Residual Catalase in Japanese Type Acatalasemia

Ogata, Masana; Mizugaki, Junko

doi:10.1247/csf.3.279

Cited by 6 publications

(6 citation statements)

References 26 publications

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“…The mean blood catalase activity levels and the standard deviation were 3,380 + 180 Pu/g Hb for five normal Japanese individuals, 1,520 _+ 350 Pu/g Hb for four hypocatalasemic cases, and 5.5 _+ 0.8 Pu/g Hb (0.16% of normal activity) for five acatalasemic cases (Ogata et al 1972;Ogata and Mizugaki 1978). There is no overlap of catalase activity in the normal, hypocatalasemic, and acatalasemic groups.…”

Section: Residual Catalase Activity In Bloodmentioning

confidence: 87%

“…Acatalasemics without Takahara's disease, have higher residual catalase activity than those with Takahara's disease (Ogata and Mizugaki 1978). Acatalasemic patients do not totally lack blood cell catalase.…”

Section: Physiological Role Of Catalasementioning

confidence: 89%

“…Acatalasemic patients do not totally lack blood cell catalase. In addition, low but significantly elevated levels of glutathione peroxidase are found in Japanese acatalasemic blood (Ogata et al 1977b;Ogata and Mizugaki 1978), and this enzyme also decomposes hydrogen peroxide in the erythrocytes of acatalasemic patients and thus prevents methemoglobin formation (Ogata et al 1975). Acatalasemics without Takahara's disease, have higher residual catalase activity than those with Takahara's disease (Ogata and Mizugaki 1978).…”

Section: Physiological Role Of Catalasementioning

confidence: 99%

“…Acatalasemia was first believed to be a molecular disease specific to some oriental races, but in 1960 acatalasemia was also found in Switzerland (Aebi et al 1961), and thereafter in Israel (Szeinberg et al 1963), the United States (Taylor and Haut 1967), and Peru (Delgado and Calderon 1979). Studies on the residual catalase suggest that acatalasemia is not caused by a defect in the structural gene (Ogata et al 1972;Ogata and Mizugaki 1978). The molecular defect in the catalase gene in acatalasemia is described in relation to the residual catalase.…”

Section: Introductionmentioning

confidence: 98%

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Acatalasemia

Ogata

1991

Hum Genet

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The abnormalities in acatalasemia at the gene level as well as properties of the residual catalase in Japanese acatalasemia are historically reviewed. The replacement of the fifth nucleic acid, guanine, in the fourth intron by adenine in the acatalasemic gene causes a splicing mutation and hence a deficiency of mRNA. The guanine-to-adenine substitution was detected in two Japanese acatalasemic cases from different families. The properties of the residual catalase are similar to those of normal catalase; the exons are identical. The properties of the residual catalase and the molecular defect in the catalase gene are compared among Japanese, Swiss, and mouse acatalasemias. The physiological role of catalase, as judged from human acatalasemic blood and acatalasemic mice, is also described.

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Section: Residual Catalase Activity In Bloodmentioning

confidence: 87%

Section: Physiological Role Of Catalasementioning

confidence: 89%

Section: Physiological Role Of Catalasementioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

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Acatalasemia

Ogata

1991

Hum Genet

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“…The physiologic role of catalase is to prevent the accumulation of melhemoglobin and to decompose hydrogen peroxide, a toxic by-product of metabolism (Deisseroth and Dounce, 1970). Acatalasemia is an autosomal recessive disease characterized by very low levels of red blood cell catalase activity, and, rarely, by oral gangrene (Ogata and Mizugaki, 1979). Low levels of catalase have also been reported in a number of Wilms tumor patients (Junien et al, 1980(Junien et al, , 1983van Heyningcn et al, 1985).…”

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confidence: 99%

Localization of the human catalase and apolipoprotein A-I genes to chromosome 11

Schroeder¹,

Saunders²

1987

Cytogenet Genome Res

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Studies of the catalase and apolipoprotein A-I genes are pertinent to the understanding of human disease. Not only are these genes involved in acatalasemia and atherosclerosis, respectively, but they are also important gene markers for chromosome 11, deletions of which are involved in the development of Wilms tumor. We have used in situ hybridization to localize these genes to specific bands on chromosome 11. Hybridization with a catalase cDNA yielded a significant number of cells (38%) exhibiting label at band 1 lpl3. A high percentage of metaphase cells (50%) hybridized with a human genomic fragment containing the gene for apolipoprotein A-I displayed labeling at 11q13.

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Heterogeneity of erythrocyte catalase in Japanese-type acatalasemia by electrofocusing

Ogata

Mizugaki

1982

Biochem Genet

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Residual Catalase in Japanese Type Acatalasemia

Cited by 6 publications

References 26 publications

Acatalasemia

Acatalasemia

Localization of the human catalase and apolipoprotein A-I genes to chromosome 11

Heterogeneity of erythrocyte catalase in Japanese-type acatalasemia by electrofocusing

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