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Catalase enzyme mutations and their association with diseases

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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.

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Acknowledgements

This work was supported with grants of the Zsigmond Diabetes Foundation (Hungarian Academy of Science, Budapest) and the Hungarian Scientific Research Fund (OTKA T042985).

The authors have provided no information on sources of funding or on conflicts of interest directly relevant to the content of this review.

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Authors and Affiliations

  1. Department of Clinical Analytical Chemistry, Medical and Health Science Center, University of Debrecen, Debrecen, Hungary

    László Góth

  2. Department of Clinical Biochemistry and Molecular Pathology, Medical and Health Science Center, University of Debrecen, Debrecen, PO Box 40, H-4012, Hungary

    László Góth

  3. Sigma-Aldrich Ltd, Budapest, Hungary

    Péter Rass

  4. Biological Research Center, Hungarian Academy of Science, Szeged, Hungary

    Anikó Páy

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  1. László Góth
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Góth, L., Rass, P. & Páy, A. Catalase enzyme mutations and their association with diseases. CNS Drugs 8, 141–149 (2004). https://doi.org/10.1007/BF03260057

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