메뉴 건너뛰기




Volumn 100, Issue 2, 2007, Pages 213-219

Glutathiolation regulates tumor necrosis factor-α-induced caspase-3 cleavage and apoptosis: Key role for glutaredoxin in the death pathway

Author keywords

Caspase 3; Endothelial cell; Glutaredoxin; Tumor necrosis factor

Indexed keywords

CASPASE 3; CASPASE 8; CYSTEINE; GLUTAREDOXIN; RECOMBINANT PROTEIN; SERINE; SMALL INTERFERING RNA; THIOL DERIVATIVE; TRANSFERASE; TUMOR NECROSIS FACTOR ALPHA;

EID: 33846809031     PISSN: 00097330     EISSN: None     Source Type: Journal    
DOI: 10.1161/01.RES.0000256089.30318.20     Document Type: Article
Times cited : (150)

References (34)
  • 1
    • 0348230942 scopus 로고    scopus 로고
    • Glutaredoxins: Glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system
    • Fernandes AP, Holmgren A. Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Antioxid Redox Signal. 2004;6:63-74.
    • (2004) Antioxid Redox Signal , vol.6 , pp. 63-74
    • Fernandes, A.P.1    Holmgren, A.2
  • 2
    • 0027238801 scopus 로고
    • Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase
    • Gravina SA, Mieyal JJ. Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase. Biochemistry. 1993;32:3368-3376.
    • (1993) Biochemistry , vol.32 , pp. 3368-3376
    • Gravina, S.A.1    Mieyal, J.J.2
  • 3
    • 0026799490 scopus 로고
    • Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14 - S) and its mixed disulfide with glutathione
    • Bushweller JH, Aslund F, Wuthrich K, Holmgren A. Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14 - S) and its mixed disulfide with glutathione. Biochemistry. 1992;31:9288-9293.
    • (1992) Biochemistry , vol.31 , pp. 9288-9293
    • Bushweller, J.H.1    Aslund, F.2    Wuthrich, K.3    Holmgren, A.4
  • 5
    • 4344686072 scopus 로고    scopus 로고
    • Oxidative stress inhibits MEKK1 by site-specific glutathionylation in the ATP-binding domain
    • Cross JV, Templeton DJ. Oxidative stress inhibits MEKK1 by site-specific glutathionylation in the ATP-binding domain. Biochem J. 2004;381:675-683.
    • (2004) Biochem J , vol.381 , pp. 675-683
    • Cross, J.V.1    Templeton, D.J.2
  • 7
    • 0037443130 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphatase 1B in intact cells by S-nitrosothiols
    • Li S, Whorton AR. Regulation of protein tyrosine phosphatase 1B in intact cells by S-nitrosothiols. Arch Biochem Biophys. 2003;410:269-279.
    • (2003) Arch Biochem Biophys , vol.410 , pp. 269-279
    • Li, S.1    Whorton, A.R.2
  • 9
    • 2542486403 scopus 로고    scopus 로고
    • Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue
    • Reddy S, Jones AD, Cross CE, Wong PS, Van Der Vliet A. Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue. Biochem J. 2000;347(pt 3):821-827.
    • (2000) Biochem J , vol.347 , Issue.PART 3 , pp. 821-827
    • Reddy, S.1    Jones, A.D.2    Cross, C.E.3    Wong, P.S.4    Van Der Vliet, A.5
  • 10
    • 0035933127 scopus 로고    scopus 로고
    • Fluid shear stress inhibits TNF-α-alpha activation of JNK but not ERK1/2 or p38 in human umbilical vein endothelial cells: Inhibitory crosstalk among MAPK family members
    • Surapisitchat J, Hoefen RJ, Pi X, Yoshizumi M, Yan C, Berk BC. Fluid shear stress inhibits TNF-α-alpha activation of JNK but not ERK1/2 or p38 in human umbilical vein endothelial cells: inhibitory crosstalk among MAPK family members. Proc Natl Acad Sci U S A. 2001;98:6476-6481.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 6476-6481
    • Surapisitchat, J.1    Hoefen, R.J.2    Pi, X.3    Yoshizumi, M.4    Yan, C.5    Berk, B.C.6
  • 11
    • 0141506872 scopus 로고    scopus 로고
    • Chronic physiological shear stress inhibits tumor necrosis factor-induced proinflammatory responses in rabbit aorta perfused ex vivo
    • Yamawaki H, Lehoux S, Berk BC. Chronic physiological shear stress inhibits tumor necrosis factor-induced proinflammatory responses in rabbit aorta perfused ex vivo. Circulation. 2003;108:1619-1625.
    • (2003) Circulation , vol.108 , pp. 1619-1625
    • Yamawaki, H.1    Lehoux, S.2    Berk, B.C.3
  • 12
    • 0031594280 scopus 로고    scopus 로고
    • TNFalpha regulation of Fas ligand expression on the vascular endothelium modulates leukocyte extravasation
    • Sata M, Walsh K. TNFalpha regulation of Fas ligand expression on the vascular endothelium modulates leukocyte extravasation. Nat Med. 1998;4:415-420.
    • (1998) Nat Med , vol.4 , pp. 415-420
    • Sata, M.1    Walsh, K.2
  • 13
    • 2642585697 scopus 로고    scopus 로고
    • In vivo induction of endothelial apoptosis leads to vessel thrombosis and endothelial denudation: A clue to the understanding of the mechanisms of thrombotic plaque erosion
    • Durand E, Scoazec A, Lafont A, Boddaert J, Al Hajzen A, Addad F, Mirshahi M, Desnos M, Tedgui A, Mallat Z. In vivo induction of endothelial apoptosis leads to vessel thrombosis and endothelial denudation: a clue to the understanding of the mechanisms of thrombotic plaque erosion. Circulation. 2004;109:2503-2506.
    • (2004) Circulation , vol.109 , pp. 2503-2506
    • Durand, E.1    Scoazec, A.2    Lafont, A.3    Boddaert, J.4    Al Hajzen, A.5    Addad, F.6    Mirshahi, M.7    Desnos, M.8    Tedgui, A.9    Mallat, Z.10
  • 14
    • 0242656497 scopus 로고    scopus 로고
    • Death receptor-induced cell killing
    • Thorburn A. Death receptor-induced cell killing. Cell Signal. 2004;16:139-144.
    • (2004) Cell Signal , vol.16 , pp. 139-144
    • Thorburn, A.1
  • 15
    • 0034641689 scopus 로고    scopus 로고
    • Identification of oxidant-sensitive proteins: TNF-α-alpha induces protein glutathiolation
    • Sullivan DM, Wehr NB, Fergusson MM, Levine RL, Finkel T. Identification of oxidant-sensitive proteins: TNF-α-alpha induces protein glutathiolation. Biochemistry. 2000;39:11121-11128.
    • (2000) Biochemistry , vol.39 , pp. 11121-11128
    • Sullivan, D.M.1    Wehr, N.B.2    Fergusson, M.M.3    Levine, R.L.4    Finkel, T.5
  • 16
    • 0037044782 scopus 로고    scopus 로고
    • Regulation of cAMP-dependent protein kinase activity by glutathionylation
    • Humphries KM, Juliano C, Taylor SS. Regulation of cAMP-dependent protein kinase activity by glutathionylation. J Biol Chem. 2002;277:43505-43511.
    • (2002) J Biol Chem , vol.277 , pp. 43505-43511
    • Humphries, K.M.1    Juliano, C.2    Taylor, S.S.3
  • 17
    • 0025895933 scopus 로고    scopus 로고
    • Mieyal JJ, Starke DW, Gravina SA, Dothey C, Chung JS. Thioltransferase in human red blood cells: purification and properties. Biochemistry. 1991;30:6088-6097.
    • Mieyal JJ, Starke DW, Gravina SA, Dothey C, Chung JS. Thioltransferase in human red blood cells: purification and properties. Biochemistry. 1991;30:6088-6097.
  • 18
    • 0025887464 scopus 로고    scopus 로고
    • Mieyal JJ, Starke DW, Gravina SA, Hocevar BA. Thioltransferase in human red blood cells: kinetics and equilibrium. Biochemistry. 1991;30:8883-8891.
    • Mieyal JJ, Starke DW, Gravina SA, Hocevar BA. Thioltransferase in human red blood cells: kinetics and equilibrium. Biochemistry. 1991;30:8883-8891.
  • 19
    • 3343011970 scopus 로고    scopus 로고
    • Caspase activation, inhibition, and reactivation: A mechanistic view
    • Shi Y. Caspase activation, inhibition, and reactivation: a mechanistic view. Protein Sci. 2004;13:1979-1987.
    • (2004) Protein Sci , vol.13 , pp. 1979-1987
    • Shi, Y.1
  • 20
    • 2942746419 scopus 로고    scopus 로고
    • Caspase activation: Revisiting the induced proximity model
    • Shi Y. Caspase activation: revisiting the induced proximity model. Cell. 2004;117:855-858.
    • (2004) Cell , vol.117 , pp. 855-858
    • Shi, Y.1
  • 21
    • 0032497928 scopus 로고    scopus 로고
    • Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity
    • Yang Y, Jao S, Nanduri S, Starke DW, Mieyal JJ, Qin J. Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity. Biochemistry. 1998;37:17145-17156.
    • (1998) Biochemistry , vol.37 , pp. 17145-17156
    • Yang, Y.1    Jao, S.2    Nanduri, S.3    Starke, D.W.4    Mieyal, J.J.5    Qin, J.6
  • 22
    • 12544256390 scopus 로고    scopus 로고
    • Nuclear translocation of caspase-3 is dependent on its proteolytic activation and recognition of a substrate-like protein(s)
    • Kamada S, Kikkawa U, Tsujimoto Y, Hunter T. Nuclear translocation of caspase-3 is dependent on its proteolytic activation and recognition of a substrate-like protein(s). J Biol Chem. 2005;280:857-860.
    • (2005) J Biol Chem , vol.280 , pp. 857-860
    • Kamada, S.1    Kikkawa, U.2    Tsujimoto, Y.3    Hunter, T.4
  • 24
    • 33644976378 scopus 로고    scopus 로고
    • GSH depletion, protein S-glutathionylation and mitochondrial transmembrane potential hyperpolarization are early events in initiation of cell death induced by a mixture of isothiazolinones in HL60 cells
    • Di Stefano A, Frosali S, Leonini A, Ettorre A, Priora R, Di Simplicio FC, Di Simplicio P. GSH depletion, protein S-glutathionylation and mitochondrial transmembrane potential hyperpolarization are early events in initiation of cell death induced by a mixture of isothiazolinones in HL60 cells. Biochim Biophys Acta. 2006;1763:214-225.
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 214-225
    • Di Stefano, A.1    Frosali, S.2    Leonini, A.3    Ettorre, A.4    Priora, R.5    Di Simplicio, F.C.6    Di Simplicio, P.7
  • 25
    • 0035816440 scopus 로고    scopus 로고
    • Caspases are reversibly inactivated by hydrogen peroxide
    • Borutaite V, Brown GC. Caspases are reversibly inactivated by hydrogen peroxide. FEBS Lett. 2001;500:114-118.
    • (2001) FEBS Lett , vol.500 , pp. 114-118
    • Borutaite, V.1    Brown, G.C.2
  • 26
    • 0030829981 scopus 로고    scopus 로고
    • Nitric oxide modulates the c-Jun N-terminal kinase/stress-activated protein kinase activity through activating c-Jun N-terminal kinase kinase
    • Kim H, Shim J, Han PL, Choi EJ. Nitric oxide modulates the c-Jun N-terminal kinase/stress-activated protein kinase activity through activating c-Jun N-terminal kinase kinase. Biochemistry. 1997;36:13677-13681.
    • (1997) Biochemistry , vol.36 , pp. 13677-13681
    • Kim, H.1    Shim, J.2    Han, P.L.3    Choi, E.J.4
  • 28
    • 2242445273 scopus 로고    scopus 로고
    • Role of glutaredoxin in metabolic oxidative stress. Glutaredoxin as a sensor of oxidative stress mediated by H2O2
    • Song JJ, Rhee JG, Suntharalingam M, Walsh SA, Spitz DR, Lee YJ. Role of glutaredoxin in metabolic oxidative stress. Glutaredoxin as a sensor of oxidative stress mediated by H2O2. J Biol Chem. 2002;277:46566-46575.
    • (2002) J Biol Chem , vol.277 , pp. 46566-46575
    • Song, J.J.1    Rhee, J.G.2    Suntharalingam, M.3    Walsh, S.A.4    Spitz, D.R.5    Lee, Y.J.6
  • 29
    • 0346749513 scopus 로고    scopus 로고
    • Glutaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt
    • Murata H, Ihara Y, Nakamura H, Yodoi J, Sumikawa K, Kondo T. Glutaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt. J Biol Chem. 2003;278:50226-50233.
    • (2003) J Biol Chem , vol.278 , pp. 50226-50233
    • Murata, H.1    Ihara, Y.2    Nakamura, H.3    Yodoi, J.4    Sumikawa, K.5    Kondo, T.6
  • 31
    • 33645806282 scopus 로고    scopus 로고
    • S-Glutathiolation by peroxynitrite of p21ras at cysteine-118 mediates its direct activation and downstream signaling in endothelial cells
    • Clavreul N, Adachi T, Pimental DR, Ido Y, Schoneich C, Cohen RA. S-Glutathiolation by peroxynitrite of p21ras at cysteine-118 mediates its direct activation and downstream signaling in endothelial cells. FASEB J. 2006;20:518-520.
    • (2006) FASEB J , vol.20 , pp. 518-520
    • Clavreul, N.1    Adachi, T.2    Pimental, D.R.3    Ido, Y.4    Schoneich, C.5    Cohen, R.A.6
  • 32
    • 3142663363 scopus 로고    scopus 로고
    • S-Glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells
    • Adachi T, Pimentel DR, Heibeck T, Hou X, Lee YJ, Jiang B, Ido Y, Cohen RA. S-Glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells. J Biol Chem. 2004;279:29857-29862.
    • (2004) J Biol Chem , vol.279 , pp. 29857-29862
    • Adachi, T.1    Pimentel, D.R.2    Heibeck, T.3    Hou, X.4    Lee, Y.J.5    Jiang, B.6    Ido, Y.7    Cohen, R.A.8
  • 34
    • 12344328181 scopus 로고    scopus 로고
    • Inflammation and Atherosclerosis
    • Steffens S, Mach F. Inflammation and Atherosclerosis. Herz. 2004;29:741-748.
    • (2004) Herz , vol.29 , pp. 741-748
    • Steffens, S.1    Mach, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.