메뉴 건너뛰기




Volumn 40, Issue 2, 2006, Pages 275-284

Specific protein interaction of human Pag with Omi/HtrA2 and the activation of the protease activity of Omi/HtrA2

Author keywords

Cell death; Human PAG; Molecular switch; Omi HtrA2; Oxidative stress; PDZ domain; Protease activity; Protein interaction; TSA AhpC family

Indexed keywords

GENE PRODUCT; PDZ PROTEIN; PROTEIN PAG; PROTEINASE; SERINE PROTEINASE OMI; THIOREDOXIN PEROXIDASE; UNCLASSIFIED DRUG;

EID: 30344475860     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2005.08.029     Document Type: Article
Times cited : (16)

References (43)
  • 2
    • 0023929362 scopus 로고
    • The isolation and purification of a specific "protector" protein which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixed-function oxidation system
    • K. Kim, I.H. Kim, K.Y. Lee, S.G. Rhee, and E.R. Stadtman The isolation and purification of a specific "protector" protein which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixed-function oxidation system J. Biol. Chem. 263 1988 4704 4711
    • (1988) J. Biol. Chem. , vol.263 , pp. 4704-4711
    • Kim, K.1    Kim, I.H.2    Lee, K.Y.3    Rhee, S.G.4    Stadtman, E.R.5
  • 4
    • 0027323871 scopus 로고
    • Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae
    • H.J. Chae, I.H. Kim, K. Kim, and S.G. Rhee Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae J. Biol. Chem. 268 1993 16815 16821
    • (1993) J. Biol. Chem. , vol.268 , pp. 16815-16821
    • Chae, H.J.1    Kim, I.H.2    Kim, K.3    Rhee, S.G.4
  • 5
    • 0027259213 scopus 로고
    • Removals of hydrogen peroxide and hydroxyl radical by thiol-specific antioxidant protein as a possible role in vivo
    • Y.S. Lim, M.K. Cha, T.B. Uhm, J.W. Park, K. Kim, and I.H. Kim Removals of hydrogen peroxide and hydroxyl radical by thiol-specific antioxidant protein as a possible role in vivo Biochem. Biophys. Res. Commun. 192 1993 273 280
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 273-280
    • Lim, Y.S.1    Cha, M.K.2    Uhm, T.B.3    Park, J.W.4    Kim, K.5    Kim, I.H.6
  • 6
    • 0028283815 scopus 로고
    • Inhibition of metal-catalyzed oxidation systems by a yeast protector protein in the presence of thioredoxin
    • S.J. Kwon, J.W. Park, W.K. Choi, I.H. Kim, and K. Kim Inhibition of metal-catalyzed oxidation systems by a yeast protector protein in the presence of thioredoxin Biochem. Biophys. Res. Commun. 201 1994 8 15
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 8-15
    • Kwon, S.J.1    Park, J.W.2    Choi, W.K.3    Kim, I.H.4    Kim, K.5
  • 7
    • 0028297121 scopus 로고
    • The thiol-specific antioxidant protein from human brain: Gene cloning and analysis of conserved cysteine regions
    • Y.S. Lim, M.K. Cha, H.K. Kim, and I.H. Kim The thiol-specific antioxidant protein from human brain: gene cloning and analysis of conserved cysteine regions Gene (Amst.) 140 1994 279 284
    • (1994) Gene (Amst.) , vol.140 , pp. 279-284
    • Lim, Y.S.1    Cha, M.K.2    Kim, H.K.3    Kim, I.H.4
  • 8
    • 0028340680 scopus 로고
    • Purification and characterization of thiol-specific antioxidant protein from human red blood cell: A new type of antioxidant protein
    • Y.S. Lim, M.K. Cha, C.H. Yun, H.K. Kim, K. Kim, and I.H. Kim Purification and characterization of thiol-specific antioxidant protein from human red blood cell: a new type of antioxidant protein Biochem. Biophys. Res. Commun. 199 1994 199 206
    • (1994) Biochem. Biophys. Res. Commun. , vol.199 , pp. 199-206
    • Lim, Y.S.1    Cha, M.K.2    Yun, C.H.3    Kim, H.K.4    Kim, K.5    Kim, I.H.6
  • 9
    • 0028845858 scopus 로고
    • Thioredoxin-linked "thiol peroxidase" from periplasmic space of Escherichia coli
    • M.K. Cha, H.K. Kim, and I.H. Kim Thioredoxin-linked "thiol peroxidase" from periplasmic space of Escherichia coli J. Biol. Chem. 270 1995 28635 28640
    • (1995) J. Biol. Chem. , vol.270 , pp. 28635-28640
    • Cha, M.K.1    Kim, H.K.2    Kim, I.H.3
  • 10
    • 0029839215 scopus 로고    scopus 로고
    • Mutation and mutagenesis of thiol peroxidase of Escherichia coli and a new type of thiol peroxidase family
    • M.K. Cha, H.K. Kim, and I.H. Kim 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
  • 11
    • 0030542040 scopus 로고    scopus 로고
    • Purification and characterization of thiol-specific antioxidant protein from human liver: A Mer5-like human isoenzyme
    • M.K. Cha, and I.H. Kim Purification and characterization of thiol-specific antioxidant protein from human liver: a Mer5-like human isoenzyme J. Biochem. Mol. Biol. 29 1996 236 240
    • (1996) J. Biochem. Mol. Biol. , vol.29 , pp. 236-240
    • Cha, M.K.1    Kim, I.H.2
  • 12
    • 0032513056 scopus 로고    scopus 로고
    • Characterization of mammalian peroxiredoxin that contains one conserved cysteine
    • S.W. Kang, I.C. Baines, and S.G. Rhee Characterization of 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
  • 13
    • 0034399152 scopus 로고    scopus 로고
    • A new member of human TSA/AhpC as thioredoxin-dependent thiol peroxidase
    • W. Jeong, M.K. Cha, and I.H. Kim A new member of human TSA/AhpC as thioredoxin-dependent thiol peroxidase J. Biochem. Mol. Biol. 33 2000 234 241
    • (2000) J. Biochem. Mol. Biol. , vol.33 , pp. 234-241
    • Jeong, W.1    Cha, M.K.2    Kim, I.H.3
  • 14
    • 0034723165 scopus 로고    scopus 로고
    • Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin comigratory protein (BCP) as a new member of the thiol-specific antioxidant protein (TSA)/alkyl hydroperoxide peroxidase C (AhpC) family
    • W. Jeong, M.K. Cha, and I.H. Kim Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin comigratory protein (BCP) as a new member of the thiol-specific antioxidant protein (TSA)/alkyl hydroperoxide peroxidase C (AhpC) family J. Biol. Chem. 275 2000 2924 2930
    • (2000) J. Biol. Chem. , vol.275 , pp. 2924-2930
    • Jeong, W.1    Cha, M.K.2    Kim, I.H.3
  • 15
    • 0000056465 scopus 로고    scopus 로고
    • Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae
    • S.K. Park, M.K. Cha, W. Jeong, and I.H. Kim Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae J. Biol. Chem. 275 2000 5723 5732
    • (2000) J. Biol. Chem. , vol.275 , pp. 5723-5732
    • Park, S.K.1    Cha, M.K.2    Jeong, W.3    Kim, I.H.4
  • 18
    • 0034737541 scopus 로고    scopus 로고
    • Peroxiredoxin I (macrophage 23 kDa stress protein) is highly and widely expressed in the rat nervous system
    • H. Mizusawa, T. Ishii, and S. Bannai Peroxiredoxin I (macrophage 23 kDa stress protein) is highly and widely expressed in the rat nervous system Neurosci. Lett. 283 2000 57 60
    • (2000) Neurosci. Lett. , vol.283 , pp. 57-60
    • Mizusawa, H.1    Ishii, T.2    Bannai, S.3
  • 20
    • 0001952829 scopus 로고    scopus 로고
    • Redox signaling: Hydrogen peroxide as intracellular messenger
    • S.G. Rhee Redox signaling: hydrogen peroxide as intracellular messenger Exp. Mol. Med. 31 1999 53 59
    • (1999) Exp. Mol. Med. , vol.31 , pp. 53-59
    • Rhee, S.G.1
  • 21
    • 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
  • 22
    • 0034533082 scopus 로고    scopus 로고
    • Reactive oxygen species in cell signaling
    • V.J. Thannickal, and B.L. Fanburg Reactive oxygen species in cell signaling Am. J. Physiol. 279 2000 L1005 L1028
    • (2000) Am. J. Physiol. , vol.279
    • Thannickal, V.J.1    Fanburg, B.L.2
  • 23
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1
    • R. Schreck, P. Rieber, and P.A. Baeuerle Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1 EMBO J. 10 1991 2247 2258
    • (1991) EMBO J. , vol.10 , pp. 2247-2258
    • Schreck, R.1    Rieber, P.2    Baeuerle, P.A.3
  • 24
    • 0029020218 scopus 로고
    • Involvement of reactive oxygen species in cytokine and growth factor induction of c-fos expression in chondrocytes
    • Y.Y. Lo, and T.F. Cruz Involvement of reactive oxygen species in cytokine and growth factor induction of c-fos expression in chondrocytes J. Biol. Chem. 270 1995 11727 11730
    • (1995) J. Biol. Chem. , vol.270 , pp. 11727-11730
    • Lo, Y.Y.1    Cruz, T.F.2
  • 25
    • 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
  • 26
    • 0035877633 scopus 로고    scopus 로고
    • Insulin-stimulated hydrogen peroxide reversible 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 reversible 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
  • 27
    • 1842295744 scopus 로고    scopus 로고
    • Regulation role for a novel human thioredoxin peroxidase in NF-Kb activation
    • Dong-Yan Jin, Ho Zoon Chae, Sue Goo Rhee, and Kuan-The Jeang Regulation role for a novel human thioredoxin peroxidase in NF-Kb activation J. Biol. Chem. 272 1997 30952 30961
    • (1997) J. Biol. Chem. , vol.272 , pp. 30952-30961
    • Dong-Yan, J.1    Ho Zoon, C.2    Sue Goo, R.3    Kuan-The, J.4
  • 28
    • 0041816362 scopus 로고    scopus 로고
    • The protein interaction of Saccharomyces cerevisiae cytoplasmic thiol peroxidase II whit SFH2p and its in vivo function
    • M.K. Cha, S.K. Hong, Y.M. Oh, and I.H. Kim The protein interaction of Saccharomyces cerevisiae cytoplasmic thiol peroxidase II whit SFH2p and its in vivo function J. Biol. Chem. 278 2003 34952 34958
    • (2003) J. Biol. Chem. , vol.278 , pp. 34952-34958
    • Cha, M.K.1    Hong, S.K.2    Oh, Y.M.3    Kim, I.H.4
  • 29
    • 0030803669 scopus 로고    scopus 로고
    • The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity
    • S.T. Wen, and R.A. Van Etten The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity Genes Dev. 11 1997 2456 2467
    • (1997) Genes Dev. , vol.11 , pp. 2456-2467
    • Wen, S.T.1    Van Etten, R.A.2
  • 30
    • 0037044804 scopus 로고    scopus 로고
    • Pag, a putative tumor suppressor, interacts with the Myc BoxII domain of c-Myc and selectively alters its biological function and target gene expression
    • Z.M. Mu, X.Y. Yin, and E.V. Prochownik Pag, a putative tumor suppressor, interacts with the Myc BoxII domain of c-Myc and selectively alters its biological function and target gene expression J. Biol. Chem. 277 2002 43175 43184
    • (2002) J. Biol. Chem. , vol.277 , pp. 43175-43184
    • Mu, Z.M.1    Yin, X.Y.2    Prochownik, E.V.3
  • 34
    • 0026009332 scopus 로고
    • Lipid hydroperoxide measurement by oxidation of Fe2+ in the presence of xylenol orange. Comparison with the TBA assay and an iodometric method
    • Z.Y. Jiang, A.C. Woollard, and S.P. Wolff Lipid hydroperoxide measurement by oxidation of Fe2+ in the presence of xylenol orange. Comparison with the TBA assay and an iodometric method Lipid 26 1991 853 856
    • (1991) Lipid , vol.26 , pp. 853-856
    • Jiang, Z.Y.1    Woollard, A.C.2    Wolff, S.P.3
  • 36
    • 0034723201 scopus 로고    scopus 로고
    • Characterization of a novel human serine protease that has extensive homology to bacterial heat shock endoprotease HtrA and is regulated by kidney ischemia
    • L. Faccio, C. Fusco, A. Chen, S. Martinotti, J.V. Bonventre, and A.J. Zervos Characterization of a novel human serine protease that has extensive homology to bacterial heat shock endoprotease HtrA and is regulated by kidney ischemia J. Biol. Chem. 275 2000 2581 2588
    • (2000) J. Biol. Chem. , vol.275 , pp. 2581-2588
    • Faccio, L.1    Fusco, C.2    Chen, A.3    Martinotti, S.4    Bonventre, J.V.5    Zervos, A.J.6
  • 37
    • 0033607229 scopus 로고    scopus 로고
    • Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product
    • S. Hirotsu, Y. Abe, K. Okada, N. Nagahara, H. Hori, T. Nishino, and T. Hakoshima 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
  • 38
    • 0012927828 scopus 로고    scopus 로고
    • PDZ domain proteins: Plug and play!
    • C. Nourry, S.G. Grant, and J.P. Borg PDZ domain proteins: plug and play! Sci STKE 179 2003 RE7
    • (2003) Sci STKE , vol.179 , pp. 7
    • Nourry, C.1    Grant, S.G.2    Borg, J.P.3
  • 39
    • 0027247446 scopus 로고
    • A Human cDNA corresponding to a gene overexpressed during cell proliferation encodes a product sharing homology with amoebic and bacterial proteins
    • M.T. Prosperi, D. Ferbus, I. Karczinski, and G. Goubin A Human cDNA corresponding to a gene overexpressed during cell proliferation encodes a product sharing homology with amoebic and bacterial proteins J. Biol. Chem. 268 1993 11050 11056
    • (1993) J. Biol. Chem. , vol.268 , pp. 11050-11056
    • Prosperi, M.T.1    Ferbus, D.2    Karczinski, I.3    Goubin, G.4
  • 41
    • 13544272571 scopus 로고    scopus 로고
    • Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-Cys peroxiredoxins
    • H.A. Woo, W. Jeong, T.S. Chang, K.J. Park, S.J. Park, J.S. Yang, and S.G. Rhee Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-Cys peroxiredoxins J. Biol. Chem. 280 2005 3125 3128
    • (2005) J. Biol. Chem. , vol.280 , pp. 3125-3128
    • Woo, H.A.1    Jeong, W.2    Chang, T.S.3    Park, K.J.4    Park, S.J.5    Yang, J.S.6    Rhee, S.G.7
  • 42
    • 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 80 984
    • (2003) Nature , vol.425 , pp. 80-984
    • Biteau, B.1    Labarre, J.2    Toledano, M.B.3
  • 43
    • 0242668688 scopus 로고    scopus 로고
    • Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation
    • H.A. Woo, H.Z. Chae, S.C. Hwang, K.-S. Yang, S.W. Kang, K. Kim, and S.G. Rhee Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation Science 300 2003 653 656
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.