메뉴 건너뛰기




Volumn 17, Issue 2, 2005, Pages 183-189

Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; GROWTH FACTOR; HYDROGEN PEROXIDE; PEROXIREDOXIN; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE;

EID: 15044362438     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2005.02.004     Document Type: Review
Times cited : (642)

References (47)
  • 1
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • J.D. Lambeth NOX enzymes and the biology of reactive oxygen Nat Rev Immunol 4 2004 181 189
    • (2004) Nat Rev Immunol , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 2
    • 0032053707 scopus 로고    scopus 로고
    • Oxygen radicals and signaling
    • T. Finkel Oxygen radicals and signaling Curr Opin Cell Biol 10 1998 248 253
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 248-253
    • Finkel, T.1
  • 3
    • 0034633602 scopus 로고    scopus 로고
    • Hydrogen peroxide: A key messenger that modulates protein phosphorylation through cysteine oxidation
    • S.G. Rhee, Y.S. Bae, S.-R. Lee, and J. Kwon Hydrogen peroxide: A key messenger that modulates protein phosphorylation through cysteine oxidation Sci STKE 2000 2000 PE1
    • (2000) Sci STKE , vol.2000 , pp. 1
    • Rhee, S.G.1    Bae, Y.S.2    Lee, S.-R.3    Kwon, J.4
  • 5
    • 0036260697 scopus 로고    scopus 로고
    • Cellular response to oxidative stress: Signaling for suicide and survival
    • J.L. Martindale, and N.J. Holbrook Cellular response to oxidative stress: signaling for suicide and survival J Cell Physiol 192 2002 1 15
    • (2002) J Cell Physiol , vol.192 , pp. 1-15
    • Martindale, J.L.1    Holbrook, N.J.2
  • 6
    • 0028918334 scopus 로고
    • Superoxide and hydrogen peroxide in relation to mammalian cell proliferation
    • R.H. Burdon Superoxide and hydrogen peroxide in relation to mammalian cell proliferation Free Radic Biol Med 18 1995 775 794
    • (1995) Free Radic Biol Med , vol.18 , pp. 775-794
    • Burdon, R.H.1
  • 7
    • 0028973482 scopus 로고
    • Requirement for generation of H2O2 for platelet-derived growth factor signal transduction
    • M. Sundaresan, Z.X. Yu, V.J. Ferrans, K. Irani, and T. Finkel Requirement for generation of H2O2 for platelet-derived growth factor signal transduction Science 270 1995 296 299
    • (1995) Science , vol.270 , pp. 296-299
    • Sundaresan, M.1    Yu, Z.X.2    Ferrans, V.J.3    Irani, K.4    Finkel, T.5
  • 8
    • 15144343374 scopus 로고    scopus 로고
    • Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation
    • Y.S. Bae, S.W. Kang, M.S. Seo, I.C. Baines, E. Tekle, P.B. Chock, and S.G. Rhee Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation J Biol Chem 272 1997 217 221
    • (1997) J Biol Chem , vol.272 , pp. 217-221
    • Bae, Y.S.1    Kang, S.W.2    Seo, M.S.3    Baines, I.C.4    Tekle, E.5    Chock, P.B.6    Rhee, S.G.7
  • 9
    • 0033529675 scopus 로고    scopus 로고
    • Reactive oxygen species mediate the activation of Akt/protein kinase B by angiotensin II in vascular smooth muscle cells
    • M. Ushio-Fukai, R.W. Alexander, M. Akers, Q. Yin, Y. Fujio, K. Walsh, and K.K. Griendling Reactive oxygen species mediate the activation of Akt/protein kinase B by angiotensin II in vascular smooth muscle cells J Biol Chem 274 1999 22699 22704
    • (1999) J Biol Chem , vol.274 , pp. 22699-22704
    • Ushio-Fukai, M.1    Alexander, R.W.2    Akers, M.3    Yin, Q.4    Fujio, Y.5    Walsh, K.6    Griendling, K.K.7
  • 10
    • 0030887994 scopus 로고    scopus 로고
    • Roles of aspartic acid-181 and serine-222 in intermediate formation and hydrolysis of the mammalian protein-tyrosine-phosphatase PTP1
    • D.L. Lohse, J.M. Denu, N. Santoro, and J.E. Dixon Roles of aspartic acid-181 and serine-222 in intermediate formation and hydrolysis of the mammalian protein-tyrosine-phosphatase PTP1 Biochemistry 36 1997 4568 4575
    • (1997) Biochemistry , vol.36 , pp. 4568-4575
    • Lohse, D.L.1    Denu, J.M.2    Santoro, N.3    Dixon, J.E.4
  • 11
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation
    • J.M. Denu, and K.G. Tanner Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation Biochemistry 37 1998 5633 5642
    • (1998) Biochemistry , vol.37 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 12
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • S.R. Lee, K.S. Kwon, S.R. Kim, and S.G. Rhee Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor J Biol Chem 273 1998 15366 15372
    • (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
  • 13
    • 0035877633 scopus 로고    scopus 로고
    • Insulin-stimulated hydrogen peroxide reversibly inhibits protein tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade
    • K. Mahadev, A. Zilbering, L. Zhu, and B.J. Goldstein Insulin-stimulated hydrogen peroxide reversibly inhibits protein tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade J Biol Chem 276 2001 21938 21942
    • (2001) J Biol Chem , vol.276 , pp. 21938-21942
    • Mahadev, K.1    Zilbering, A.2    Zhu, L.3    Goldstein, B.J.4
  • 14
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • T.C. Meng, T. Fukada, and N.K. Tonks Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo Mol Cell 9 2002 387 399
    • (2002) Mol Cell , vol.9 , pp. 387-399
    • Meng, T.C.1    Fukada, T.2    Tonks, N.K.3
  • 15
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • A. Salmeen, J.N. Andersen, M.P. Myers, T.C. Meng, J.A. Hinks, N.K. Tonks, and D. Barford Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate Nature 423 2003 769 773
    • (2003) Nature , vol.423 , pp. 769-773
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Meng, T.C.4    Hinks, J.A.5    Tonks, N.K.6    Barford, D.7
  • 16
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
    • R.L. van Montfort, M. Congreve, D. Tisi, R. Carr, and H. Jhoti Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B Nature 423 2003 773 777
    • (2003) Nature , vol.423 , pp. 773-777
    • Van Montfort, R.L.1    Congreve, M.2    Tisi, D.3    Carr, R.4    Jhoti, H.5
  • 17
    • 0033521019 scopus 로고    scopus 로고
    • Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B
    • W.C. Barrett, J.P. DeGnore, Y.F. Keng, Z.Y. Zhang, M.B. Yim, and P.B. Chock Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B J Biol Chem 274 1999 34543 34546
    • (1999) J Biol Chem , vol.274 , pp. 34543-34546
    • Barrett, W.C.1    Degnore, J.P.2    Keng, Y.F.3    Zhang, Z.Y.4    Yim, M.B.5    Chock, P.B.6
  • 18
    • 0034912744 scopus 로고    scopus 로고
    • PTEN and myotubularin: Novel phosphoinositide phosphatases
    • T. Maehama, G.E. Taylor, and J.E. Dixon PTEN and myotubularin: novel phosphoinositide phosphatases Annu Rev Biochem 70 2001 247 279
    • (2001) Annu Rev Biochem , vol.70 , pp. 247-279
    • Maehama, T.1    Taylor, G.E.2    Dixon, J.E.3
  • 19
    • 0033615538 scopus 로고    scopus 로고
    • Crystal structure of the PTEN tumor suppressor: Implications for its phosphoinositide phosphatase activity and membrane association
    • J.O. Lee, H. Yang, M.M. Georgescu, A. Di Cristofano, T. Maehama, Y. Shi, J.E. Dixon, P. Pandolfi, and N.P. Pavletich Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association Cell 99 1999 323 334
    • (1999) Cell , vol.99 , pp. 323-334
    • Lee, J.O.1    Yang, H.2    Georgescu, M.M.3    Di Cristofano, A.4    Maehama, T.5    Shi, Y.6    Dixon, J.E.7    Pandolfi, P.8    Pavletich, N.P.9
  • 20
    • 0037036358 scopus 로고    scopus 로고
    • Regulation of PTEN by superoxide and H2O2 through the reversible formation of a disulfide between Cys124 and Cys71
    • S.-R. Lee, K.-S. Yang, J. Kwon, C. Lee, W. Jeong, and S.G. Rhee Regulation of PTEN by superoxide and H2O2 through the reversible formation of a disulfide between Cys124 and Cys71 J Biol Chem 277 2002 20336 20342
    • (2002) J Biol Chem , vol.277 , pp. 20336-20342
    • Lee, S.-R.1    Yang, K.-S.2    Kwon, J.3    Lee, C.4    Jeong, W.5    Rhee, S.G.6
  • 28
    • 0025886108 scopus 로고
    • Distribution of glutathione peroxidases and glutathione reductase in rat brain mitochondria
    • E. Panfili, G. Sandri, and L. Ernster Distribution of glutathione peroxidases and glutathione reductase in rat brain mitochondria FEBS Lett 290 1991 35 37
    • (1991) FEBS Lett , vol.290 , pp. 35-37
    • Panfili, E.1    Sandri, G.2    Ernster, L.3
  • 29
    • 0028226006 scopus 로고
    • Cloning and sequencing of thiol-specific antioxidant from mammalian brain: Alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes
    • H.Z. Chae, K. Robison, L.B. Poole, G. Church, G. Storz, and S.G. Rhee Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes Proc Natl Acad Sci USA 91 1994 7017 7021
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7017-7021
    • Chae, H.Z.1    Robison, K.2    Poole, L.B.3    Church, G.4    Storz, G.5    Rhee, S.G.6
  • 33
    • 0032513056 scopus 로고    scopus 로고
    • Characterization of a mammalian peroxiredoxin that contains one conserved cysteine
    • S.W. Kang, I.C. Baines, and S.G. Rhee Characterization of a mammalian peroxiredoxin that contains one conserved cysteine J Biol Chem 273 1998 6303 6311
    • (1998) J Biol Chem , vol.273 , pp. 6303-6311
    • Kang, S.W.1    Baines, I.C.2    Rhee, S.G.3
  • 34
    • 0001015125 scopus 로고    scopus 로고
    • Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate
    • M.S. Seo, S.W. Kang, K. Kim, I.C. Baines, T.H. Lee, and S.G. Rhee Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate J Biol Chem 275 2000 20346 20354
    • (2000) J Biol Chem , vol.275 , pp. 20346-20354
    • Seo, M.S.1    Kang, S.W.2    Kim, K.3    Baines, I.C.4    Lee, T.H.5    Rhee, S.G.6
  • 35
    • 0141746553 scopus 로고    scopus 로고
    • Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-α
    • S.W. Kang, H.Z. Chae, M.S. Seo, K. Kim, I.C. Baines, and S.G. Rhee Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-α J Biol Chem 273 1998 6297 6302
    • (1998) J Biol Chem , vol.273 , pp. 6297-6302
    • Kang, S.W.1    Chae, H.Z.2    Seo, M.S.3    Kim, K.4    Baines, I.C.5    Rhee, S.G.6
  • 36
    • 0030692005 scopus 로고    scopus 로고
    • Thioredoxin peroxidase is a novel inhibitor of apoptosis with a mechanism distinct from that of Bcl-2
    • P. Zhang, B. Liu, S.W. Kang, M.S. Seo, S.G. Rhee, and L.M. Obeid Thioredoxin peroxidase is a novel inhibitor of apoptosis with a mechanism distinct from that of Bcl-2 J Biol Chem 272 1997 30615 30618
    • (1997) J Biol Chem , vol.272 , pp. 30615-30618
    • Zhang, P.1    Liu, B.2    Kang, S.W.3    Seo, M.S.4    Rhee, S.G.5    Obeid, L.M.6
  • 37
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • H.Z. Chae, S.J. Chung, and S.G. Rhee Thioredoxin-dependent peroxide reductase from yeast J Biol Chem 269 1994 27670 27678
    • (1994) J Biol Chem , vol.269 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.G.3
  • 38
    • 0028229670 scopus 로고
    • Dimerization of thiol-specific antioxidant and the essential role of cysteine 47
    • H.Z. Chae, T.B. Uhm, and S.G. Rhee Dimerization of thiol-specific antioxidant and the essential role of cysteine 47 Proc Natl Acad Sci USA 91 1994 7022 7026
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7022-7026
    • Chae, H.Z.1    Uhm, T.B.2    Rhee, S.G.3
  • 40
    • 0037064080 scopus 로고    scopus 로고
    • Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid
    • K.S. Yang, S.W. Kang, H.A. Woo, S.C. Hwang, H.Z. Chae, K. Kim, and S.G. Rhee Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid J Biol Chem 277 2002 38029 38036
    • (2002) J Biol Chem , vol.277 , pp. 38029-38036
    • Yang, K.S.1    Kang, S.W.2    Woo, H.A.3    Hwang, S.C.4    Chae, H.Z.5    Kim, K.6    Rhee, S.G.7
  • 41
    • 0037205455 scopus 로고    scopus 로고
    • Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site
    • T. Rabilloud, M. Heller, F. Gasnier, S. Luche, C. Rey, R. Aebersold, M. Benahmed, P. Louisot, and J. Lunardi Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site J Biol Chem 277 2002 19396 19401
    • (2002) J Biol Chem , vol.277 , pp. 19396-19401
    • Rabilloud, T.1    Heller, M.2    Gasnier, F.3    Luche, S.4    Rey, C.5    Aebersold, R.6    Benahmed, M.7    Louisot, P.8    Lunardi, J.9
  • 42
    • 0242668688 scopus 로고    scopus 로고
    • Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation
    • 2 is gradually reduced to the catalytically active thiol form, thus contradicting the general belief that oxidation to the sulfinic state is an irreversible process in cells.
    • (2003) Science , vol.300 , pp. 653-656
    • Woo, H.A.1    Chae, H.Z.2    Hwang, S.C.3    Yang, K.S.4    Kang, S.W.5    Kim, K.6    Rhee, S.G.7
  • 43
    • 0346850874 scopus 로고    scopus 로고
    • Reversible oxidation of the active site cysteine of peroxiredoxins to cysteine sulfinic acid. Immunoblot detection with antibodies specific for the hyperoxidized cysteine-containing sequence
    • H.A. Woo, S.W. Kang, H.K. Kim, K.S. Yang, H.Z. Chae, and S.G. Rhee Reversible oxidation of the active site cysteine of peroxiredoxins to cysteine sulfinic acid. Immunoblot detection with antibodies specific for the hyperoxidized cysteine-containing sequence J Biol Chem 278 2003 47361 47364
    • (2003) J Biol Chem , vol.278 , pp. 47361-47364
    • Woo, H.A.1    Kang, S.W.2    Kim, H.K.3    Yang, K.S.4    Chae, H.Z.5    Rhee, S.G.6
  • 44
    • 0242416188 scopus 로고    scopus 로고
    • ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin
    • B. Biteau, J. Labarre, and M.B. Toledano ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin Nature 425 2003 980 984 This paper was the first to describe sulfiredoxin and its catalysis of the conversion of highly oxidized cysteine amino acid residues back to cysteine in yeast.
    • (2003) Nature , vol.425 , pp. 980-984
    • Biteau, B.1    Labarre, J.2    Toledano, M.B.3
  • 45
    • 10944237769 scopus 로고    scopus 로고
    • Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine
    • T.-S. Chang, W. Jeong, H.A. Woo, S.M. Lee, S. Park, and S.G. Rhee Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine J Biol Chem 279 2004 50994 51001 This paper characterizes mammalian sulfiredoxin and shows that the rate of its catalytic action is very slow.
    • (2004) J Biol Chem , vol.279 , pp. 50994-51001
    • Chang, T.-S.1    Jeong, W.2    Woo, H.A.3    Lee, S.M.4    Park, S.5    Rhee, S.G.6
  • 46
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • Z.A. Wood, L.B. Poole, and P.A. Karplus Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling Science 300 2003 650 653 This paper proposes that susceptibility to hyperoxidation might be a selected regulatory feature unique to eukaryotic Prxs.
    • (2003) Science , vol.300 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 47
    • 0037466621 scopus 로고    scopus 로고
    • Biochemistry. An overoxidation journey with a return ticket
    • G. Georgiou, and L. Masip Biochemistry. An overoxidation journey with a return ticket Science 300 2003 592 594
    • (2003) Science , vol.300 , pp. 592-594
    • Georgiou, G.1    Masip, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.