메뉴 건너뛰기




Volumn 358, Issue 2, 2006, Pages 199-207

Measuring "free" iron levels in Caenorhabditis elegans using low-temperature Fe(III) electron paramagnetic resonance spectroscopy

Author keywords

"Free" iron; C. elegans; Iron EPR; Iron measurements; Oxidative stress; ROS measurements

Indexed keywords

ELECTRON RESONANCE; ELECTRON SPIN RESONANCE SPECTROSCOPY; ESCHERICHIA COLI; FREE RADICALS; OXIDATIVE STRESS; PARAMAGNETIC RESONANCE; PARAMAGNETISM; TEMPERATURE; YEAST;

EID: 33750027464     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2006.08.025     Document Type: Article
Times cited : (14)

References (36)
  • 1
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • Balaban R.S., Nemoto S., and Finkel T. Mitochondria, oxidants, and aging. Cell 120 (2005) 483-495
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 2
    • 0028587756 scopus 로고
    • Oxygen-derived species: Their relation to human disease and environmental stress
    • Halliwell B., and Cross C.E. Oxygen-derived species: Their relation to human disease and environmental stress. Environ. Health Perspect. 102 Suppl. 10 (1994) 5-12
    • (1994) Environ. Health Perspect. , vol.102 , Issue.SUPPL. 10 , pp. 5-12
    • Halliwell, B.1    Cross, C.E.2
  • 3
  • 4
    • 0031741551 scopus 로고    scopus 로고
    • Free radicals: Their history and current status in aging and disease
    • Knight J.A. Free radicals: Their history and current status in aging and disease. Ann. Clin. Lab. Sci. 28 (1998) 331-346
    • (1998) Ann. Clin. Lab. Sci. , vol.28 , pp. 331-346
    • Knight, J.A.1
  • 6
    • 0018263443 scopus 로고
    • The biology of oxygen radicals
    • Fridovich I. The biology of oxygen radicals. Science 201 (1978) 875-880
    • (1978) Science , vol.201 , pp. 875-880
    • Fridovich, I.1
  • 7
    • 0026679293 scopus 로고
    • Molecular genetics of superoxide dismutases in yeasts and related fungi
    • Gralla E.B., and Kosman D.J. Molecular genetics of superoxide dismutases in yeasts and related fungi. Adv. Genet. 30 (1992) 251-319
    • (1992) Adv. Genet. , vol.30 , pp. 251-319
    • Gralla, E.B.1    Kosman, D.J.2
  • 8
    • 0025938799 scopus 로고
    • Null mutants of Saccharomyces cerevisiae Cu,Zn superoxide dismutase: characterization and spontaneous mutation rates
    • Gralla E.B., and Valentine J.S. Null mutants of Saccharomyces cerevisiae Cu,Zn superoxide dismutase: characterization and spontaneous mutation rates. J. Bacteriol. 173 (1991) 5918-5920
    • (1991) J. Bacteriol. , vol.173 , pp. 5918-5920
    • Gralla, E.B.1    Valentine, J.S.2
  • 10
    • 0026011632 scopus 로고
    • Superoxide sensitivity of the Escherichia coli 6-phosphogluconate dehydratase
    • Gardner P.R., and Fridovich I. Superoxide sensitivity of the Escherichia coli 6-phosphogluconate dehydratase. J. Biol. Chem. 266 (1991) 1478-1483
    • (1991) J. Biol. Chem. , vol.266 , pp. 1478-1483
    • Gardner, P.R.1    Fridovich, I.2
  • 11
    • 0026045587 scopus 로고
    • Superoxide sensitivity of the Escherichia coli aconitase
    • Gardner P.R., and Fridovich I. Superoxide sensitivity of the Escherichia coli aconitase. J. Biol. Chem. 266 (1991) 19328-19333
    • (1991) J. Biol. Chem. , vol.266 , pp. 19328-19333
    • Gardner, P.R.1    Fridovich, I.2
  • 12
    • 0026806913 scopus 로고
    • Inactivation-reactivation of aconitase in Escherichia coli: a sensitive measure of superoxide radical
    • Gardner P.R., and Fridovich I. Inactivation-reactivation of aconitase in Escherichia coli: a sensitive measure of superoxide radical. J. Biol. Chem. 267 (1992) 8757-8763
    • (1992) J. Biol. Chem. , vol.267 , pp. 8757-8763
    • Gardner, P.R.1    Fridovich, I.2
  • 13
    • 0027289724 scopus 로고
    • NADPH inhibits transcription of the Escherichia coli manganese superoxide dismutase gene (sodA) in vitro
    • Gardner P.R., and Fridovich I. NADPH inhibits transcription of the Escherichia coli manganese superoxide dismutase gene (sodA) in vitro. J. Biol. Chem. 268 (1993) 12958-12963
    • (1993) J. Biol. Chem. , vol.268 , pp. 12958-12963
    • Gardner, P.R.1    Fridovich, I.2
  • 14
    • 0028266323 scopus 로고
    • Paraquat diaphorases in Escherichia coli
    • Liochev S.I., and Fridovich I. Paraquat diaphorases in Escherichia coli. Free Radic. Biol. Med. 16 (1994) 555-559
    • (1994) Free Radic. Biol. Med. , vol.16 , pp. 555-559
    • Liochev, S.I.1    Fridovich, I.2
  • 15
    • 0026594013 scopus 로고
    • Effects of overproduction of superoxide dismutases in Escherichia coli on inhibition of growth and on induction of glucose-6-phosphate dehydrogenase by paraquat
    • Liochev S.I., and Fridovich I. Effects of overproduction of superoxide dismutases in Escherichia coli on inhibition of growth and on induction of glucose-6-phosphate dehydrogenase by paraquat. Arch. Biochem. Biophys. 294 (1992) 138-143
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 138-143
    • Liochev, S.I.1    Fridovich, I.2
  • 16
    • 0027258954 scopus 로고
    • Modulation of the fumarases of Escherichia coli in response to oxidative stress
    • Liochev S.I., and Fridovich I. Modulation of the fumarases of Escherichia coli in response to oxidative stress. Arch. Biochem. Biophys. 301 (1993) 379-384
    • (1993) Arch. Biochem. Biophys. , vol.301 , pp. 379-384
    • Liochev, S.I.1    Fridovich, I.2
  • 17
    • 0027165156 scopus 로고
    • The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase
    • Flint D.H., Emptage M.H., Finnegan M.G., Fu W., and Johnson M.K. The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase. J. Biol. Chem. 268 (1993) 14732-14742
    • (1993) J. Biol. Chem. , vol.268 , pp. 14732-14742
    • Flint, D.H.1    Emptage, M.H.2    Finnegan, M.G.3    Fu, W.4    Johnson, M.K.5
  • 18
    • 0030857377 scopus 로고    scopus 로고
    • Iron homeostasis, oxidative stress, and DNA damage
    • Meneghini R. Iron homeostasis, oxidative stress, and DNA damage. Free Radic. Biol. Med. 23 (1997) 783-792
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 783-792
    • Meneghini, R.1
  • 19
    • 0028871420 scopus 로고
    • Superoxide and the production of oxidative DNA damage
    • Keyer K., Gort A.S., and Imlay J.A. Superoxide and the production of oxidative DNA damage. J. Bacteriol. 177 (1995) 6782-6790
    • (1995) J. Bacteriol. , vol.177 , pp. 6782-6790
    • Keyer, K.1    Gort, A.S.2    Imlay, J.A.3
  • 20
    • 0030465238 scopus 로고    scopus 로고
    • Superoxide accelerates DNA damage by elevating free-iron levels
    • Keyer K., and Imlay J.A. Superoxide accelerates DNA damage by elevating free-iron levels. Proc. Natl. Acad. Sci. USA 93 (1996) 13635-13640
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13635-13640
    • Keyer, K.1    Imlay, J.A.2
  • 21
    • 0034703101 scopus 로고    scopus 로고
    • Yeast lacking superoxide dismutase(s) show elevated levels of "free iron" as measured by whole cell electron paramagnetic resonance
    • Srinivasan C., Liba A., Imlay J.A., Valentine J.S., and Gralla E.B. Yeast lacking superoxide dismutase(s) show elevated levels of "free iron" as measured by whole cell electron paramagnetic resonance. J. Biol. Chem. 275 (2000) 29187-29192
    • (2000) J. Biol. Chem. , vol.275 , pp. 29187-29192
    • Srinivasan, C.1    Liba, A.2    Imlay, J.A.3    Valentine, J.S.4    Gralla, E.B.5
  • 22
    • 0036124216 scopus 로고    scopus 로고
    • Measurement of "free" or electron paramagnetic resonance-detectable iron in whole yeast cells as indicator of superoxide stress
    • Srinivasan C., and Gralla E.B. Measurement of "free" or electron paramagnetic resonance-detectable iron in whole yeast cells as indicator of superoxide stress. Methods Enzymol. 349 (2002) 173-180
    • (2002) Methods Enzymol. , vol.349 , pp. 173-180
    • Srinivasan, C.1    Gralla, E.B.2
  • 23
    • 33750031624 scopus 로고    scopus 로고
    • I.A. Hope, Oxford University Press, New York, 1999.
  • 24
    • 0027771804 scopus 로고
    • C. elegans mutant that lives twice as long as wild type
    • Kenyon C., Chang J., Gensch E., Rudner A., and Tabtiang A.R. C. elegans mutant that lives twice as long as wild type. Nature 366 (1993) 461-464
    • (1993) Nature , vol.366 , pp. 461-464
    • Kenyon, C.1    Chang, J.2    Gensch, E.3    Rudner, A.4    Tabtiang, A.R.5
  • 25
    • 0036828581 scopus 로고    scopus 로고
    • Animal models of oxidative stress, aging, and therapeutic antioxidant interventions
    • Melov S. Animal models of oxidative stress, aging, and therapeutic antioxidant interventions. Int. J. Biochem. Cell Biol. 34 (2002) 1395-1400
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , pp. 1395-1400
    • Melov, S.1
  • 26
    • 2442465387 scopus 로고    scopus 로고
    • Oxidative stress in Caenorhabditis elegans: Protective effects of superoxide dismutase/catalase mimetics
    • Sampayo J.N., Olsen A., and Lithgow G.J. Oxidative stress in Caenorhabditis elegans: Protective effects of superoxide dismutase/catalase mimetics. Aging Cell 2 (2003) 319-326
    • (2003) Aging Cell , vol.2 , pp. 319-326
    • Sampayo, J.N.1    Olsen, A.2    Lithgow, G.J.3
  • 27
    • 33644898819 scopus 로고    scopus 로고
    • Manganous ion supplementation accelerates wild type development, enhances stress resistance, and rescues the life span of a short-lived Caenorhabditis elegans mutant
    • Lin Y.T., Hoang H., Hsieh S.I., Rangel N., Foster A.L., Sampayo J.N., Lithgow G.J., and Srinivasan C. Manganous ion supplementation accelerates wild type development, enhances stress resistance, and rescues the life span of a short-lived Caenorhabditis elegans mutant. Free Radic. Biol. Med. 40 (2006) 1185-1193
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 1185-1193
    • Lin, Y.T.1    Hoang, H.2    Hsieh, S.I.3    Rangel, N.4    Foster, A.L.5    Sampayo, J.N.6    Lithgow, G.J.7    Srinivasan, C.8
  • 28
    • 0036022026 scopus 로고    scopus 로고
    • Temperature-dependence of mitochondrial function and production of reactive oxygen species in the intertidal mud clam Mya arenaria
    • Abele D., Heise K., Portner H.O., and Puntarulo S. Temperature-dependence of mitochondrial function and production of reactive oxygen species in the intertidal mud clam Mya arenaria. J. Exp. Biol. 205 (2002) 1831-1841
    • (2002) J. Exp. Biol. , vol.205 , pp. 1831-1841
    • Abele, D.1    Heise, K.2    Portner, H.O.3    Puntarulo, S.4
  • 29
    • 0346034910 scopus 로고    scopus 로고
    • Production of reactive oxygen species by isolated mitochondria of the Antarctic bivalve Laternula elliptica (King and Broderip) under heat stress
    • Heise K., Puntarulo S., Portner H.O., and Abele D. Production of reactive oxygen species by isolated mitochondria of the Antarctic bivalve Laternula elliptica (King and Broderip) under heat stress. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 134 (2003) 79-90
    • (2003) Comp. Biochem. Physiol. C Toxicol. Pharmacol. , vol.134 , pp. 79-90
    • Heise, K.1    Puntarulo, S.2    Portner, H.O.3    Abele, D.4
  • 30
    • 0018220069 scopus 로고
    • Superoxide radical and the oxygen enhancement of the toxicity of paraquat in Escherichia coli
    • Hassan H.M., and Fridovich I. Superoxide radical and the oxygen enhancement of the toxicity of paraquat in Escherichia coli. J. Biol. Chem. 253 (1978) 8143-8148
    • (1978) J. Biol. Chem. , vol.253 , pp. 8143-8148
    • Hassan, H.M.1    Fridovich, I.2
  • 31
    • 0018604132 scopus 로고
    • Paraquat and Escherichia coli: Mechanism of production of extracellular superoxide radical
    • Hassan H.M., and Fridovich I. Paraquat and Escherichia coli: Mechanism of production of extracellular superoxide radical. J. Biol. Chem. 254 (1979) 10846-10852
    • (1979) J. Biol. Chem. , vol.254 , pp. 10846-10852
    • Hassan, H.M.1    Fridovich, I.2
  • 34
    • 0030070138 scopus 로고    scopus 로고
    • "Free" iron, as detected by electron paramagnetic resonance spectroscopy, increases unequally in different tissues during dietary iron overload in the rat
    • Kozlov A.V., Bini A., Gallesi D., Giovannini F., Iannone A., Masini A., Meletti E., and Tomasi A. "Free" iron, as detected by electron paramagnetic resonance spectroscopy, increases unequally in different tissues during dietary iron overload in the rat. Biometals 9 (1996) 98-103
    • (1996) Biometals , vol.9 , pp. 98-103
    • Kozlov, A.V.1    Bini, A.2    Gallesi, D.3    Giovannini, F.4    Iannone, A.5    Masini, A.6    Meletti, E.7    Tomasi, A.8
  • 35
    • 0028831155 scopus 로고
    • Adaptation to oxidative stress in young, but not in mature or old, Caenorhabditis elegans
    • Darr D., and Fridovich I. Adaptation to oxidative stress in young, but not in mature or old, Caenorhabditis elegans. Free Radic. Biol. Med. 18 (1995) 195-201
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 195-201
    • Darr, D.1    Fridovich, I.2
  • 36
    • 0032053198 scopus 로고    scopus 로고
    • Identification of stress-responsive genes in Caenorhabditis elegans using RT-PCR differential display
    • Tawe W.N., Eschbach M.L., Walter R.D., and Henkle-Duhrsen K. Identification of stress-responsive genes in Caenorhabditis elegans using RT-PCR differential display. Nucleic Acids Res. 26 (1998) 1621-1627
    • (1998) Nucleic Acids Res. , vol.26 , pp. 1621-1627
    • Tawe, W.N.1    Eschbach, M.L.2    Walter, R.D.3    Henkle-Duhrsen, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.