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. 2003 May;8(2):37-40.
doi: 10.1007/BF02897924.

Animal model for oxidative stress research-Catalase mutant mice

Da-Hong Wang  1 , Noriyoshi Masuoka, Shohei Kira
Affiliations

Animal model for oxidative stress research-Catalase mutant mice

Da-Hong Wang et al. Environ Health Prev Med. 2003 May.

Abstract

Catalase-deficient mouse strains was initially established by Feinstein et al. through a large scale screening of the progeny of irradiated C3H mice in 1966. Later, Feinstein provided the mice of catalase mutant strain C3H/AnICs(a)Cs(a) (wild-type), C3H/AnICs(b)Cs(b) and C3H/AnlCs(c)Cs(c) to Okayama University Medical School in Japan. It is known that a point mutation at amino acid 11 (from glutamine to histidine) of acatalasemic mouse catalase and a point mutation at amino acid 439 (from as paragine to serine) of hypocatalasemic mouse catalase are responsible for the catalase deficiency of acatalasemic and hypocatalasemic mice, respectively. Recently, a liver cell line from an acatalasemic mouse andEscherichia coli (E. coli) strains with murine normal, hypocatalasemic, or acatalasemic catalase have been established. The construction of these new systems would be useful for studying the effects of oxidative stress at the cellular level. In this review, we give a brief overview of recent findings of studies in utilizing the catalase-deficient mice and evaluate the possibility of these mouse strains as a candidate animal model for oxidative stress research.

Keywords: acatalasemia; catalase activity; catalase mutant mice; hydrogen peroxide; oxidative stress.

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References

    1. {'text': '', 'ref_index': 1, 'ids': [{'type': 'PubMed', 'value': '2066646', 'is_inner': True, 'url': 'https://pubmed.ncbi.nlm.nih.gov/2066646/'}]}
    2. Scott MD, Lubin BH, Zuo L, Kuypers FA. Erythrocyte defense against hydrogen peroxide: preeminent importance of catalase. J. Lab. Clin. Med. 1991; 118: 7–16. - PubMed
    1. {'text': '', 'ref_index': 1, 'ids': [{'type': 'DOI', 'value': '10.1016/0891-5849(90)90156-D', 'is_inner': False, 'url': 'https://doi.org/10.1016/0891-5849(90)90156-d'}, {'type': 'PubMed', 'value': '2193855', 'is_inner': True, 'url': 'https://pubmed.ncbi.nlm.nih.gov/2193855/'}]}
    2. Sun Y. Free radicals, antioxidant enzymes, and carcinogenesis. Free Radic. Biol. Med. 1990; 8: 583–599. - PubMed
    1. Aebi HE. Catalase. In: Bergmeyer HU, eds, Methods of enzymatic analysis, 3rd edn. Vol 7. VCH Verlagsgesellschatt mbH, 1985: 273–286.
    1. None
    2. Takahara S, Miyamoto H. Clinical and experimental studies on the odontogenous progressive necrotic ostitis due to lack of blood catalase. J. Otorhinol. Soc. Jpn. 1948; 51: 163–164.
    1. None
    2. Aebi HE, Wyss SR. Acatalasemia. In: Stanbury JB, Wyngaarden JB, Fredricson S, eds. 4th edn. The metabolic basis of inherited disease. New York: Megraw-Hill, 1978; 1792–1807.