메뉴 건너뛰기




Volumn 268, Issue 3, 2000, Pages 921-927

Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis

Author keywords

Apoptosis; p53; Peroxiredoxin; Reactive oxygen species (ROS); Redox; Thioredoxin peroxidase

Indexed keywords

PEROXIREDOXIN; PROTEIN P53; REACTIVE OXYGEN METABOLITE; THIOREDOXIN PEROXIDASE;

EID: 0034708217     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2000.2231     Document Type: Article
Times cited : (152)

References (40)
  • 1
    • 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
    • Chae H. Z., Robison K., Poole L. B., Church G., Storz G., Rhee S. G. 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
  • 3
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • Chae H. Z., Chung S. J., Rhee S. G. 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
  • 4
    • 0141746553 scopus 로고    scopus 로고
    • Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-α
    • Kang S. W., Chae H. Z., Seo M. S., Kim K., Baines I. C., Rhee S. G. 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
  • 5
    • 1842295744 scopus 로고    scopus 로고
    • Regulatory role for a novel human thioredoxin peroxidase in NF-κB activation
    • Jin D.-Y., Chae H. Z., Rhee S. G., Jeang K.-T. Regulatory role for a novel human thioredoxin peroxidase in NF-κB activation. J. Biol. Chem. 272:1997;30952-30961.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30952-30961
    • Jin, D.-Y.1    Chae, H.Z.2    Rhee, S.G.3    Jeang, K.-T.4
  • 6
    • 0032570772 scopus 로고    scopus 로고
    • Sequence analysis of the tryparedoxin peroxidase gene from Crithidia fasciculata and its functional expression in Escherichia coli
    • Montemartini M., Nogoceke E., Singh M., Steinert P., Flohe L., Kalisz H. M. Sequence analysis of the tryparedoxin peroxidase gene from Crithidia fasciculata and its functional expression in Escherichia coli. J. Biol. Chem. 273:1998;4864-4871.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4864-4871
    • Montemartini, M.1    Nogoceke, E.2    Singh, M.3    Steinert, P.4    Flohe, L.5    Kalisz, H.M.6
  • 7
    • 0032475983 scopus 로고    scopus 로고
    • A novel glutathione peroxidase in bovine eye: Sequence analysis, mRNA level, and translation
    • Singh A. K., Shichi H. A novel glutathione peroxidase in bovine eye: Sequence analysis, mRNA level, and translation. J. Biol. Chem. 273:1998;26171-26178.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26171-26178
    • Singh, A.K.1    Shichi, H.2
  • 8
    • 0033597885 scopus 로고    scopus 로고
    • Phospholipid hydroperoxides are substrates for non-selenium glutathione peroxidase
    • Fisher A. B., Dodia C., Manevich Y., Chen J.-W., Feinstein S. I. Phospholipid hydroperoxides are substrates for non-selenium glutathione peroxidase. J. Biol. Chem. 274:1999;21326-21334.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21326-21334
    • Fisher, A.B.1    Dodia, C.2    Manevich, Y.3    Chen, J.-W.4    Feinstein, S.I.5
  • 9
    • 0031945918 scopus 로고    scopus 로고
    • Crystal structure of a novel human peroxidase enzyme at 2.0 angstrom resolution
    • Choi H.-J., Kang S. W., Yang C.-H., Rhee S. G., Ryu S.-E. Crystal structure of a novel human peroxidase enzyme at 2.0 angstrom resolution. Nat. Struct. Biol. 5:1998;400-406.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 400-406
    • Choi, H.-J.1    Kang, S.W.2    Yang, C.-H.3    Rhee, S.G.4    Ryu, S.-E.5
  • 10
    • 0033607229 scopus 로고    scopus 로고
    • Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product
    • Hirotsu S., Abe Y., Okada K., Nagahara N., Hori H., Nishino T., Hakoshima T. Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product. Proc. Natl. Acad. Sci. USA. 96:1999;12333-12338.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12333-12338
    • Hirotsu, S.1    Abe, Y.2    Okada, K.3    Nagahara, N.4    Hori, H.5    Nishino, T.6    Hakoshima, T.7
  • 11
    • 0030889766 scopus 로고    scopus 로고
    • Murine thioredoxin peroxidase delays neuronal apoptosis and is expressed in areas of the brain most susceptible to hypoxic and ischemic injury
    • Ichimiya S., Davis J. G., O'Rourke D. M., Katsumata M., Greene M. I. Murine thioredoxin peroxidase delays neuronal apoptosis and is expressed in areas of the brain most susceptible to hypoxic and ischemic injury. DNA Cell Biol. 16:1997;311-321.
    • (1997) DNA Cell Biol. , vol.16 , pp. 311-321
    • Ichimiya, S.1    Davis, J.G.2    O'Rourke, D.M.3    Katsumata, M.4    Greene, M.I.5
  • 12
    • 0030692005 scopus 로고    scopus 로고
    • Thioredoxin peroxidase is a novel inhibitor of apoptosis with a mechanism distinct from that of Bcl-2
    • Zhang P., Liu B., Kang S. W., Seo M. S., Rhee S. G., Obeid L. M. 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
  • 13
    • 0032557424 scopus 로고    scopus 로고
    • The thiol-specific antioxidant enzyme prevents mitochondrial permeability transition: Evidence for the participation of reactive oxygen species in this mechanism
    • Kowaltowski A. J., Netto L. E., Vercesi A. E. The thiol-specific antioxidant enzyme prevents mitochondrial permeability transition: Evidence for the participation of reactive oxygen species in this mechanism. J. Biol. Chem. 273:1998;12766-12769.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12766-12769
    • Kowaltowski, A.J.1    Netto, L.E.2    Vercesi, A.E.3
  • 15
    • 0028845858 scopus 로고
    • Thioredoxin-linked "thiol peroxidase" from periplasmic space of Escherichia coli
    • Cha M.-K., Kim H.-K., Kim I.-H. Thioredoxin-linked "thiol peroxidase" from periplasmic space of Escherichia coli. J. Biol. Chem. 270:1995;28635-28641.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28635-28641
    • Cha, M.-K.1    Kim, H.-K.2    Kim, I.-H.3
  • 17
    • 0029839215 scopus 로고    scopus 로고
    • Mutation and mutagenesis of thiol peroxidase of Escherichia coli and a new type of thiol peroxidase family
    • Cha M.-K., Kim H.-K., Kim I.-H. Mutation and mutagenesis of thiol peroxidase of Escherichia coli and a new type of thiol peroxidase family. J. Bacteriol. 178:1996;5610-5614.
    • (1996) J. Bacteriol. , vol.178 , pp. 5610-5614
    • Cha, M.-K.1    Kim, H.-K.2    Kim, I.-H.3
  • 19
    • 0000300772 scopus 로고    scopus 로고
    • Purification and characterization of a second type thioredoxin peroxidase (type II TPx) from Saccharomyces cerevisiae
    • Jeong J. S., Kwon S. J., Kang S. W., Rhee S. G., Kim K. Purification and characterization of a second type thioredoxin peroxidase (type II TPx) from Saccharomyces cerevisiae. Biochemistry. 38:1999;776-783.
    • (1999) Biochemistry , vol.38 , pp. 776-783
    • Jeong, J.S.1    Kwon, S.J.2    Kang, S.W.3    Rhee, S.G.4    Kim, K.5
  • 20
    • 0033582416 scopus 로고    scopus 로고
    • A new antioxidant with alkyl hydroperoxide defense properties in yeast
    • Lee J., Spector D., Godon C., Labarre J., Toledano M. B. A new antioxidant with alkyl hydroperoxide defense properties in yeast. J. Biol. Chem. 274:1999;4537-4544.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4537-4544
    • Lee, J.1    Spector, D.2    Godon, C.3    Labarre, J.4    Toledano, M.B.5
  • 21
    • 0033538442 scopus 로고    scopus 로고
    • In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family
    • Verdoucq L., Vignols F., Jacquot J. P., Chartier Y., Meyer Y. In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family. J. Biol. Chem. 274:1999;19714-19722.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19714-19722
    • Verdoucq, L.1    Vignols, F.2    Jacquot, J.P.3    Chartier, Y.4    Meyer, Y.5
  • 22
    • 0032513056 scopus 로고    scopus 로고
    • Characterization of a mammalian peroxiredoxin that contains one conserved cysteine
    • Kang S. W., Baines I. C., Rhee S. G. 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
  • 23
    • 0030903157 scopus 로고    scopus 로고
    • The human homologue of a bovine non-selenium glutathione peroxidase is a novel keratinocyte growth factor-regulated gene
    • Frank S., Munz B., Werner S. The human homologue of a bovine non-selenium glutathione peroxidase is a novel keratinocyte growth factor-regulated gene. Oncogene. 14:1997;915-921.
    • (1997) Oncogene , vol.14 , pp. 915-921
    • Frank, S.1    Munz, B.2    Werner, S.3
  • 26
  • 29
    • 0032478547 scopus 로고    scopus 로고
    • Human T cell leukemia virus type 1 oncoprotein Tax targets the human mitotic checkpoint protein MAD1
    • Jin D.-Y., Spencer F., Jeang K.-T. Human T cell leukemia virus type 1 oncoprotein Tax targets the human mitotic checkpoint protein MAD1. Cell. 93:1998;81-91.
    • (1998) Cell , vol.93 , pp. 81-91
    • Jin, D.-Y.1    Spencer, F.2    Jeang, K.-T.3
  • 30
    • 0031773474 scopus 로고    scopus 로고
    • Preparation and assay of mammalian thioredoxin and thioredoxin reductase
    • Arner E. S. J., Zhong L., Holmgren A. Preparation and assay of mammalian thioredoxin and thioredoxin reductase. Methods Enzymol. 300:1999;226-239.
    • (1999) Methods Enzymol. , vol.300 , pp. 226-239
    • Arner, E.S.J.1    Zhong, L.2    Holmgren, A.3
  • 31
    • 0000385805 scopus 로고    scopus 로고
    • Isoforms of mammalian peroxiredoxins that reduce peroxides in presence of thioredoxin
    • Chae H. Z., Kang S. W., Rhee S. G. Isoforms of mammalian peroxiredoxins that reduce peroxides in presence of thioredoxin. Methods Enzymol. 300:1999;219-226.
    • (1999) Methods Enzymol. , vol.300 , pp. 219-226
    • Chae, H.Z.1    Kang, S.W.2    Rhee, S.G.3
  • 32
    • 0031135669 scopus 로고    scopus 로고
    • Reanalysis of published DNA sequence amplified from Cretaceous dinosaur egg fossil
    • Wang H.-L., Yan Z.-Y., Jin D.-Y. Reanalysis of published DNA sequence amplified from Cretaceous dinosaur egg fossil. Mol. Biol. Evol. 14:1997;589-591.
    • (1997) Mol. Biol. Evol. , vol.14 , pp. 589-591
    • Wang, H.-L.1    Yan, Z.-Y.2    Jin, D.-Y.3
  • 33
    • 0030829922 scopus 로고    scopus 로고
    • Identification of a single genotype of hepatitis G virus by comparison of one complete genome from a healthy carrier with eight from patients with hepatitis
    • Wang H.-L., Hou Y.-D., Jin D.-Y. Identification of a single genotype of hepatitis G virus by comparison of one complete genome from a healthy carrier with eight from patients with hepatitis. J. Gen. Virol. 78:1997;3247-3253.
    • (1997) J. Gen. Virol. , vol.78 , pp. 3247-3253
    • Wang, H.-L.1    Hou, Y.-D.2    Jin, D.-Y.3
  • 34
    • 0033229866 scopus 로고    scopus 로고
    • P53 regulates mitochondrial membrane potential through reactive oxygen species and induces cytochrome c-independent apoptosis blocked by bcl-2
    • Li P.-F., Dietz R., von Harsdorf R. p53 regulates mitochondrial membrane potential through reactive oxygen species and induces cytochrome c-independent apoptosis blocked by bcl-2. EMBO J. 18:1999;6027-6036.
    • (1999) EMBO J. , vol.18 , pp. 6027-6036
    • Li, P.-F.1    Dietz, R.2    Von Harsdorf, R.3
  • 35
    • 0033580931 scopus 로고    scopus 로고
    • Role of adapter function in oncoprotein-mediated activation of NF-κB: Human T-cell leukemia virus type I Tax interacts directly with IκB kinase γ
    • Jin D.-Y., Giordano V., Kibler K. V., Nakano H., Jeang K.-T. Role of adapter function in oncoprotein-mediated activation of NF-κB: Human T-cell leukemia virus type I Tax interacts directly with IκB kinase γ J. Biol. Chem. 274:1999;17402-17405.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17402-17405
    • Jin, D.-Y.1    Giordano, V.2    Kibler, K.V.3    Nakano, H.4    Jeang, K.-T.5
  • 36
  • 37
    • 0033106406 scopus 로고    scopus 로고
    • A novel human DNA-binding protein with sequence similarity to a subfamily of redox proteins which is able to repress RNA-polymerase-III-driven transcription of the Alu-family retroposons in vitro
    • Kropotov A., Sedova V., Ivanov V., Sazeeva N., Tomilin A., Krutilina R., Oei S. L., Griesenbeck J., Buchlow G., Tomilin N. A novel human DNA-binding protein with sequence similarity to a subfamily of redox proteins which is able to repress RNA-polymerase-III-driven transcription of the Alu-family retroposons in vitro. Eur. J. Biochem. 260:1999;336-346.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 336-346
    • Kropotov, A.1    Sedova, V.2    Ivanov, V.3    Sazeeva, N.4    Tomilin, A.5    Krutilina, R.6    Oei, S.L.7    Griesenbeck, J.8    Buchlow, G.9    Tomilin, N.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.