005},
	eissn = {1522-2683},
	pages = {1646-1649}
}

@article{MTMT:2539241,
	title = {Simple PCR heteroduplex, SSCP mutation screening methods for the detection of novel catalase mutations in Hungarian patients with type 2 diabetes mellitus},
	url = {https://m2.mtmt.hu/api/publication/2539241},
	author = {Vitai, Márta and Fatrai, S and Rass, P and Csordas, M and Tarnai, I},
	doi = {10.1515/CCLM.2005.230},
	journal-iso = {CLIN CHEM LAB MED},
	journal = {CLINICAL CHEMISTRY AND LABORATORY MEDICINE},
	volume = {43},
	unique-id = {2539241},
	issn = {1434-6621},
	abstract = {Background: The enzyme catalase is the main regulator of hydrogen peroxide metabolism. Deficiency of catalase may cause high concentrations of hydrogen peroxide and increase the risk of the development of pathologies for which oxidative stress is a contributing factor, for example, type 2 diabetes mellitus. Catalase deficiency has been reported to be associated with increased frequency of diabetes mellitus in a cohort of patients in Hungary. In this cohort, the majority of mutations in the catalase gene occur in exon 2. Methods: Type 2 diabetic patients (n = 308) were evaluated for mutations in intron 1 (81 bp), exon 2 (172 bp) and intron 2 (13 bp) of the catalase gene. Screening for mutations utilized PCR single-strand conformational polymorphism (SSCP) and PCR heteroduplex methods. Verification of detected mutations was by nucleotide sequence analysis. Results: A total of 11 catalase gene mutations were detected in the 308 subjects (3.57%, p < 0.001). Five of the 11 were at two previously reported mutation sites: exon 2 (79) G insertion and (138) GA insertion. Six of the 11 were at five previously unreported catalase mutation sites: intron 1 (60) G -> T; intron 2 (7) G -> A and (5) G -> C; exon 2 (96) T -> A; and exon 2 (135) T -> A. The novel missense mutations on exon 2 (96 and 135) are associated with 59% and 48% decreased catalase activity, respectively; the novel G -> C mutation on intron 2 (5) is associated with a 62% decrease in catalase activity. Mutations detected on intron 1 (60) and intron 2 (7) showed no change in catalase activity. The G -> C mutation on intron 2 (5) might be a splicing mutation. The two missense mutations on exon 2 (96) and (135) cause substitutions of amino acids 53 (Asp -> Glu) and 66 (Glu -> Cys) of the catalase protein. These are close to amino acids that are important for the binding of heme to catalase, 44 (Val) and 72-75 Arg, Val, Val, His). Changes in heme binding may be responsible for the activity losses. Conclusion: Mutations that cause decreased catalase activity may contribute to susceptibility to inherited type 2 diabetes mellitus. Exon 2 and neighboring introns of the catalase gene may be minor hot spots for type 2 diabetes mellitus susceptibility mutations.},
	keywords = {ERYTHROCYTES; MECHANISM; COMPLICATIONS; nucleotide sequence; HYDROGEN-PEROXIDE; Diabetes; JAPANESE; Catalase gene; INSERTION; Acatalasemia; common mutation; DEFICIENCIES; PCR-SSCP; PCR heteroduplex; Oxidative stress},
	year = {2005},
	eissn = {1437-4331},
	pages = {1346-1350}
}

@article{MTMT:25464008,
	title = {Aging in vertebrates, and the effect of caloric restriction: a mitochondrial free radical production-DNA damage mechanism?},
	url = {https://m2.mtmt.hu/api/publication/25464008},
	author = {Barja, G},
	doi = {10.1017/S1464793103006213},
	journal-iso = {BIOL REV},
	journal = {BIOLOGICAL REVIEWS},
	volume = {79},
	unique-id = {25464008},
	issn = {1464-7931},
	year = {2004},
	eissn = {1469-185X},
	pages = {235-251}
}

@article{MTMT:2506535,
	title = {Catalase enzyme mutations and their association with diseases},
	url = {https://m2.mtmt.hu/api/publication/2506535},
	author = {Góth, László and Rass, P and Páy, Anikó},
	doi = {10.2165/00066982-200408030-00001},
	journal-iso = {MOL DIAGN},
	journal = {MOLECULAR DIAGNOSIS},
	volume = {8},
	unique-id = {2506535},
	issn = {1084-8592},
	abstract = {Enzyme catalase seems to be the main regulator of hydrogen peroxide metabolism. Hydrogen peroxide at high concentrations is a toxic agent, while at low concentrations it appears to modulate some physiological processes such as signaling in cell proliferation, apoptosis, carbohydrate metabolism, and platelet activation. Benign catalase gene mutations of 5′ noncoding region (15) and intron 1 (4) have no effect on catalase activity and are not associated with disease. Catalase gene mutations have been detected in association with diabetes mellitus, hypertension, and vitiligo. Decreases in catalase activity in patients with tumors is more likely to be due to decreased enzyme synthesis rather than to catalase mutations. Acatalasemia, the inherited deficiency of catalase has been detected in 11 countries. Its clinical features might be oral gangrene, altered lipid, carbohydrate, homocysteine metabolism and the increased risk of diabetes mellitus. The Japanese, Swiss, and Hungarian types of acatalasemia display differences in biochemical and genetic aspects. However, there are only limited reports on the syndrome causing these mutations. These data show that acatalasemia may be a syndrome with clinical, biochemical, genetic characteristics rather than just a simple enzyme deficiency. © 2004 Adis Data Information BV. All rights reserved.},
	keywords = {Humans; MUTATION; APOPTOSIS; TUMOR; signal transduction; Polymorphism, Genetic; single nucleotide polymorphism; review; human; diabetes mellitus; risk factor; Genetic Predisposition to Disease; disease association; gene mutation; clinical feature; HYPERTENSION; cell proliferation; enzyme activity; lipid metabolism; hydrogen peroxide; gene insertion; carbohydrate metabolism; Catalase; symptom; intron; Alzheimer disease; Vitiligo; thrombocyte activation; gangrene; enzyme synthesis; amino acid metabolism; untranslated region; Acatalasia; catalase deficiency},
	year = {2004},
	pages = {141-149}
}

@article{MTMT:22160969,
	title = {Oxidative stress, human genetic variation, and disease},
	url = {https://m2.mtmt.hu/api/publication/22160969},
	author = {Forsberg, L and de Faire, U and Morgenstern, R},
	doi = {10.1006/abbi.2001.2295},
	journal-iso = {ARCH BIOCHEM BIOPHYS},
	journal = {ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS},
	volume = {389},
	unique-id = {22160969},
	issn = {0003-9861},
	year = {2001},
	eissn = {1096-0384},
	pages = {84-93}
}

@article{MTMT:2393883,
	title = {A new type of inherited catalase deficiencies: Its characterization and comparison to the Japanese and Swiss type of acatalasemia},
	url = {https://m2.mtmt.hu/api/publication/2393883},
	author = {Góth, László},
	doi = {10.1006/bcmd.2001.0415},
	journal-iso = {BLOOD CELL MOL DIS},
	journal = {BLOOD CELLS MOLECULES AND DISEASES},
	volume = {27},
	unique-id = {2393883},
	issn = {1079-9796},
	abstract = {Thirteen Hungarian families that exhibited inherited catalase deficiencies have been detected. Differences between the deficiencies reported from Hungary and the previously reported Swiss acatalasemia were characterized using biochemical analysis of the catalase proteins. Molecular biological methods were used to compare the previously reported types of catalase deficiencies in Japan and the Hungarian deficiencies. Three mutations (a GA insertion in exon 2, a G insertion in exon 2, and a T to G substitution in intron 7) are responsible for decreased catalase activity in 7 of the 13 Hungarian kindreds; the other 6 families have not yet been characterized. These are not the mutations observed in Japan. Changes in lipid and carbohydrate metabolism and the high incidence (12.7%) of diabetes mellitus in the Hungarian kindreds suggest that individuals with inherited catalase deficiency are at risk of atherosclerosis and diabetes mellitus. The Hungarian subjects were detected during screening of a large population for catalase activity; no overt disease state was associated with the deficiencies. We hypothesize that the increased risk of disease may be due to prolonged exposure to elevated levels of blood hydrogen peroxide due to the lack of normal removal of hydrogen peroxide by blood catalase. © 2001 Academic Press.},
	keywords = {Adult; Adolescent; Female; Middle Aged; Male; Humans; MUTATION; ATHEROSCLEROSIS; exposure; human; diabetes mellitus; Hungary; Incidence; genetic analysis; amino acid substitution; genetic screening; risk factor; genetic association; priority journal; major clinical study; gene mutation; controlled study; Japan; conference paper; enzyme activity; SWITZERLAND; hydrogen peroxide; ethnic group; gene insertion; carbohydrate metabolism; Catalase; blood level; intron; exon; Hungarian; Acatalasia; catalase deficiency; Acatalasemia; Hypocatalasemia},
	year = {2001},
	eissn = {1096-0961},
	pages = {512-517}
}

@article{MTMT:2393882,
	title = {A novel catalase mutation (a G insertion in exon 2) causes the type B of the Hungarian acatalasemia},
	url = {https://m2.mtmt.hu/api/publication/2393882},
	author = {Góth, László},
	doi = {10.1016/S0009-8981(01)00609-X},
	journal-iso = {CLIN CHIM ACTA},
	journal = {CLINICA CHIMICA ACTA},
	volume = {311},
	unique-id = {2393882},
	issn = {0009-8981},
	keywords = {Adult; Female; Middle Aged; Humans; SCHIZOPHRENIA; MUTATION; human; Hungary; polymerase chain reaction; nucleotide sequence; amino acid sequence; Pedigree; risk factor; priority journal; sequence analysis; case report; letter; enzyme activity; Exons; reverse transcriptase polymerase chain reaction; lipid metabolism; hydrogen peroxide; Diabetes; cholesterol; Catalase; low density lipoprotein cholesterol; enzyme blood level; exon; apolipoprotein B; non insulin dependent diabetes mellitus; Catalase gene; heteroduplex; Acatalasia; catalase deficiency; Hypocatalasemia; Blood catalase},
	year = {2001},
	eissn = {1873-3492},
	pages = {161-163}
}

@article{MTMT:2875875,
	title = {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},
	url = {https://m2.mtmt.hu/api/publication/2875875},
	author = {Góth, László and Rass, P and Madarasi, I},
	doi = {10.1002/1522-2683(200101)22:1<49::AID-ELPS49>3.0.CO;2-W},
	journal-iso = {ELECTROPHORESIS},
	journal = {ELECTROPHORESIS},
	volume = {22},
	unique-id = {2875875},
	issn = {0173-0835},
	abstract = {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.},
	keywords = {Female; Male; Humans; MUTATION; ARTICLE; INTRONS; human; Hungary; polymerase chain reaction; nucleotide sequence; Pedigree; genetic screening; immunoblotting; gene mutation; Sequence Analysis, DNA; sequence analysis; Blotting, Western; Exons; protein blood level; Catalase; intron; exon; Polymorphism, Single-Stranded Conformational; familial disease; single strand conformation polymorphism; nucleic acid base substitution; Acatalasia; catalase deficiency; Hungarian acatalasemia; Splicing mutation; Single-strand conformation polymorphism},
	year = {2001},
	eissn = {1522-2683},
	pages = {49-51}
}