The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

CAT  -  catalase

Bos taurus

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of MGC128112

  • Immunoblot analysis indicated that neither hypoxia alone nor reoxygenation changed CuZn superoxide dismutase (SOD), MnSOD, and catalase levels [1].
  • A heme d prosthetic group with the configuration of a cis-hydroxychlorin gamma-spirolactone has been found in the crystal structures of Penicillium vitale catalase and Escherichia coli catalase hydroperoxidase II (HPII) [2].
  • In addition, phorbol myristate acetate (PMA) and normal neutrophils, but not O2 metabolite deficient neutrophils from patients with chronic granulomatous disease (CGD), caused DMTU disappearance in vitro which was decreased by simultaneous addition of catalase, but not SOD, sodium benzoate or DMSO [3].
  • Furthermore, s.c. injection of catalase also greatly inhibited metastasis (11 +/- 6, p < 0.001) [4].
  • Accordingly, different antioxidants, including catalase, vitamin E, Mn(IIItetrakis(4-benzoic acid)porphyrin chloride (MnTBAP) or ascorbic acid, provided protection against 6-OHDA-induced toxicity [5].
 

Psychiatry related information on MGC128112

  • The singlet oxygen-mediated damage to SOD and catalase may result in the perturbation of cellular antioxidant defense mechanisms and subsequently lead to a pro-oxidant condition [6].
 

High impact information on MGC128112

  • In addition, bovine catalase uses unbound NAD(P)H to prevent substrate inactivation without displacing catalase-bound NADP(+) [7].
  • H2O2 degradation occurred via the glutathione redox cycle and catalase [8].
  • Catalase, which is involved in the degradation of H(2)O(2) into water and oxygen, is the major H(2)O(2)-scavenging enzyme in all aerobic organisms [9].
  • When NO was generated by 3-morpholinosydnonimine hydrochloride in the presence of SOD, NO- or a similar reductant was formed, which reduced catalase compound II and promoted the formation of the catalase [Fe(III)]-NO complex [10].
  • Both superoxide dismutase and catalase totally abolish this radical signal, suggesting that O2 is sequentially reduced from O2-. to H2O2 to OH.. Addition of ethanol resulted in trapping of the ethoxy radical, further confirming the generation of OH.. Endothelial radical generation was shown to cause cell death, as evidenced by trypan blue uptake [11].
 

Chemical compound and disease context of MGC128112

  • Antioxidants, including bovine liver catalase, bovine erythrocyte CuZn-SOD, sodium selenite and Trolox, a water soluble vitamin E analogue, as well as hypoxia, inhibited dexamethasone-induced apoptosis [12].
  • Neither inactivated catalase nor BSA showed any effects on the number of metastatic colonies, indicating that the enzymatic activity of catalase to detoxify H(2)O(2) is the critical factor inhibiting metastasis [4].
  • NADPH binding and control of catalase compound II formation: comparison of bovine, yeast, and Escherichia coli enzymes [13].
  • The catalase level of Bacteroides distasonis (ATCC 8503, type strain) varied with the amount of hemin supplied to the medium when the cells were grown in either a prereduced medium containing 0.5% peptone, 0.5% yeast extract, and 1% glucose or in a prereduced, defined heme-deficient medium [14].
  • METHODS: Bovine aortic EC cultures were exposed to 2 hours of normoxia, then 1 hour of hypoxia (PO2 = 10 +/- 3.5 mm Hg), followed by 1.5 hours of reoxygenation in either normal medium or medium plus either superoxide dismutase (SOD, 300 units/ml), catalase (1200 units/ml), allopurinol (5.0 x 10(-4) mol/L), or dinitrophenol (10(-4) mol/L) [15].
 

Biological context of MGC128112

  • The amino acid sequence of beef liver catalase is known and contains (at least) 506 amino acid residues [16].
  • Catalase inhibited DBBF-Hb oxidation, the loss of thiols, and the onset of G2/M arrest and apoptosis [17].
  • Mechanisms of protection of catalase by NADPH. Kinetics and stoichiometry [18].
  • 2. Superoxide dismutase inhibited this lipid peroxidation, as did catalase, thus indicating that both O2- and H2O2 were essential intermediates [19].
  • The discovery that SA inhibits catalase from tobacco led us to suggest that H2O2 acts as second messenger to activate plant defenses [20].
 

Anatomical context of MGC128112

  • The complete amino acid sequence of bovine liver catalase and the partial sequence of bovine erythrocyte catalase [21].
  • Detection of catalase in rat heart mitochondria [22].
  • Monocyte-dependent death of freshly isolated T lymphocytes: induction by phorbolester and mitogens and differential effects of catalase [23].
  • The uptake and degradation of bovine serum albumin (BSA), bovine liver catalase, and rabbit muscle enolase have been studied in cultured mouse peritoneal macrophages (MPM) and baby hamster kidney fibroblasts (BHK cells) [24].
  • Incubation of eosinophils with azide that inhibits EPO, and catalase that degrades H2O2, significantly increased the amount of SRS activity detected in the extracellular medium after A23187 stimulation [25].
 

Associations of MGC128112 with chemical compounds

  • In contrast, beef liver catalase contains one bound NADP molecule per subunit in a position equivalent to the chain region, leading to the flavodoxin-like domain, of P. vitale catalase [16].
  • This strain-induced ERK activity was attenuated after ECs were treated with N-acetylcysteine or catalase [26].
  • Commercially produced bovine liver catalase, lactoperoxidase, HRP, and vitamin E all mimic the ability of the purified human protein to support neuronal survival in vitro [27].
  • In addition, the antitumor effect of the hypoxanthine and xanthine oxidase reaction was significantly inhibited by the administration of superoxide dismutase and catalase [28].
  • This product was also observed when 2,5-dimethylfuran was exposed to the xanthine oxidase system, in which case its accumulation was prevented by superoxide dismutase or by catalase, but not by scavengers of hydroxyl radical [19].
 

Other interactions of MGC128112

 

Analytical, diagnostic and therapeutic context of MGC128112

  • The growth mechanisms and physical properties of the orthorhombic crystal form of beef liver catalase were investigated using in situ atomic force microscopy (AFM) [34].
  • However, when TFIIIB was analyzed by gel filtration chromatography it was determined to have a Stokes radius of 53 A, eluting from this chromatography matrix near the position of catalase (Mr = 248,000) [35].
  • We have studied the time course of the absorption of bovine liver catalase after pulse radiolysis with oxygen saturation in the presence and absence of superoxide dismutase [36].
  • Mitochondrial fractionation studies and quantitative electron microscopic immunocytochemistry revealed that most catalase was matrix-associated [22].
  • The number of protons produced in the reaction was measured by "pH stat" titration and hydrogen peroxide production by the effect of the enzyme catalase on the measured stoichiometry [37].

References

  1. Reoxygenation of endothelial cells increases permeability by oxidant-dependent mechanisms. Lum, H., Barr, D.A., Shaffer, J.R., Gordon, R.J., Ezrin, A.M., Malik, A.B. Circ. Res. (1992) [Pubmed]
  2. Structure of the heme d of Penicillium vitale and Escherichia coli catalases. Murshudov, G.N., Grebenko, A.I., Barynin, V., Dauter, Z., Wilson, K.S., Vainshtein, B.K., Melik-Adamyan, W., Bravo, J., Ferrán, J.M., Ferrer, J.C., Switala, J., Loewen, P.C., Fita, I. J. Biol. Chem. (1996) [Pubmed]
  3. Dimethylthiourea prevents hydrogen peroxide and neutrophil mediated damage to lung endothelial cells in vitro and disappears in the process. Toth, K.M., Harlan, J.M., Beehler, C.J., Berger, E.M., Parker, N.B., Linas, S.L., Repine, J.E. Free Radic. Biol. Med. (1989) [Pubmed]
  4. Inhibition of experimental pulmonary metastasis by controlling biodistribution of catalase in mice. Nishikawa, M., Tamada, A., Kumai, H., Yamashita, F., Hashida, M. Int. J. Cancer (2002) [Pubmed]
  5. Chromaffin cell death induced by 6-hydroxydopamine is independent of mitochondrial swelling and caspase activation. Galindo, M.F., Jordán, J., González-García, C., Ceña, V. J. Neurochem. (2003) [Pubmed]
  6. Inactivation of catalase and superoxide dismutase by singlet oxygen derived from photoactivated dye. Kim, S.Y., Kwon, O.J., Park, J.W. Biochimie (2001) [Pubmed]
  7. Mammalian catalase: a venerable enzyme with new mysteries. Kirkman, H.N., Gaetani, G.F. Trends Biochem. Sci. (2007) [Pubmed]
  8. Neutrophil-endothelial cell interaction. Evidence for and mechanisms of the self-protection of bovine microvascular endothelial cells from hydrogen peroxide-induced oxidative stress. Dobrina, A., Patriarca, P. J. Clin. Invest. (1986) [Pubmed]
  9. Hydrogen peroxide homeostasis: activation of plant catalase by calcium/calmodulin. Yang, T., Poovaiah, B.W. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  10. Reversible conversion of nitroxyl anion to nitric oxide by superoxide dismutase. Murphy, M.E., Sies, H. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  11. Measurement of endothelial cell free radical generation: evidence for a central mechanism of free radical injury in postischemic tissues. Zweier, J.L., Kuppusamy, P., Lutty, G.A. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  12. Decreased antioxidant defence and increased oxidant stress during dexamethasone-induced apoptosis: bcl-2 prevents the loss of antioxidant enzyme activity. Baker, A.F., Briehl, M.M., Dorr, R., Powis, G. Cell Death Differ. (1996) [Pubmed]
  13. NADPH binding and control of catalase compound II formation: comparison of bovine, yeast, and Escherichia coli enzymes. Hillar, A., Nicholls, P., Switala, J., Loewen, P.C. Biochem. J. (1994) [Pubmed]
  14. Production and some properties of catalase and superoxide dismutase from the anaerobe Bacteroides distasonis. Gregory, E.M., Kowalski, J.B., Holdeman, L.V. J. Bacteriol. (1977) [Pubmed]
  15. Endogenous reactive oxygen metabolites mediate sublethal endothelial cell dysfunction during reoxygenation. Watkins, M.T., al-Badawi, H., Cardenas, R., Dubois, E., Larson, D.M. J. Vasc. Surg. (1996) [Pubmed]
  16. Comparison of beef liver and Penicillium vitale catalases. Melik-Adamyan, W.R., Barynin, V.V., Vagin, A.A., Borisov, V.V., Vainshtein, B.K., Fita, I., Murthy, M.R., Rossmann, M.G. J. Mol. Biol. (1986) [Pubmed]
  17. Redox cycling of diaspirin cross-linked hemoglobin induces G2/M arrest and apoptosis in cultured endothelial cells. D'Agnillo, F., Alayash, A.I. Blood (2001) [Pubmed]
  18. Mechanisms of protection of catalase by NADPH. Kinetics and stoichiometry. Kirkman, H.N., Rolfo, M., Ferraris, A.M., Gaetani, G.F. J. Biol. Chem. (1999) [Pubmed]
  19. Superoxide, hydrogen peroxide, and singlet oxygen in lipid peroxidation by a xanthine oxidase system. Kellogg, E.W., Fridovich, I. J. Biol. Chem. (1975) [Pubmed]
  20. Salicylic acid is a modulator of tobacco and mammalian catalases. Durner, J., Klessig, D.F. J. Biol. Chem. (1996) [Pubmed]
  21. The complete amino acid sequence of bovine liver catalase and the partial sequence of bovine erythrocyte catalase. Schroeder, W.A., Shelton, J.R., Shelton, J.B., Robberson, B., Apell, G., Fang, R.S., Bonaventura, J. Arch. Biochem. Biophys. (1982) [Pubmed]
  22. Detection of catalase in rat heart mitochondria. Radi, R., Turrens, J.F., Chang, L.Y., Bush, K.M., Crapo, J.D., Freeman, B.A. J. Biol. Chem. (1991) [Pubmed]
  23. Monocyte-dependent death of freshly isolated T lymphocytes: induction by phorbolester and mitogens and differential effects of catalase. Wesch, D., Marx, S., Kabelitz, D. J. Immunol. (1998) [Pubmed]
  24. Degradation and regurgitation of extracellular proteins by cultured mouse peritoneal macrophages and baby hamster kidney fibroblasts. Kinetic evidence that the transfer of proteins to lysosomes is not irreversible. Buktenica, S., Olenick, S.J., Salgia, R., Frankfater, A. J. Biol. Chem. (1987) [Pubmed]
  25. Eosinophil peroxidase-mediated inactivation of leukotrienes B4, C4, and D4. Henderson, W.R., Jörg, A., Klebanoff, S.J. J. Immunol. (1982) [Pubmed]
  26. Modulation of Ras/Raf/extracellular signal-regulated kinase pathway by reactive oxygen species is involved in cyclic strain-induced early growth response-1 gene expression in endothelial cells. Wung, B.S., Cheng, J.J., Chao, Y.J., Hsieh, H.J., Wang, D.L. Circ. Res. (1999) [Pubmed]
  27. Purification of a human red blood cell protein supporting the survival of cultured CNS neurons, and its identification as catalase. Walicke, P., Varon, S., Manthrope, M. J. Neurosci. (1986) [Pubmed]
  28. A novel cancer therapy based on oxygen radicals. Yoshikawa, T., Kokura, S., Tainaka, K., Naito, Y., Kondo, M. Cancer Res. (1995) [Pubmed]
  29. Demonstration of the ascorbate dependence of membrane-bound dopamine beta-monooxygenase in adrenal chromaffin granule ghosts. Herman, H.H., Wimalasena, K., Fowler, L.C., Beard, C.A., May, S.W. J. Biol. Chem. (1988) [Pubmed]
  30. Interaction of rhodanese with intermediates of oxygen reduction. Cannella, C., Berni, R. FEBS Lett. (1983) [Pubmed]
  31. Drug-induced changes in selenium-dependent glutathione peroxidase activity in the chick. Mercurio, S.D., Combs, G.F. J. Nutr. (1985) [Pubmed]
  32. The Adriamycin (doxorubicin)-induced inactivation of cytochrome c oxidase depends on the presence of iron or copper. Hasinoff, B.B., Davey, J.P., O'Brien, P.J. Xenobiotica (1989) [Pubmed]
  33. Fibrin membrane endowed with biological function. V. Multienzyme complex of uricase, catalase, allantoinase and allantoicase. Okamoto, H., Tipayang, P., Inada, Y. Biochim. Biophys. Acta (1980) [Pubmed]
  34. Structure of orthorhombic crystals of beef liver catalase. Ko, T.P., Day, J., Malkin, A.J., McPherson, A. Acta Crystallogr. D Biol. Crystallogr. (1999) [Pubmed]
  35. Properties of yeast class III gene transcription factor TFIIIB. Implications regarding mechanism of action. Klekamp, M.S., Weil, P.A. J. Biol. Chem. (1987) [Pubmed]
  36. The reaction of superoxide radical with catalase. Mechanism of the inhibition of catalase by superoxide radical. Shimizu, N., Kobayashi, K., Hayashi, K. J. Biol. Chem. (1984) [Pubmed]
  37. Iron oxidation chemistry in ferritin. Increasing Fe/O2 stoichiometry during core formation. Xu, B., Chasteen, N.D. J. Biol. Chem. (1991) [Pubmed]
 
WikiGenes - Universities