메뉴 건너뛰기




Volumn 397, Issue 2, 2010, Pages 144-151

Analysis of activity and inhibition of oxygen-dependent enzymes by optical respirometry on the LightCycler system

Author keywords

Cyclooxygenase; Cytochrome P450; Enzymatic assays; LightCycler; Monoamine oxidase; Optical oxygen respirometry; Oxygen sensitive probes; Phosphorescence

Indexed keywords

DETOXIFICATION; DISEASES; DRUG DELIVERY; ENZYME INHIBITION; OXYGEN; PHOSPHORESCENCE; PROBES;

EID: 72049119622     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.10.029     Document Type: Article
Times cited : (15)

References (35)
  • 1
    • 0014314486 scopus 로고
    • Some observations upon a new inhibitor of monoamine oxidase in brain tissue
    • Johnston J.P. Some observations upon a new inhibitor of monoamine oxidase in brain tissue. Biochem. Pharmacol. 17 7 (1968) 1285-1297
    • (1968) Biochem. Pharmacol. , vol.17 , Issue.7 , pp. 1285-1297
    • Johnston, J.P.1
  • 2
    • 0021945989 scopus 로고
    • Combined MAOI, TCA, and direct stimulant therapy of treatment-resistant depression
    • Feighner J.P., Herbstein J., and Damlouji N. Combined MAOI, TCA, and direct stimulant therapy of treatment-resistant depression. J. Clin. Psychiatry 46 6 (1985) 206-209
    • (1985) J. Clin. Psychiatry , vol.46 , Issue.6 , pp. 206-209
    • Feighner, J.P.1    Herbstein, J.2    Damlouji, N.3
  • 3
    • 0028145566 scopus 로고
    • Increased monoamine oxidase B activity in plaque-associated astrocytes of Alzheimer brains revealed by quantitative enzyme radioautography
    • Saura J., et al. Increased monoamine oxidase B activity in plaque-associated astrocytes of Alzheimer brains revealed by quantitative enzyme radioautography. Neuroscience 62 1 (1994) 15-30
    • (1994) Neuroscience , vol.62 , Issue.1 , pp. 15-30
    • Saura, J.1
  • 4
    • 0015274536 scopus 로고
    • Some puzzling pharmacological effects of monoamine oxidase inhibitors
    • Knoll J., and Magyar K. Some puzzling pharmacological effects of monoamine oxidase inhibitors. Adv. Biochem. Psychopharmacol. 5 (1972) 393-408
    • (1972) Adv. Biochem. Psychopharmacol. , vol.5 , pp. 393-408
    • Knoll, J.1    Magyar, K.2
  • 5
    • 30444437749 scopus 로고    scopus 로고
    • Monoamine oxidase: isoforms and inhibitors in Parkinson's disease and depressive illness
    • Youdim M.B., and Bakhle Y.S. Monoamine oxidase: isoforms and inhibitors in Parkinson's disease and depressive illness. Br. J. Pharmacol. 147 Suppl. 1 (2006) S287-S296
    • (2006) Br. J. Pharmacol. , vol.147 , Issue.SUPPL. 1
    • Youdim, M.B.1    Bakhle, Y.S.2
  • 6
    • 56349096248 scopus 로고    scopus 로고
    • Clorgyline and other propargylamine derivatives as inhibitors of succinate-dependent H(2)O(2) release at NADH:UBIQUINONE oxidoreductase (Complex I) in brain mitochondria
    • Zoccarato F., Cappellotto M., and Alexandre A. Clorgyline and other propargylamine derivatives as inhibitors of succinate-dependent H(2)O(2) release at NADH:UBIQUINONE oxidoreductase (Complex I) in brain mitochondria. J. Bioenerg. Biomembr. 40 4 (2008) 289-296
    • (2008) J. Bioenerg. Biomembr. , vol.40 , Issue.4 , pp. 289-296
    • Zoccarato, F.1    Cappellotto, M.2    Alexandre, A.3
  • 7
    • 0034770465 scopus 로고    scopus 로고
    • Human drug metabolism and the cytochromes P450: application and relevance of in vitro models
    • Venkatakrishnan K., Von Moltke L.L., and Greenblatt D.J. Human drug metabolism and the cytochromes P450: application and relevance of in vitro models. J. Clin. Pharmacol. 41 11 (2001) 1149-1179
    • (2001) J. Clin. Pharmacol. , vol.41 , Issue.11 , pp. 1149-1179
    • Venkatakrishnan, K.1    Von Moltke, L.L.2    Greenblatt, D.J.3
  • 8
    • 0028009093 scopus 로고
    • The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1
    • Picot D., Loll P.J., and Garavito R.M. The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1. Nature 367 6460 (1994) 243-249
    • (1994) Nature , vol.367 , Issue.6460 , pp. 243-249
    • Picot, D.1    Loll, P.J.2    Garavito, R.M.3
  • 9
    • 0027992733 scopus 로고
    • Purification, characterization and selective inhibition of human prostaglandin G/H synthase 1 and 2 expressed in the baculovirus system
    • Barnett J., et al. Purification, characterization and selective inhibition of human prostaglandin G/H synthase 1 and 2 expressed in the baculovirus system. Biochim. Biophys. Acta 1209 1 (1994) 130-139
    • (1994) Biochim. Biophys. Acta , vol.1209 , Issue.1 , pp. 130-139
    • Barnett, J.1
  • 10
    • 0021943450 scopus 로고
    • Inactivation of prostaglandin H synthase and prostacyclin synthase by phenylbutazone. Requirement for peroxidative metabolism
    • Reed G.A., Griffin I.O., and Eling T.E. Inactivation of prostaglandin H synthase and prostacyclin synthase by phenylbutazone. Requirement for peroxidative metabolism. Mol. Pharmacol. 27 1 (1985) 109-114
    • (1985) Mol. Pharmacol. , vol.27 , Issue.1 , pp. 109-114
    • Reed, G.A.1    Griffin, I.O.2    Eling, T.E.3
  • 11
    • 13144260638 scopus 로고    scopus 로고
    • Pharmacological analysis of cyclooxygenase-1 in inflammation
    • Smith C.J., et al. Pharmacological analysis of cyclooxygenase-1 in inflammation. Proc. Natl. Acad. Sci. USA 95 22 (1998) 13313-13318
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.22 , pp. 13313-13318
    • Smith, C.J.1
  • 12
    • 0037652327 scopus 로고    scopus 로고
    • Nonsteroidal antiinflammatory drugs and a selective cyclooxygenase 2 inhibitor uncouple mitochondria in intact cells
    • Krause M.M., et al. Nonsteroidal antiinflammatory drugs and a selective cyclooxygenase 2 inhibitor uncouple mitochondria in intact cells. Arthritis Rheum. 48 5 (2003) 1438-1444
    • (2003) Arthritis Rheum. , vol.48 , Issue.5 , pp. 1438-1444
    • Krause, M.M.1
  • 13
    • 23944510006 scopus 로고    scopus 로고
    • An overview of the recent developments in analytical methodologies for determination of COX-2 inhibitors in bulk drugs, pharmaceuticals and biological matrices
    • Nageswara Rao R., Meena S., and Raghuram Rao A. An overview of the recent developments in analytical methodologies for determination of COX-2 inhibitors in bulk drugs, pharmaceuticals and biological matrices. J. Pharm. Biomed. Anal. 39 3-4 (2005) 349-363
    • (2005) J. Pharm. Biomed. Anal. , vol.39 , Issue.3-4 , pp. 349-363
    • Nageswara Rao, R.1    Meena, S.2    Raghuram Rao, A.3
  • 14
    • 14344261179 scopus 로고    scopus 로고
    • HPLC-based bioactivity profiling of plant extracts: a kinetic assay for the identification of monoamine oxidase-A inhibitors using human recombinant monoamine oxidase-A
    • Dittmann K., Riese U., and Hamburger M. HPLC-based bioactivity profiling of plant extracts: a kinetic assay for the identification of monoamine oxidase-A inhibitors using human recombinant monoamine oxidase-A. Phytochemistry 65 21 (2004) 2885-2891
    • (2004) Phytochemistry , vol.65 , Issue.21 , pp. 2885-2891
    • Dittmann, K.1    Riese, U.2    Hamburger, M.3
  • 15
    • 22244465541 scopus 로고    scopus 로고
    • Development and validation of a reversed-phase liquid chromatographic method for separation and simultaneous determination of COX-2 inhibitors in pharmaceuticals and its application to biological fluids
    • Rao R.N., et al. Development and validation of a reversed-phase liquid chromatographic method for separation and simultaneous determination of COX-2 inhibitors in pharmaceuticals and its application to biological fluids. Biomed. Chromatogr. 19 5 (2005) 362-368
    • (2005) Biomed. Chromatogr. , vol.19 , Issue.5 , pp. 362-368
    • Rao, R.N.1
  • 16
    • 0031570357 scopus 로고    scopus 로고
    • Microtiter plate assays for inhibition of human, drug-metabolizing cytochromes P450
    • Crespi C.L., Miller V.P., and Penman B.W. Microtiter plate assays for inhibition of human, drug-metabolizing cytochromes P450. Anal. Biochem. 248 1 (1997) 188-190
    • (1997) Anal. Biochem. , vol.248 , Issue.1 , pp. 188-190
    • Crespi, C.L.1    Miller, V.P.2    Penman, B.W.3
  • 17
    • 0031573401 scopus 로고    scopus 로고
    • A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: applications in detecting the activity of phagocyte NADPH oxidase and other oxidases
    • Zhou M., et al. A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: applications in detecting the activity of phagocyte NADPH oxidase and other oxidases. Anal. Biochem. 253 2 (1997) 162-168
    • (1997) Anal. Biochem. , vol.253 , Issue.2 , pp. 162-168
    • Zhou, M.1
  • 18
    • 0033551732 scopus 로고    scopus 로고
    • The binding of arachidonic acid in the cyclooxygenase active site of mouse prostaglandin endoperoxide synthase-2 (COX-2). A putative L-shaped binding conformation utilizing the top channel region
    • Rowlinson S.W., et al. The binding of arachidonic acid in the cyclooxygenase active site of mouse prostaglandin endoperoxide synthase-2 (COX-2). A putative L-shaped binding conformation utilizing the top channel region. J. Biol. Chem. 274 33 (1999) 23305-23310
    • (1999) J. Biol. Chem. , vol.274 , Issue.33 , pp. 23305-23310
    • Rowlinson, S.W.1
  • 19
    • 0034708764 scopus 로고    scopus 로고
    • Different catalytically competent arrangements of arachidonic acid within the cyclooxygenase active site of prostaglandin endoperoxide H synthase-1 lead to the formation of different oxygenated products
    • Thuresson E.D., Lakkides K.M., and Smith W.L. Different catalytically competent arrangements of arachidonic acid within the cyclooxygenase active site of prostaglandin endoperoxide H synthase-1 lead to the formation of different oxygenated products. J. Biol. Chem. 275 12 (2000) 8501-8507
    • (2000) J. Biol. Chem. , vol.275 , Issue.12 , pp. 8501-8507
    • Thuresson, E.D.1    Lakkides, K.M.2    Smith, W.L.3
  • 20
    • 0035971116 scopus 로고    scopus 로고
    • Prostaglandin endoperoxide H synthase-1: the functions of cyclooxygenase active site residues in the binding, positioning, and oxygenation of arachidonic acid
    • Thuresson E.D., et al. Prostaglandin endoperoxide H synthase-1: the functions of cyclooxygenase active site residues in the binding, positioning, and oxygenation of arachidonic acid. J. Biol. Chem. 276 13 (2001) 10347-10357
    • (2001) J. Biol. Chem. , vol.276 , Issue.13 , pp. 10347-10357
    • Thuresson, E.D.1
  • 21
    • 1642443176 scopus 로고    scopus 로고
    • Methods in optical oxygen sensing: protocols and critical analyses
    • Papkovsky D.B. Methods in optical oxygen sensing: protocols and critical analyses. Oxygen Sensing 381 (2004) 715-735
    • (2004) Oxygen Sensing , vol.381 , pp. 715-735
    • Papkovsky, D.B.1
  • 22
    • 72049114369 scopus 로고    scopus 로고
    • Toxicological assessment of chemicals using Caenorhabditis elegans and optical oxygen respirometry
    • Schouest K., et al. Toxicological assessment of chemicals using Caenorhabditis elegans and optical oxygen respirometry. Environ Toxicol. Chem. (2008) 1
    • (2008) Environ Toxicol. Chem. , pp. 1
    • Schouest, K.1
  • 23
    • 22044442695 scopus 로고    scopus 로고
    • Optical oxygen microrespirometry as a platform for environmental toxicology and animal model studies
    • O'Mahony F.C., et al. Optical oxygen microrespirometry as a platform for environmental toxicology and animal model studies. Environ. Sci. Technol. 39 13 (2005) 5010-5014
    • (2005) Environ. Sci. Technol. , vol.39 , Issue.13 , pp. 5010-5014
    • O'Mahony, F.C.1
  • 24
    • 0001745377 scopus 로고
    • Phosphorescent complexes of porphyrin-ketones-optical properties and application to oxygen sensing
    • Papkovsky D.B., et al. Phosphorescent complexes of porphyrin-ketones-optical properties and application to oxygen sensing. Anal. Chem. 67 22 (1995) 4112-4117
    • (1995) Anal. Chem. , vol.67 , Issue.22 , pp. 4112-4117
    • Papkovsky, D.B.1
  • 25
    • 2942672091 scopus 로고    scopus 로고
    • Iridium luminophore complexes for unimolecular oxygen sensors
    • DeRosa M.C., et al. Iridium luminophore complexes for unimolecular oxygen sensors. J. Am. Chem. Soc. 126 24 (2004) 7619-7626
    • (2004) J. Am. Chem. Soc. , vol.126 , Issue.24 , pp. 7619-7626
    • DeRosa, M.C.1
  • 26
    • 0001560696 scopus 로고    scopus 로고
    • Photostable optical oxygen sensing material: platinum tetrakis(pentafluorophenyl)porphyrin immobilized in polystyrene
    • Lee S.K., and Okura I. Photostable optical oxygen sensing material: platinum tetrakis(pentafluorophenyl)porphyrin immobilized in polystyrene. Anal. Commun. 34 6 (1997) 185-188
    • (1997) Anal. Commun. , vol.34 , Issue.6 , pp. 185-188
    • Lee, S.K.1    Okura, I.2
  • 27
    • 0032402089 scopus 로고    scopus 로고
    • Use of platinum coproporphyrin and delayed luminescence imaging to extend the number of targets FISH karyotyping
    • Tanke H.J., et al. Use of platinum coproporphyrin and delayed luminescence imaging to extend the number of targets FISH karyotyping. Cytometry 33 4 (1998) 453-459
    • (1998) Cytometry , vol.33 , Issue.4 , pp. 453-459
    • Tanke, H.J.1
  • 28
    • 58149462497 scopus 로고    scopus 로고
    • Luminescent nanobeads for optical sensing and imaging of dissolved oxygen
    • Borisov S.M., and Klimant I. Luminescent nanobeads for optical sensing and imaging of dissolved oxygen. Microchim. Acta 164 (2009) 7-15
    • (2009) Microchim. Acta , vol.164 , pp. 7-15
    • Borisov, S.M.1    Klimant, I.2
  • 29
    • 35349019683 scopus 로고    scopus 로고
    • Ultrabright oxygen optodes based on cyclometalated iridium(III) coumarin complexes
    • Borisov S.M., and Klimant I. Ultrabright oxygen optodes based on cyclometalated iridium(III) coumarin complexes. Anal. Chem. 79 19 (2007) 7501-7509
    • (2007) Anal. Chem. , vol.79 , Issue.19 , pp. 7501-7509
    • Borisov, S.M.1    Klimant, I.2
  • 30
    • 38949162248 scopus 로고    scopus 로고
    • Data analysis algorithm for high throughput enzymatic oxygen consumption assays based on quenched-fluorescence detection Sens
    • Ogurtsov V.I., et al. Data analysis algorithm for high throughput enzymatic oxygen consumption assays based on quenched-fluorescence detection Sens. Actuators B 129 2 (2007) 581-590
    • (2007) Actuators B , vol.129 , Issue.2 , pp. 581-590
    • Ogurtsov, V.I.1
  • 31
    • 34147159979 scopus 로고    scopus 로고
    • Analysis of mitochondrial function using phosphorescent oxygen-sensitive probes
    • Will Y., et al. Analysis of mitochondrial function using phosphorescent oxygen-sensitive probes. Nat. Protoc. 1 6 (2006) 2563-2572
    • (2006) Nat. Protoc. , vol.1 , Issue.6 , pp. 2563-2572
    • Will, Y.1
  • 33
    • 22944472372 scopus 로고    scopus 로고
    • Phosphorescent oxygen-sensitive materials for biological applications
    • O'Donovan C., et al. Phosphorescent oxygen-sensitive materials for biological applications. J. Mater. Chem. 15 27-28 (2005) 2946-2951
    • (2005) J. Mater. Chem. , vol.15 , Issue.27-28 , pp. 2946-2951
    • O'Donovan, C.1
  • 34
    • 2142698577 scopus 로고    scopus 로고
    • Fluorinated phenylcyclopropylamines. Part 3. Inhibition of monoamine oxidase A and B
    • Yoshida S., et al. Fluorinated phenylcyclopropylamines. Part 3. Inhibition of monoamine oxidase A and B. Bioorg. Med. Chem. 12 10 (2004) 2645-2652
    • (2004) Bioorg. Med. Chem. , vol.12 , Issue.10 , pp. 2645-2652
    • Yoshida, S.1
  • 35
    • 0021943450 scopus 로고
    • Inactivation of prostaglandin H synthase and prostacyclin synthase by phenylbutazone. Requirement for peroxidative metabolism
    • Reed G., Griffin I., and Eling T. Inactivation of prostaglandin H synthase and prostacyclin synthase by phenylbutazone. Requirement for peroxidative metabolism. Mol. Pharmacol. 27 1 (1985) 109-114
    • (1985) Mol. Pharmacol. , vol.27 , Issue.1 , pp. 109-114
    • Reed, G.1    Griffin, I.2    Eling, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.