CAT (CAT)

catalase /11p13
Previous Symbols:
Synomyms:
Entrez Gene: 847
Uniprot: P04040
HUGO Accession: HGNC:1516

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  • OMIM (Online Mendellian Inheritance in Man)

    OMIM: 115500
    DESCRIPTION

    Catalase (EC 1.11.1.6) catalyzes the decomposition of hydrogen peroxide to oxygen and water. Mammalian catalase of approximately 240 kD occurs as a complex of 4 identical subunits, each of which contains 526 amino acid residues (summary by Ogata, 1991; Ogata et al., 2008).

    CLONING

    Bell et al. (1986) gave the cDNA sequence for human kidney catalase. The coding region had 1,581 basepairs.

    GENE STRUCTURE

    Quan et al. (1986) found that the CAT gene is 34 kb long and split into 13 exons.

    MAPPING

    Wieacker et al. (1980) assigned a gene for catalase to 11p by study of man-mouse cell hybrid clones. In the hybrid cells, detection of human catalase was precluded by the complexity of the electrophoretic patterns resulting from interference by a catalase-modifying enzyme activity. Therefore, a specific antihuman antibody was used in conjunction with electrophoresis. In mouse, catalase is not syntenic to the beta-globin cluster or to LDH-A.

    Niikawa et al. (1982) confirmed the close linkage of catalase to the gene of the WAGR complex (see 194070) by demonstrating low levels of catalase activity in the erythrocytes of 2 unrelated patients with the WAGR syndrome and small deletions in 11p. From the study of dosage in 2 unrelated patients with an interstitial deletion involving 11p13, Narahara et al. (1984) concluded that both the catalase locus and the WAGR locus are situated in the chromosome segment 11p1306-p1305, with catalase distal to WAGR.

    By classic linkage studies using RFLPs of the several genes as markers, Kittur et al. (1985) derived the following sequence of loci: cen--CAT--16 cM--CALC--8 cM--PTH--pter, with the interval between CAT and PTH estimated at 26 cM.

    CYTOGENETICS

    Junien et al. (1980) investigated catalase gene dosage effects in a case of 11p13 deletion, a case of trisomy of all of 11p except 11p13, and a case of trisomy 11p13. The results were consistent with assignment of the catalase locus to 11p13 and its linkage with the WAGR complex (194070). Assay of catalase activity should be useful in identifying those cases of presumed new mutation aniridia that have a risk of Wilms tumor or gonadoblastoma, even in the absence of visible chromosomal deletion. In karyotypically normal patients with aniridia, Wilms tumor, or the combination of the 2, Ferrell and Riccardi (1981) found normal catalase levels.

    BIOCHEMICAL FEATURES

    Several rare electrophoretic variants of red cell catalase were identified by Baur (1963). Nance et al. (1968) also described electrophoretic variants.

    Kenney et al. (2005) found that keratoconus (see 148300) corneas exhibited a 2.20-fold increase in catalase mRNA and 1.8-fold increase in enzyme activity. They concluded that elevated levels of cathepsins V/L2, B (116810), and G (116830) in keratoconus corneas could stimulate hydrogen peroxide production which, in turn, could upregulate catalase, an antioxidant enzyme. These and other findings supported the hypothesis that keratoconus corneas undergo oxidative stress and tissue degradation.

    Shibata et al. (1967) found that an immunologically reactive but enzymatically inactive protein about one-sixth the size of active catalase is present in red cells of patients with acatalasemia (614097).

    MOLECULAR GENETICS

    Data on gene frequencies of allelic variants were tabulated by Roychoudhury and Nei (1988).

    - Acatalasemia

    In Japanese patients with acatalasemia (614097), Wen et al. (1990) identified a homozygous splice site mutation in the CAT gene (115500.0001).

    Goth and Eaton (2000) reported an increased frequency of diabetes in catalase-deficient (hypo/acatalasemic) Hungarian patients as compared with unaffected first-degree relatives and the general Hungarian population. The authors speculated that quantitative deficiency of catalase might predispose to cumulative oxidant damage of pancreatic beta-cells and resulting diabetes.

    - Aniridia

    Boyd et al. (1986) described a catalase RFLP with 2 different enzymes and used these polymorphisms to exclude deletion of the catalase gene in patients with sporadic aniridia, including one who was known to have a deletion and another suspected of having a deletion.

    Mannens et al. (1987) found deletion of the catalase locus in 6 of 9 patients with aniridia (AN2; 106210). One of these catalase-deficient aniridia patients had a normal karyotype. No catalase deletion could be demonstrated in 7 Wilms tumors.

    - Hypertension

    Jiang et al. (2001) found an association between essential hypertension defined as elevation of systolic blood pressure and a single-nucleotide polymorphism (SNP) located 844 bp upstream of the start codon of the CAT gene. The TT phenotype was associated with higher blood pressure than the CC phenotype and CT was intermediate.

    ANIMAL MODEL

    In the acatalasemic mouse, Shaffer and Preston (1990) demonstrated that a CAG (glutamine)-to-CAT (histidine) transversion in the third position of codon 11 was responsible for the deficiency.

    To determine the role of reactive oxygen species in mammalian longevity, Schriner et al. (2005) generated transgenic mice that overexpressed human catalase localized to the peroxisome, the nucleus, or mitochondria. Median and maximum life spans were maximally increased (average of 5 months and 5.5 months, respectively) in the mitochondrial catalase-expressing animals. Cardiac pathology and cataract development were delayed, oxidative damage was reduced, peroxide production and peroxide-induced aconitase inactivation were attenuated, and the development of mitochondrial deletions was reduced. Schriner et al. (2005) concluded that their results support the free radical theory of aging and reinforce the importance of mitochondria as a source of these radicals. Inheritance
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REFERENCES
  1. Agar, N. S.; Sadrzadeh, S. M. H.; Hallaway, P. E.; Eaton, J. W.
    Erythrocyte catalase: a somatic oxidant defense?
    J. Clin. Invest. 77 319-321 (1986)
  2. Baur, E. W.
    Catalase abnormality in a Caucasian family in the United States.
    Science 140 816-817 (1963)
  3. Bell, G. I.; Najarian, R. C.; Mullenbach, G. T.; Hallewell, R. A.
    cDNA sequence coding for human kidney catalase.
    Nucleic Acids Res. 14 5561-5562 (1986)
  4. Boyd, P.; van Heyningen, V.; Seawright, A.; Fekete, G.; Hastie, N.
    Use of catalase polymorphisms in the study of sporadic aniridia.
    Hum. Genet. 73 171-174 (1986)
  5. Feinstein, R. N.; Howard, J. B.; Braun, J. T.; Seaholm, J. E.
    Acatalasemic and hypocatalasemic mouse mutants.
    Genetics 53 923-933 (1966)
  6. Ferrell, R. E.; Riccardi, V. M.
    Catalase levels in patients with aniridia and-or Wilms' tumor: utility and limitations.
    Cytogenet. Cell Genet. 31 120-123 (1981)
  7. Goth, L.; Eaton, J. W.
    Hereditary catalase deficiencies and increased risk of diabetes.
    Lancet 356 1820-1821 (2000)
  8. Goth, L.; Shemirani, A.; Kalmar, T.
    A novel catalase mutation (a GA insertion) causes the Hungarian type of acatalasemia.
    Blood Cells Molec. Dis. 26 151-154 (2000)
  9. Hirono, A.; Sasaya-Hamada, F.; Kanno, H.; Fujii, H.; Yoshida, T.; Miwa, S.
    A novel human catalase mutation (358T-del) causing Japanese-type acatalasemia.
    Blood Cells Molec. Dis. 21 232-234 (1995)
  10. Jiang, Z.; Akey, J. M.; Shi, J.; Xiong, M.; Wang, Y.; Shen, Y.; Xu, X.; Chen, H.; Wu, H.; Xiao, J.; Lu, D.; Huang, W.; Jin, L.
    A polymorphism in the promoter region of catalase is associated with blood pressure levels.
    Hum. Genet. 109 95-98 (2001)
  11. Junien, C.; Turleau, C.; de Grouchy, J.; Said, R.; Rethore, M.-O.; Tenconi, R.; Dufier, J. L.
    Regional assignment of catalase (CAT) gene to band 11p13: association with the aniridia-Wilms' tumor-gonadoblastoma (WAGR) complex.
    Ann. Genet. 23 165-168 (1980)
  12. Kenney, M. C.; Chwa, M.; Atilano, S. R.; Tran, A.; Carballo, M.; Saghizadeh, M.; Vasiliou, V.; Adachi, W.; Brown, D. J.
    Increased levels of catalase and cathepsin V/L2 but decreased TIMP-1 in keratoconus corneas: evidence that oxidative stress plays an role in this disorder.
    Invest. Ophthal. Vis. Sci. 46 823-832 (2005)
  13. Kidd, J. R.; Castiglione, C. M.; Pakstis, A. J.; Kidd, K. K.
    The anonymous RFLP locus D11S16 is tightly linked to catalase on 11p.
    Cytogenet. Cell Genet. 45 63-64 (1987)
  14. Kishimoto, Y.; Murakami, Y.; Hayashi, K.; Takahara, S.; Sugimura, T.; Sekiya, T.
    Detection of a common mutation of the catalase gene in Japanese acatalasemic patients.
    Hum. Genet. 88 487-490 (1992)
  15. Kittur, S. D.; Hoppener, J. W. M.; Antonarakis, S. E.; Daniels, J. D. J.; Meyers, D. A.; Maestri, N. E.; Jansen, M.; Korneluk, R. G.; Nelkin, B. D.; Kazazian, H. H., Jr.
    Linkage map of the short arm of human chromosome 11: location of the genes for catalase calcitonin, and insulin-like growth factor II.
    Proc. Nat. Acad. Sci. 82 5064-5067 (1985)
  16. Mannens, M.; Slater, R. M.; Heyting, C.; Bliek, J.; Hoovers, J.; Bleeker-Wagemakers, E. M.; Voute, P. A.; Coad, N.; Frants, R. R.; Pearson, P. L.
    Chromosome 11, Wilms' tumour and associated congenital diseases.
    (Abstract) Cytogenet. Cell Genet. 46 655 (1987)
  17. Nance, W. E.; Empson, J. E.; Bennett, T. W.; Larson, L.
    Haptoglobin and catalase loci in man: possible genetic linkage.
    Science 160 1230-1231 (1968)
  18. Narahara, K.; Kikkawa, K.; Kimira, S.; Kimoto, H.; Ogata, M.; Kasai, R.; Hamawaki, M.; Matsuoka, K.
    Regional mapping of catalase and Wilms tumor--aniridia, genitourinary abnormalities, and mental retardation triad loci to the chromosome segment 11p1305-p1306.
    Hum. Genet. 66 181-185 (1984)
  19. Niikawa, N.; Fukushima, Y.; Taniguchi, N.; Iizuka, S.; Kajii, T.
    Chromosome abnormalities involving 11p13 and low erythrocyte catalase activity.
    Hum. Genet. 60 373-375 (1982)
  20. Ogata, M.
    Acatalasemia.
    Hum. Genet. 86 331-340 (1991)
  21. Ogata, M.; Wang, D.-H.; Ogino, K.
    Mammalian acatalasemia: the perspectives of bioinformatics and genetic toxicology.
    Acta Med. Okayama 62 345-361 (2008)
  22. Quan, F.; Korneluk, R. G.; MacLeod, H. L.; Tsui, L. C.; Gravel, R. A.
    An RFLP associated with the human catalase gene.
    Nucleic Acids Res. 13 8288 (1985)
  23. Quan, F.; Korneluk, R. G.; Tropak, M. B.; Gravel, R. A.
    Isolation and characterization of the human catalase gene.
    Nucleic Acids Res. 14 5321-5335 (1986)
  24. Roychoudhury, A. K.; Nei, M.
    Human Polymorphic Genes: World Distribution.
    New York: Oxford Univ. Press (pub.) 1988.
  25. Schriner, S. E.; Linford, N. J.; Martin, G. M.; Treuting, P.; Ogburn, C. E.; Emond, M.; Coskun, P. E.; Ladiges, W.; Wolf, N.; Van Remmen, H.; Wallace, D. C.; Rabinovitch, P. S.
    Extension of murine life span by overexpression of catalase targeted to mitochondria.
    Science 308 1909-1911 (2005)
  26. Schroeder, W. T.; Saunders, G. F.
    Localization of the human catalase and apolipoprotein A-I genes to chromosome 11.
    Cytogenet. Cell Genet. 44 231-233 (1987)
  27. Shaffer, J. B.; Preston, K. E.
    Molecular analysis of an acatalasemic mouse mutant.
    Biochem. Biophys. Res. Commun. 173 1043-1050 (1990)
  28. Shibata, Y.; Higashi, T.; Hirai, H.; Hamilton, H. B.
    Immunochemical studies on catalase.
    II. An anticatalase reacting component in normal hypocatalasic, and acatalasic human erythrocytes. Arch. Biochem. 118 200-209 (1967)
  29. Wen, J. K.; Osumi, T.; Hashimoto, T.; Ogata, M.
    Molecular analysis of human acatalasemia: identification of a splicing mutation.
    J. Molec. Biol. 211 383-393 (1990)
  30. Wieacker, P.; Mueller, C. R.; Mayerova, A.; Grzeschik, K. H.; Ropers, H. H.
    Assignment of the gene coding for human catalase to the short arm of chromosome 11.
    Ann. Genet. 23 73-77 (1980)
OMIM and Online Mendelian Inheritance in Man are registered trademarks of the Johns Hopkins University. Copyright 1966-2011 Johns Hopkins University.



HPRD (Human Protein Reference Database)

Proteins Linked to CAT Gene: 4