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Volumn 2, Issue 4, 2009, Pages 365-374

Fluorescent images of mitochondrial redox states in in situ mouse hypoxic ischemic intestines

Author keywords

flavoprotein; fluorescence; in vivo; ischemia; NADH; Optical diagnosis

Indexed keywords

FLAVOPROTEIN; IN-VIVO; ISCHEMIA; NADH; OPTICAL DIAGNOSIS;

EID: 79960516909     PISSN: 17935458     EISSN: 17937205     Source Type: Journal    
DOI: 10.1142/S1793545809000723     Document Type: Article
Times cited : (17)

References (40)
  • 1
    • 0035470979 scopus 로고    scopus 로고
    • Understanding the contributions of NADH and collagen to cervical tissue fluorescence spectra: Modeling, measurements, and implications
    • DOI 10.1117/1.1413209
    • R. Drezek, K. Sokolov, U. Utzinger, I. Boiko, A. Malpica, M. Follen, R. Richards-Kortum, Understanding the contributions of NADH and collagen to cervical tissue fluorescence spectra: Modeling, measurements, and implications, J. Biomed. Opt. 6, 385-396 (2001). (Pubitemid 34220957)
    • (2001) Journal of Biomedical Optics , vol.6 , Issue.4 , pp. 385-396
    • Drezek, R.1    Sokolov, K.2    Utzinger, U.3    Boiko, I.4    Malpica, A.5    Follen, M.6    Richards-Kortum, R.7
  • 2
    • 0032914851 scopus 로고    scopus 로고
    • In vivo identification of colonic dysplasia using fluorescence endoscopic imaging
    • DOI 10.1016/S0016-5107(99)70041-6
    • T. D. Wang, J. M. Crawford, M. S. Feld, Y. Wang, I. Itzkan, J. Van Dam, In vivo identification of colonic dysplasia using fluorescence endoscopic imaging, Gastrointest. Endosc. 49, 447-455 (1999). (Pubitemid 29217331)
    • (1999) Gastrointestinal Endoscopy , vol.49 , Issue.4 , pp. 447-455
    • Wang, T.D.1    Crawford, J.M.2    Feld, M.S.3    Wang, Y.4    Itzkan, I.5    Van Dam, J.6
  • 3
    • 33847080430 scopus 로고    scopus 로고
    • Mitochondrial function in vivo evaluated by NADH fluorescence: From animal models to human studies
    • A. Mayevsky and G. Rogatsky, Mitochondrial function in vivo evaluated by NADH fluorescence: From animal models to human studies, Am. J. Physiol. Cell. Physiol. 292, C615-C640 (2007).
    • (2007) Am. J. Physiol. Cell. Physiol. , vol.292
    • Mayevsky, A.1    Rogatsky, G.2
  • 5
    • 0023180318 scopus 로고
    • Inducers of adenylate cyclase reverse the effect of leukotriene D4 in isolated working guinea pig heart
    • O. G. Bjornsson, K. Kobayashi, J. R. Williamson, Inducers of adenylate cyclase reverse the effect of leukotriene D4 in isolated working guinea pig heart, Am. J. Physiol. 252, H1235-H1241 (1987).
    • (1987) Am. J. Physiol. , vol.252
    • Bjornsson, O.G.1    Kobayashi, K.2    Williamson, J.R.3
  • 6
    • 33646199857 scopus 로고    scopus 로고
    • Observation of mitochondrial morphology and biochemistry changes undergoing apoptosis by angularly resolved light scattering and cryoimaging
    • M. Ranji, D. L. Jaggard, B. Chance, Observation of mitochondrial morphology and biochemistry changes undergoing apoptosis by angularly resolved light scattering and cryoimaging, Proc. SPIE 6087, 60780K1-60780K9 (2006).
    • (2006) Proc. SPIE , vol.6087
    • Ranji, M.1    Jaggard, D.L.2    Chance, B.3
  • 8
    • 0032929504 scopus 로고    scopus 로고
    • Three-dimensional redox image of the normal gerbil brain
    • DOI 10.1016/S0306-4522(98)00670-8, PII S0306452298006708
    • A. Shino, M. Haida, B. Beauvoit, B. Chance, Three-dimensional redox image of the normal gerbil brain, Neuroscience 91, 1581-1585 (1999). (Pubitemid 29234284)
    • (1999) Neuroscience , vol.91 , Issue.4 , pp. 1581-1585
    • Shiino, A.1    Haida, M.2    Beauvoit, B.3    Chance, B.4
  • 9
    • 64349108767 scopus 로고    scopus 로고
    • Transcranial flavoprotein fluorescence imaging of mouse cortical activity and plasticity
    • M. Tohmi, K. Takahashi, Y. Kubota, R. Hishida, K. Shibuki. Transcranial flavoprotein fluorescence imaging of mouse cortical activity and plasticity, J. Neurochem. 109, 3-9 (2009).
    • (2009) J. Neurochem. , vol.109 , pp. 3-9
    • Tohmi, M.1    Takahashi, K.2    Kubota, Y.3    Hishida, R.4    Shibuki, K.5
  • 10
    • 66849097830 scopus 로고    scopus 로고
    • Autofluorescence imaging of NADH and flavoproteins in the rat brain: Insights from Monte Carlo simulations
    • B. L'Heureux, H. Gurden, F. Pain, Autofluorescence imaging of NADH and flavoproteins in the rat brain: Insights from Monte Carlo simulations, Opt. Express. 17, 9477-9490 (2009).
    • (2009) Opt. Express. , vol.17 , pp. 9477-9490
    • L'Heureux, B.1    Gurden, H.2    Pain, F.3
  • 11
    • 66349090820 scopus 로고    scopus 로고
    • Rapid and sensitive mapping of long-range connections in vitro using flavoprotein autofluorescence imaging combined with laser photostimulation
    • D. A. Llano, B. B. Theyel, A. K. Mallik, S. M. Sherman, N. P. Issa, Rapid and sensitive mapping of long-range connections in vitro using flavoprotein autofluorescence imaging combined with laser photostimulation, J. Neurophysiol. 101, 3325-3340 (2009).
    • (2009) J. Neurophysiol. , vol.101 , pp. 3325-3340
    • Llano, D.A.1    Theyel, B.B.2    Mallik, A.K.3    Sherman, S.M.4    Issa, N.P.5
  • 12
    • 77049233362 scopus 로고
    • Respiratory enzymes in oxidative phosphorylation. I. Kinetics of oxygen utilization
    • B. Chance, G. R. Williams, Respiratory enzymes in oxidative phosphorylation. I. Kinetics of oxygen utilization, J. Biol. Chem. 217, 383-393 (1955).
    • (1955) J. Biol. Chem. , vol.217 , pp. 383-393
    • Chance, B.1    Williams, G.R.2
  • 13
    • 0000432007 scopus 로고
    • Respiratory enzymes in oxidative phosphorylation. II. Difference spectra
    • B. Chance, G. R. Williams, Respiratory enzymes in oxidative phosphorylation. II. Difference spectra, J. Biol. Chem. 217(1), 395-407 (1955).
    • (1955) J. Biol. Chem. , vol.217 , Issue.1 , pp. 395-407
    • Chance, B.1    Williams, G.R.2
  • 14
    • 77049249588 scopus 로고
    • Respiratory enzymes in oxidative phosphorylation. III. The steady state
    • B. Chance, G. R. Williams, Respiratory enzymes in oxidative phosphorylation. III. The steady state, J. Biol. Chem. 217(1), 409-427 (1955).
    • (1955) J. Biol. Chem. , vol.217 , Issue.1 , pp. 409-427
    • Chance, B.1    Williams, G.R.2
  • 15
    • 77049248708 scopus 로고
    • Respiratory enzymes in oxidative phosphorylation. IV. The respiratory chain
    • B. Chance, G. R. Williams, Respiratory enzymes in oxidative phosphorylation. IV. The respiratory chain, J. Biol. Chem. 217(1), 429-438 (1955).
    • (1955) J. Biol. Chem. , vol.217 , Issue.1 , pp. 429-438
    • Chance, B.1    Williams, G.R.2
  • 16
    • 67349160864 scopus 로고
    • Respiratory enzymes in oxidative phosphorylation. V. A mechanism for oxidative phosphorylation
    • B. Chance, G. R. Williams, W. F. Holmes, J. Higgins, Respiratory enzymes in oxidative phosphorylation. V. A mechanism for oxidative phosphorylation, J. Biol. Chem. 217, 439-451 (1955).
    • (1955) J. Biol. Chem. , vol.217 , pp. 439-451
    • Chance, B.1    Williams, G.R.2    Holmes, W.F.3    Higgins, J.4
  • 17
    • 0018786822 scopus 로고
    • Oxidation-reduction ratio studies of mitochondria in freeze-trapped samples
    • B. Chance, B. Schoener, R. Oshino, F. Itshak, Y. Nakase, Oxidation-reduction ratio studies of mitochondria in freeze-trapped samples, J. Biol. Chem. 254, 4764-4771 (1979).
    • (1979) J. Biol. Chem. , vol.254 , pp. 4764-4771
    • Chance, B.1    Schoener, B.2    Oshino, R.3    Itshak, F.4    Nakase, Y.5
  • 18
    • 0031729302 scopus 로고    scopus 로고
    • Poor recovery of mitochondrial redox state in CA1 after transient forebrain ischemia in gerbils
    • A. Shino, M. Matsuda, J. Handa, B. Chance, Poor recovery of mitochondrial redox state in CA1 after transient forebrain ischemia in gerbils, Stroke 46, 2421-2425 (1999). (Pubitemid 28511967)
    • (1998) Stroke , vol.29 , Issue.11 , pp. 2421-2425
    • Shiino, A.1    Matsuda, M.2    Handa, J.3    Chance, B.4
  • 22
    • 0022912511 scopus 로고
    • Scanning fluorometer for the rapid assessment of pyridine nucleotide and flavoprotein fluorescence changes in tissues in vivo
    • B. M. Paddle, G. Brown, P. Vincent, Scanning fluorometer for the rapid assessment of pyridine nucleotide and flavoprotein fluorescence changes in tissues in vivo. J. Biomed. Eng. 8, 334-340 (1986). (Pubitemid 16026580)
    • (1986) Journal of Biomedical Engineering , vol.8 , Issue.4 , pp. 334-340
    • Paddle, B.M.1    Brown, G.2    Vincent, P.3
  • 23
    • 0034759986 scopus 로고    scopus 로고
    • Two-photon excitation laser scanning microscopy of human, porcine, and rabbit nasal septal cartilage
    • DOI 10.1089/107632701753213219
    • B. J. Wong, V. Wallace, M. Coleno, H. P. Benton, B. J. Tromberg, Two-photon excitation laser scanning microscopy of human, porcine, and rabbit nasal septal cartilage, Tissue Eng. 7, 599-606 (2001). (Pubitemid 33032382)
    • (2001) Tissue Engineering , vol.7 , Issue.5 , pp. 599-606
    • Wong, B.J.F.1    Wallace, V.2    Coleno, M.3    Benton, H.P.4    Tromberg, B.J.5
  • 24
    • 0020490677 scopus 로고
    • Quantitative histochemical resolution of the oxidation-reduction and phosphate potentials within the simple hepatic acinus
    • A. Ghosh, D. Finegold, W. White, K. Zawalich, F. M. Matschinsky, Quantitative histochemical resolution of the oxidation-reduction and phosphate potentials within the simple hepatic acinus, J. Biol. Chem. 257, 5476-5481 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 5476-5481
    • Ghosh, A.1    Finegold, D.2    White, W.3    Zawalich, K.4    Matschinsky, F.M.5
  • 25
    • 80052094177 scopus 로고
    • Inhibition of electron and energy transfer in mitochondria, 1. Effects of amytal, thiopental, rotenone, progesterone and methylene glycol
    • B. Chance, G. Hollunger, Inhibition of electron and energy transfer in mitochondria, 1. Effects of amytal, thiopental, rotenone, progesterone and methylene glycol, J. Biol. Chem. 238, 8-31 (1963).
    • (1963) J. Biol. Chem. , vol.238 , pp. 8-31
    • Chance, B.1    Hollunger, G.2
  • 26
    • 0001696061 scopus 로고
    • Respiratory enzymes in oxidative phosphorylation. VII. Binding of intramitochondrial reduced pyridine nucleotide
    • B. Chance, H. Baltschefsky, Respiratory enzymes in oxidative phosphorylation. VII. Binding of intramitochondrial reduced pyridine nucleotide, J. Biol. Chem. 233, 736-739 (1958).
    • (1958) J. Biol. Chem. , vol.233 , pp. 736-739
    • Chance, B.1    Baltschefsky, H.2
  • 27
    • 0000613615 scopus 로고
    • Intracellular oxidation-reduction states in vivo
    • B. Chance, P. Cohen, F. Jobsis, B. Schoener, Intracellular oxidation-reduction states in vivo, Science 137, 499-508 (1962).
    • (1962) Science , vol.137 , pp. 499-508
    • Chance, B.1    Cohen, P.2    Jobsis, F.3    Schoener, B.4
  • 29
    • 0015295895 scopus 로고
    • Fluorometric studies of oxidative metabolism in isolated papillary muscle of the rabbit
    • J. B. Chapman, Fluorometric studies of oxidative metabolism in isolated papillary muscle of the rabbit, J. Gen. Physiol. 59, 135154 (1972).
    • (1972) J. Gen. Physiol. , vol.59 , pp. 135154
    • Chapman, J.B.1
  • 32
    • 0030895058 scopus 로고    scopus 로고
    • (Semi-)quantitative analysis of reduced nicotinamide adenine dinucleotide fluorescence images of blood-perfused rat heart
    • J. M. C. C. Coremans, C. Ince, H. A. Bruining, G. J. Puppels, Semi-quantitative analysis of reduced nicotinamide adenine dinucleotide fluorescence images of blood-perfused rat heart, Biophysical Journal 72, 1849-1860 (1997). (Pubitemid 27133124)
    • (1997) Biophysical Journal , vol.72 , Issue.4 , pp. 1849-1860
    • Coremans, J.M.C.C.1    Ince, C.2    Bruining, H.A.3    Puppels, G.J.4
  • 34
    • 0023890242 scopus 로고
    • Metabolic substrate utilization by rabbit proximal tubule. An NADH fluorescence study
    • R. S. Balaban, L. J. Mandel, Metabolic substrate utilization by rabbit proximal tubule. An NADH fluorescence study, Am. J. Physiol. Renal Fluid Electrolyte Physiol. 254, F407F416 (1988).
    • (1988) Am. J. Physiol. Renal Fluid Electrolyte Physiol. , vol.254
    • Balaban, R.S.1    Mandel, L.J.2
  • 36
    • 0017823707 scopus 로고
    • Pentobarbital-induced reduction of pyridine nucleotide measured by surface fluorometry in perfused rat heart
    • DOI 10.1016/0006-2952(78)90110-7
    • J. P. Weiss, C. H. Barlow, B. Chance, Pentobarbital-induced reduction of pyridine nucleotide measured by surface fluorometry in perfused rat heart, Biochem. Pharmacol. 15(27), 1510-1511 (1978). (Pubitemid 8401753)
    • (1978) Biochemical Pharmacology , vol.27 , Issue.10 , pp. 1510-1511
    • Weiss, J.P.1    Barlow, C.H.2    Chance, B.3
  • 37
    • 0014761090 scopus 로고
    • Reaction sites of rotenone, piericidin A, and amytal in relation to the nonheme iron components of NADH dehydrogenase
    • M. Gutman, T. P. Singer, H. Beinert, J. E. Casida, Reaction sites of rotenone, piericidin A, and amytal in relation to the nonheme iron components of NADH dehydrogenase, Proc. Natl. Acad. Sci. USA 65, 763-770 (1970).
    • (1970) Proc. Natl. Acad. Sci. USA , vol.65 , pp. 763-770
    • Gutman, M.1    Singer, T.P.2    Beinert, H.3    Casida, J.E.4
  • 40
    • 79960817863 scopus 로고    scopus 로고
    • Quantitative redox scanning of tissue samples using a calibration procedure
    • H. N. Xu, B. Wu, S. Nioka, B. Chance, L. Z. Li, Quantitative redox scanning of tissue samples using a calibration procedure, J. Innov. Opt. Health. Sci. 2(4), 375-385 (2009).
    • (2009) J. Innov. Opt. Health. Sci. , vol.2 , Issue.4 , pp. 375-385
    • Xu, H.N.1    Wu, B.2    Nioka, S.3    Chance, B.4    Li, L.Z.5


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