Overexpression of wild-type and nuclear-targeted catalase modulates resistance to oxidative stress but does not alter spontaneous mutant frequencies at APRT

Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis

Volumn 449, Issue 1-2, 2000, Pages 21-31

  Schriner, Samuel E ^a   Smith, Annette C ^a   Dang, Ngocthao H ^a   Fukuchi, Ken Ichiro ^b   Martin, George M ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

^b UNIVERSITY OF ALABAMA SCHOOL OF MEDICINE   (United States)

Author keywords

Catalase; Mutant frequency; Oxidative stress; P19

Indexed keywords

ADENINE PHOSPHORIBOSYLTRANSFERASE; BLEOMYCIN; CATALASE; HYDROGEN PEROXIDE; HYDROXYL RADICAL; MUTANT PROTEIN;

ARTICLE; CELL PROTECTION; CHEMOSENSITIVITY; CONTROLLED STUDY; DNA DAMAGE; GENE FREQUENCY; GENE MUTATION; HUMAN; HUMAN CELL; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN EXPRESSION;

ADENINE PHOSPHORIBOSYLTRANSFERASE; BLEOMYCIN; CATALASE; CELL NUCLEUS; CELLS, CULTURED; DNA DAMAGE; HUMANS; MUTATION; OXIDATIVE STRESS; TRANSGENES;

ANIMALIA; MURINAE;

EID: 0034599492     PISSN: 00275107     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0027-5107(00)00011-7     Document Type: Article

References (28)

1. Chance B., Sies H., Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59:1979;527-605.
2. Beckmann K.B., Ames B.N. The free radical theory of aging matures. Physiol. Rev. 78:1998;547-581.
3. Halliwell B., Gutteridge J.M.C. Free Radicals in Biology and Medicine. 1989;Oxford Univ. Press, Oxford.
4. Harman D. Aging: a theory based on free radical and radiation chemistry. J. Gerontol. 2:1956;298-300.
5. Cerutti P.A. Prooxidant states and tumor promotion. Science. 227:1985;375-381.
6. Aruoma O.I., Halliwell B., Dizdaroglu M. Damage to the bases in DNA induced by hydrogen peroxide and ferric iron chelates. J. Biol. Chem. 264:1989;20509-20512.
7. Cantoni O., Cattabeni F., Stocchi V., Meyn R.E., Cerutti P., Murray D. Hydrogen peroxide insult in cultured mammalian cells: relationships between DNA single-strand breakage, poly(ADP-ribose) metabolism and cell killing. Biochim. Biophys. Acta. 1014:1989;1-7.
8. Ziegler-Skylakakis K., Andrae U. Mutagenicity of hydrogen peroxide in V79 Chinese hamster cells. Mutat. Res. 192:1987;65-67.
9. Martin G.M., Hoehn H., Bryant E.M. Evidence against somatic mutation as a mechanism of clonal senescence. Adv. Exp. Med. Biol. 129:1980;139-143.
10. Martin G.M., Smith A.C., Ketterer D.J., Ogburn C.E., Disteche C.M. Increased chromosomal aberrations in first metaphases of cells isolated from the kidneys of aged mice. Isr. J. Med. Sci. 21:1985;296-301.
11. Martin G.M., Fry M., Loeb L.A. Somatic mutation and aging in mammalian cells. Sohal R.S., Birnbaum L.S., Cutler R.G. Molecular Biology of Aging: Gene Stability and Gene Expression. 1985;7-21 Raven Press, New York.
12. Fukuchi K.-I., Martin G.M., Monnat R.J. The mutator phenotype of Werner syndrome is characterized by extensive deletions. Proc. Natl. Acad. Sci. 86:1989;5893-5897.
13. Martin G.M., Ogburn C.E., Colgin L.M., Edland S., Monnat R.J. Somatic mutations are frequent and increase with age in human kidney epithelial cells. Hum. Mol. Genet. 5:1996;49-59.
14. Yu C.E., Oshima J., Fu Y.H., Wijsman E.M., Hisima F., Alisch R., Matthews S.F., Nakura J., Miki T., Ouais S., Martin G.M., Mulligan J., Schellenberg G.D. Positional cloning of the Werner's syndrome gene. Science. 272:1996;258-262.
15. Reimer D.L., Bailley J., Singh S.M. Complete cDNA and 5′ genomic sequences and multilevel regulation of the mouse catalase gene. Genomics. 21:1994;325-335.
16. Cooper G.E., DiMartino D.L., Turker M.S. Molecular analysis of APRT deficiency in mouse P19 teratocarcinoma stem cell line. Somat. Cell Mol. Genet. 17:1991;105-116.
17. Speranza M.J., Bagley A.C., Lynch R.E. Cells enriched for catalase are sensitized to the toxicities of bleomycin, adriamycin, and paraquat. J. Biol. Chem. 268:1993;19039-19043.
18. Makkerh J.P.S., Dingwall C., Laskey R.A. Comparative mutagenesis of nuclear localization signals reveals the importance of neutral and acidic amino acids. Curr. Biol. 6:1996;1025-1027.
19. Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning: A Laboratory Manual. 1989;Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
20. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
21. Ausubel F.M., Brent R., Kingston R.E., Moore D.D., Seidman J.G., Smith J.A., Struhl K. Current Protocols in Molecular Biology. 1994;Wiley.
22. Harlow E., Lane D. Antibodies: A Laboratory Manual. 1988;Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
23. Yasmineh W.G., Chung M., Caspers J.I. Determination of catalase activity on a centrifugal analyzer by an NADP/NADPH coupled enzyme reaction system. Clin. Biochem. 25:1992;21-27.
24. Schisler N.J., Singh S.M. A quantitative genetic analysis of tissue-specific catalase activity in Mus musculus. Biochem. Genet. 29:1991;65-89.
25. Cortes F., Dominguez I., Sandstrom B. Exogenous catalase introduced into CHO cells by electroporation does not protect against chromosome damage induced by ionizing radiation. Cell Biol. Int. 18:1994;959-965.
26. Hepel L.A., Porterfield V.T. Metabolism of inorganic nitrite and nitrate esters. J. Biol. Chem. 178:1949;549-556.
27. Chance B., Oshino N. Kinetics and mechanisms of catalase of the mitochondrial fraction. Biochem. J. 122:1971;225-233.
28. Turker M., Walker K.A., Jennings C.D., Mellon I., Yusufji A., Urano M. Spontaneous and ionizing radiation induced mutations involve large events when selecting for loss of an autosomal locus. Mutat. Res. 329:1995;97-105.