메뉴 건너뛰기




Volumn 3, Issue 5, 2007, Pages 263-267

Molecular imaging of hydrogen peroxide produced for cell signaling

Author keywords

[No Author keywords available]

Indexed keywords

DYE; GROWTH FACTOR; HYDROGEN PEROXIDE; PEROXY CRIMSON; PEROXY GREEN; PEROXY RADICAL; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 34247255302     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio871     Document Type: Article
Times cited : (396)

References (29)
  • 1
    • 33745631769 scopus 로고    scopus 로고
    • 2, a necessary evil for cell signaling. Science 312, 1882-1883 (2006).
    • 2, a necessary evil for cell signaling. Science 312, 1882-1883 (2006).
  • 2
    • 0037376674 scopus 로고    scopus 로고
    • Oxidant signals and oxidative stress
    • Finkel, T. Oxidant signals and oxidative stress. Curr. Opin. Cell Biol. 15, 247-254 (2003).
    • (2003) Curr. Opin. Cell Biol , vol.15 , pp. 247-254
    • Finkel, T.1
  • 3
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of aging matures
    • Beckman, K.B. & Ames, B.N. The free radical theory of aging matures. Physiol. Rev. 78, 547-581 (1998).
    • (1998) Physiol. Rev , vol.78 , pp. 547-581
    • Beckman, K.B.1    Ames, B.N.2
  • 4
    • 33646698671 scopus 로고    scopus 로고
    • Hydrogen peroxide: A signaling messenger
    • Stone, J.R. & Yang, S. Hydrogen peroxide: a signaling messenger. Antioxid. Redox Signal. 8, 243-270 (2006).
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 243-270
    • Stone, J.R.1    Yang, S.2
  • 6
    • 15144343374 scopus 로고    scopus 로고
    • Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation
    • Bae, Y.S. et al. Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation. J. Biol. Chem. 272, 217-221 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 217-221
    • Bae, Y.S.1
  • 7
    • 0028015832 scopus 로고
    • Production of hydrogen peroxide by transforming growth factor-β1 and its involvement in induction of egr-1 in mouse osteoblastic cells
    • Ohba, M., Shibanuma, M., Kuroki, T. & Nose, K. Production of hydrogen peroxide by transforming growth factor-β1 and its involvement in induction of egr-1 in mouse osteoblastic cells. J. Cell Biol. 126, 1079-1088 (1994).
    • (1994) J. Cell Biol , vol.126 , pp. 1079-1088
    • Ohba, M.1    Shibanuma, M.2    Kuroki, T.3    Nose, K.4
  • 8
    • 0028851241 scopus 로고
    • 2+ signaling followed by phospholipase-A2 activation and potentiated by an adenosine derivative
    • 2+ signaling followed by phospholipase-A2 activation and potentiated by an adenosine derivative. Endocrinology 136, 116-123 (1995).
    • (1995) Endocrinology , vol.136 , pp. 116-123
    • Kimura, T.1    Okajima, F.2    Sho, K.3    Kobayashi, I.4    Kondo, Y.5
  • 9
    • 0034177790 scopus 로고    scopus 로고
    • 5-Hydroxytryptamine1A receptor/Gibetagamma stimulates mitogen-activated protein kinase via NAD(P)H oxidase and reactive oxygen species upstream of src in chinese hamster ovary fibroblasts
    • Mukhin, Y.V. et al. 5-Hydroxytryptamine1A receptor/Gibetagamma stimulates mitogen-activated protein kinase via NAD(P)H oxidase and reactive oxygen species upstream of src in chinese hamster ovary fibroblasts. Biochem. J. 347, 61-67 (2000).
    • (2000) Biochem. J , vol.347 , pp. 61-67
    • Mukhin, Y.V.1
  • 10
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • Lee, S.R., Kwon, K.S., Kim, S.R. & Rhee, S.G. Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J. Biol. Chem. 273, 15366-15372 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 15366-15372
    • Lee, S.R.1    Kwon, K.S.2    Kim, S.R.3    Rhee, S.G.4
  • 11
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • Salmeen, A. et al. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature 423, 769-773 (2003).
    • (2003) Nature , vol.423 , pp. 769-773
    • Salmeen, A.1
  • 13
    • 0029170274 scopus 로고
    • The roles of hydrogen peroxide and superoxide as messengers in the activation of transcription factor NF-κB
    • Schmidt, K.N., Amstad, P., Cerutti, P. & Baeuerle, P.A. The roles of hydrogen peroxide and superoxide as messengers in the activation of transcription factor NF-κB. Chem. Biol. 2, 13-22 (1995).
    • (1995) Chem. Biol , vol.2 , pp. 13-22
    • Schmidt, K.N.1    Amstad, P.2    Cerutti, P.3    Baeuerle, P.A.4
  • 14
    • 0141482021 scopus 로고    scopus 로고
    • 2 underlies glutamate-dependent inhibition of striatal dopamine release
    • 2 underlies glutamate-dependent inhibition of striatal dopamine release. Proc. Natl. Acad. Sci. USA 100, 11729-11734 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11729-11734
    • Avshalumov, M.V.1    Rice, M.E.2
  • 15
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • Wood, Z.A., Poole, L.B. & Karplus, P.A. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300, 650-653 (2003).
    • (2003) Science , vol.300 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 16
    • 0242668688 scopus 로고    scopus 로고
    • Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation
    • Woo, H.A. et al. Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation. Science 300, 653-656 (2003).
    • (2003) Science , vol.300 , pp. 653-656
    • Woo, H.A.1
  • 17
    • 0242416188 scopus 로고    scopus 로고
    • ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin
    • Biteau, B., Labarre, J. & Toledano, M.B. ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature 425, 980-984 (2003).
    • (2003) Nature , vol.425 , pp. 980-984
    • Biteau, B.1    Labarre, J.2    Toledano, M.B.3
  • 18
    • 33645037891 scopus 로고    scopus 로고
    • 2 by metal-catalysed histidine oxidation
    • 2 by metal-catalysed histidine oxidation. Nature 440, 363-367 (2006).
    • (2006) Nature , vol.440 , pp. 363-367
    • Lee, J.-W.1    Helmann, J.D.2
  • 20
    • 33749018509 scopus 로고    scopus 로고
    • Recent advances in fluorescent probes for the detection of reactive oxygen species
    • Soh, N. Recent advances in fluorescent probes for the detection of reactive oxygen species. Anal. Bioanal. Chem. 386, 532-543 (2006).
    • (2006) Anal. Bioanal. Chem , vol.386 , pp. 532-543
    • Soh, N.1
  • 21
    • 0032783532 scopus 로고    scopus 로고
    • Dihydro-fluorescein diacetate is superior for detecting intracellular oxidants: Comparison with 2′,7′- dichlorodihydrofluorescein diacetate, 5(and 6)-carboxy-2′,7′- dichlorodihydro-fluorescein diacetate, and dihydrorhodamine 123
    • Hempel, S.L., Buettner, G.R., O'Malley, Y.Q., Wessels, D.A. & Flaherty, D.M. Dihydro-fluorescein diacetate is superior for detecting intracellular oxidants: comparison with 2′,7′- dichlorodihydrofluorescein diacetate, 5(and 6)-carboxy-2′,7′- dichlorodihydro-fluorescein diacetate, and dihydrorhodamine 123. Free Radic. Biol. Med. 27, 146-159 (1999).
    • (1999) Free Radic. Biol. Med , vol.27 , pp. 146-159
    • Hempel, S.L.1    Buettner, G.R.2    O'Malley, Y.Q.3    Wessels, D.A.4    Flaherty, D.M.5
  • 22
    • 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., Diwu, Z., Panchuk-Voloshina, N. & Haugland, R.P. 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, 162-168 (1997).
    • (1997) Anal. Biochem , vol.253 , pp. 162-168
    • Zhou, M.1    Diwu, Z.2    Panchuk-Voloshina, N.3    Haugland, R.P.4
  • 23
    • 4544229167 scopus 로고    scopus 로고
    • Fluorescent probes for hydrogen peroxide based on a non-oxidative mechanism
    • Maeda, H. et al. Fluorescent probes for hydrogen peroxide based on a non-oxidative mechanism. Angew. Chem. Int. Ed. 43, 2389-2391 (2004).
    • (2004) Angew. Chem. Int. Ed , vol.43 , pp. 2389-2391
    • Maeda, H.1
  • 24
    • 33645283923 scopus 로고    scopus 로고
    • Genetically encoded fluorescent indicator for intracellular hydrogen peroxide
    • Belousov, V.V. et al. Genetically encoded fluorescent indicator for intracellular hydrogen peroxide. Nat. Methods 3, 281-286 (2006).
    • (2006) Nat. Methods , vol.3 , pp. 281-286
    • Belousov, V.V.1
  • 25
    • 9644273757 scopus 로고    scopus 로고
    • A selective, cell-permeable optical probe for hydrogen peroxide in living cells
    • Chang, M.C., Pralle, A., Isacoff, E.Y. & Chang, C.J. A selective, cell-permeable optical probe for hydrogen peroxide in living cells. J. Am. Chem. Soc. 126, 15392-15393 (2004).
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 15392-15393
    • Chang, M.C.1    Pralle, A.2    Isacoff, E.Y.3    Chang, C.J.4
  • 26
    • 28444495141 scopus 로고    scopus 로고
    • Boronate-based fluorescent probes for imaging cellular hydrogen peroxide
    • Miller, E.W., Albers, A.E., Pralle, A., Isacoff, E.Y. & Chang, C.J. Boronate-based fluorescent probes for imaging cellular hydrogen peroxide. J. Am. Chem. Soc. 127, 16652-16659 (2005).
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 16652-16659
    • Miller, E.W.1    Albers, A.E.2    Pralle, A.3    Isacoff, E.Y.4    Chang, C.J.5
  • 27
    • 0037474309 scopus 로고    scopus 로고
    • Development of novel fluorescence probes that can reliably detect reactive oxygen species and distinguish specific species
    • Setsukinai, K.-I., Urano, Y., Kakinuma, K., Majima, H.J. & Nagano, T. Development of novel fluorescence probes that can reliably detect reactive oxygen species and distinguish specific species. J. Biol. Chem. 278, 3170-3175 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 3170-3175
    • Setsukinai, K.-I.1    Urano, Y.2    Kakinuma, K.3    Majima, H.J.4    Nagano, T.5
  • 28
    • 0021273420 scopus 로고
    • Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells
    • Ullrich, A. et al. Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells. Nature 309, 418-425 (1984).
    • (1984) Nature , vol.309 , pp. 418-425
    • Ullrich, A.1
  • 29
    • 1942541169 scopus 로고    scopus 로고
    • The role of epidermal growth factor and its receptors in mammalian CNS
    • Wong, R.W.C. & Guillaud, L. The role of epidermal growth factor and its receptors in mammalian CNS. Cytokine Growth Factor Rev. 15, 147-156 (2004).
    • (2004) Cytokine Growth Factor Rev , vol.15 , pp. 147-156
    • Wong, R.W.C.1    Guillaud, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.