메뉴 건너뛰기




Volumn 1773, Issue 6, 2007, Pages 945-953

Aqueous peroxyl radical exposure to THP-1 cells causes glutathione loss followed by protein oxidation and cell death without increased caspase-3 activity

Author keywords

AAPH; Apoptosis; Caspase; Cell death; Glutathione; Macrophage; Protein oxidation; THP 1

Indexed keywords

AZO COMPOUND; BUTHIONINE SULFOXIMINE; CASPASE 3; CYTOCHROME C; FREE RADICAL; GLUTATHIONE; HYDROXYL GROUP; LIPOCORTIN 5; PEROXY RADICAL; PROPIDIUM IODIDE;

EID: 34249738107     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2007.04.001     Document Type: Article
Times cited : (16)

References (52)
  • 2
    • 0000061171 scopus 로고
    • Modification of low density lipoprotein by endothelial cells involves lipid peroxidation and degradation of low density lipoprotein phospholipids
    • Steinbrecher U.P., Parthasarathy S., Leake D.S., Witztum J.L., and Steinberg D. Modification of low density lipoprotein by endothelial cells involves lipid peroxidation and degradation of low density lipoprotein phospholipids. Proc. Natl. Acad. Sci. U. S. A. 81 (1984) 3883-3887
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 3883-3887
    • Steinbrecher, U.P.1    Parthasarathy, S.2    Leake, D.S.3    Witztum, J.L.4    Steinberg, D.5
  • 6
    • 0023144962 scopus 로고
    • Inactivation of enzymes and oxidative modification of proteins by stimulated neutrophils
    • Oliver C.N. Inactivation of enzymes and oxidative modification of proteins by stimulated neutrophils. Arch. Biochem. Biophys. 253 (1987) 62-72
    • (1987) Arch. Biochem. Biophys. , vol.253 , pp. 62-72
    • Oliver, C.N.1
  • 7
    • 0030915481 scopus 로고    scopus 로고
    • Myeloperoxidase: a key regulator of neutrophil oxidant production
    • Kettle A.J., and Winterbourn C.C. Myeloperoxidase: a key regulator of neutrophil oxidant production. Redox Rep. 3 (1997) 3-15
    • (1997) Redox Rep. , vol.3 , pp. 3-15
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 8
    • 0034080482 scopus 로고    scopus 로고
    • The dissection of oxidative changes in human blood serum and U937 cells exposed to free radicals
    • Gebicki J.M., Collins J., Gay C., Duggan S., and Gieseg S.P. The dissection of oxidative changes in human blood serum and U937 cells exposed to free radicals. Redox Rep. 5 (2000) 55-56
    • (2000) Redox Rep. , vol.5 , pp. 55-56
    • Gebicki, J.M.1    Collins, J.2    Gay, C.3    Duggan, S.4    Gieseg, S.P.5
  • 9
    • 0034663470 scopus 로고    scopus 로고
    • Peroxidation of proteins before lipids in U937 cells exposed to peroxyl radicals
    • Gieseg S.P., Duggan S., and Gebicki J.M. Peroxidation of proteins before lipids in U937 cells exposed to peroxyl radicals. Biochem. J. 350 (2000) 215-218
    • (2000) Biochem. J. , vol.350 , pp. 215-218
    • Gieseg, S.P.1    Duggan, S.2    Gebicki, J.M.3
  • 10
    • 4143092694 scopus 로고    scopus 로고
    • Proteins are major initial cell targets of hydroxyl free radicals
    • Du J., and Gebicki J.M. Proteins are major initial cell targets of hydroxyl free radicals. Int. J. Biochem. Cell Biol. 36 (2004) 2334-2343
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2334-2343
    • Du, J.1    Gebicki, J.M.2
  • 11
    • 0033560051 scopus 로고    scopus 로고
    • Crosslinking of DNA and proteins induced by protein hydroperoxides
    • Gebicki S., and Gebicki J.M. Crosslinking of DNA and proteins induced by protein hydroperoxides. Biochem. J. 338 (1999) 629-636
    • (1999) Biochem. J. , vol.338 , pp. 629-636
    • Gebicki, S.1    Gebicki, J.M.2
  • 12
    • 0037063365 scopus 로고    scopus 로고
    • Inactivation of cellular caspases by peptide-derived tryptophan and tyrosine peroxides
    • Hampton M.B., Morgan P.E., and Davies M.J. Inactivation of cellular caspases by peptide-derived tryptophan and tyrosine peroxides. FEBS Lett. 527 (2002) 289-292
    • (2002) FEBS Lett. , vol.527 , pp. 289-292
    • Hampton, M.B.1    Morgan, P.E.2    Davies, M.J.3
  • 13
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean R.T., Fu S., Stocker R., and Davies M.J. Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 324 (1997) 1-18
    • (1997) Biochem. J. , vol.324 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3    Davies, M.J.4
  • 14
    • 0021927593 scopus 로고
    • Oxidation of biological membranes and its inhibition. Free radical chain oxidation of erythrocyte ghost membranes by oxygen
    • Yamamoto Y., Niki E., Eguchi J., Kamiya Y., and Shimasaki H. Oxidation of biological membranes and its inhibition. Free radical chain oxidation of erythrocyte ghost membranes by oxygen. Biochim. Biophys. Acta 819 (1985) 29-36
    • (1985) Biochim. Biophys. Acta , vol.819 , pp. 29-36
    • Yamamoto, Y.1    Niki, E.2    Eguchi, J.3    Kamiya, Y.4    Shimasaki, H.5
  • 15
    • 0034905658 scopus 로고    scopus 로고
    • Enhancement of hyperthermia-induced apoptosis by a free radical initiator, 2,2′-azobis (2-amidinopropane) dihydrochloride, in human histiocytic lymphoma U937 cells
    • Li F.J., Kondo T., Zhao Q.L., Tanabe K., Ogawa R., Li M., and Arai Y. Enhancement of hyperthermia-induced apoptosis by a free radical initiator, 2,2′-azobis (2-amidinopropane) dihydrochloride, in human histiocytic lymphoma U937 cells. Free Radic. Res. 35 (2001) 281-299
    • (2001) Free Radic. Res. , vol.35 , pp. 281-299
    • Li, F.J.1    Kondo, T.2    Zhao, Q.L.3    Tanabe, K.4    Ogawa, R.5    Li, M.6    Arai, Y.7
  • 16
    • 0037135712 scopus 로고    scopus 로고
    • Protein and thiol oxidation in cells exposed to peroxyl radicals, is inhibited by the macrophage synthesised pterin 7,8-dihydroneopterin
    • Gieseg S.P., Duggan S., Rait C., and Platt A. Protein and thiol oxidation in cells exposed to peroxyl radicals, is inhibited by the macrophage synthesised pterin 7,8-dihydroneopterin. Biochim. Biophys. Acta 1591 (2002) 139-145
    • (2002) Biochim. Biophys. Acta , vol.1591 , pp. 139-145
    • Gieseg, S.P.1    Duggan, S.2    Rait, C.3    Platt, A.4
  • 17
    • 0036958539 scopus 로고    scopus 로고
    • Lipid peroxidation-mediated cytotoxicity and DNA damage in U937 cells
    • Park J.E., Yang J.H., Yoon S.J., Lee J.H., Yang E.S., and Park J.W. Lipid peroxidation-mediated cytotoxicity and DNA damage in U937 cells. Biochimie 84 (2002) 1198-1204
    • (2002) Biochimie , vol.84 , pp. 1198-1204
    • Park, J.E.1    Yang, J.H.2    Yoon, S.J.3    Lee, J.H.4    Yang, E.S.5    Park, J.W.6
  • 18
    • 0032830131 scopus 로고    scopus 로고
    • Effects of reactive oxygen species on brain synaptic plasma membrane Ca2+-ATPase
    • Zaidi A., and Michaelis M.L. Effects of reactive oxygen species on brain synaptic plasma membrane Ca2+-ATPase. Free Radic. Biol. Med. 27 (1999) 810-821
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 810-821
    • Zaidi, A.1    Michaelis, M.L.2
  • 19
  • 20
    • 0030771213 scopus 로고    scopus 로고
    • Apoptotic cell death and caspase 3 (Cpp32) activation induced by calcium ionophore at low concentrations and their prevention by nerve growth factor in Pc12 cells
    • Takadera T., and Ohyashiki T. Apoptotic cell death and caspase 3 (Cpp32) activation induced by calcium ionophore at low concentrations and their prevention by nerve growth factor in Pc12 cells. Eur. J. Biochem. 249 (1997) 8-12
    • (1997) Eur. J. Biochem. , vol.249 , pp. 8-12
    • Takadera, T.1    Ohyashiki, T.2
  • 21
    • 0346666709 scopus 로고    scopus 로고
    • A lipophilic free radical initiator, 2,2'-azobis (2,4-dimethylvaleronitrile) (AMVN) enhances caspase-dependent apoptosis induced by hyperthermia
    • Li F.J., Kondo T., Zhao Q.L., Hayashi Y., Ogawa R., Cui Z.G., and Feril J.L.B. A lipophilic free radical initiator, 2,2'-azobis (2,4-dimethylvaleronitrile) (AMVN) enhances caspase-dependent apoptosis induced by hyperthermia. Int. J. Hypertherm. 19 (2003) 165-177
    • (2003) Int. J. Hypertherm. , vol.19 , pp. 165-177
    • Li, F.J.1    Kondo, T.2    Zhao, Q.L.3    Hayashi, Y.4    Ogawa, R.5    Cui, Z.G.6    Feril, J.L.B.7
  • 22
    • 0035126008 scopus 로고    scopus 로고
    • Activation of caspase-3 by lysosomal cysteine proteases and its role in 2,2′-azobis-(2-amidinopropane) dihydrochloride (AAPH)-induced apoptosis in HL-60 cells
    • Ishisaka R., Kanno T., Akiyama J., Yoshioka T., Utsumi K., and Utsumi T. Activation of caspase-3 by lysosomal cysteine proteases and its role in 2,2′-azobis-(2-amidinopropane) dihydrochloride (AAPH)-induced apoptosis in HL-60 cells. J. Biochem. 129 (2001) 35-41
    • (2001) J. Biochem. , vol.129 , pp. 35-41
    • Ishisaka, R.1    Kanno, T.2    Akiyama, J.3    Yoshioka, T.4    Utsumi, K.5    Utsumi, T.6
  • 23
    • 9644294591 scopus 로고    scopus 로고
    • Oxidised LDL triggers phosphatidylserine exposure in human monocyte cell lines by both caspase-dependent and independent mechanisms
    • Baird S.K., Hampton M., and Gieseg S.P. Oxidised LDL triggers phosphatidylserine exposure in human monocyte cell lines by both caspase-dependent and independent mechanisms. FEBS Lett. 578 (2004) 169-174
    • (2004) FEBS Lett. , vol.578 , pp. 169-174
    • Baird, S.K.1    Hampton, M.2    Gieseg, S.P.3
  • 24
    • 24944590455 scopus 로고    scopus 로고
    • OxLDL induced cell death is inhibited by the macrophage synthesised pterin, 7,8-dihydroneopterin, in U937 cells but not THP-1 cells
    • Baird S.K., Reid L., Hampton M., and Gieseg S.P. OxLDL induced cell death is inhibited by the macrophage synthesised pterin, 7,8-dihydroneopterin, in U937 cells but not THP-1 cells. Biochim. Biophys. Acta 1745 (2005) 361-369
    • (2005) Biochim. Biophys. Acta , vol.1745 , pp. 361-369
    • Baird, S.K.1    Reid, L.2    Hampton, M.3    Gieseg, S.P.4
  • 26
    • 0031577532 scopus 로고    scopus 로고
    • Rapid and specific efflux of glutathione before hepatocyte injury induced by hypoxia
    • Khan S., and Obrien P.J. Rapid and specific efflux of glutathione before hepatocyte injury induced by hypoxia. Biochem. Biophys. Res. Commun. 238 (1997) 320-322
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 320-322
    • Khan, S.1    Obrien, P.J.2
  • 28
    • 0034991034 scopus 로고    scopus 로고
    • Signalling apoptosis: a radical approach
    • Carmody R.J., and Cotter T.G. Signalling apoptosis: a radical approach. Redox Rep. 6 (2001) 77-90
    • (2001) Redox Rep. , vol.6 , pp. 77-90
    • Carmody, R.J.1    Cotter, T.G.2
  • 29
    • 0037273831 scopus 로고    scopus 로고
    • Protein thiol inhibited protein hydroperoxide formation
    • Platt A.A., and Gieseg S.P. Protein thiol inhibited protein hydroperoxide formation. Redox Rep. 8 (2003) 81-86
    • (2003) Redox Rep. , vol.8 , pp. 81-86
    • Platt, A.A.1    Gieseg, S.P.2
  • 31
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 65 (1983) 55-63
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 32
    • 0029043888 scopus 로고
    • A novel assay for apoptosis-flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein-labeled annexin-V
    • Vermes I., Haanen C., Steffensnakken H., and Reutelingsperger C. A novel assay for apoptosis-flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein-labeled annexin-V. J. Immunol. Methods 184 (1995) 39-51
    • (1995) J. Immunol. Methods , vol.184 , pp. 39-51
    • Vermes, I.1    Haanen, C.2    Steffensnakken, H.3    Reutelingsperger, C.4
  • 33
    • 0022818865 scopus 로고
    • Methodologies for the application of monobromobimane to the simultaneous analysis of soluble and protein thiol components of biological systems
    • Cotgreave I.A., and Moldeus P. Methodologies for the application of monobromobimane to the simultaneous analysis of soluble and protein thiol components of biological systems. J. Biochem. Biophys. Methods 13 (1986) 231-249
    • (1986) J. Biochem. Biophys. Methods , vol.13 , pp. 231-249
    • Cotgreave, I.A.1    Moldeus, P.2
  • 34
    • 0028283301 scopus 로고
    • Measurement of protein thiol groups and glutathione in plasma
    • Hu M. Measurement of protein thiol groups and glutathione in plasma. Methods Enzymol. 233 (1994) 380-385
    • (1994) Methods Enzymol. , vol.233 , pp. 380-385
    • Hu, M.1
  • 35
    • 0037165630 scopus 로고    scopus 로고
    • Interaction with substrate sensitises caspase-3 to inactivation by hydrogen peroxide
    • Hampton M.B., Stamenkovic I., and Winterbourn C.C. Interaction with substrate sensitises caspase-3 to inactivation by hydrogen peroxide. FEBS Lett. 517 (2002) 229-232
    • (2002) FEBS Lett. , vol.517 , pp. 229-232
    • Hampton, M.B.1    Stamenkovic, I.2    Winterbourn, C.C.3
  • 36
    • 0030030643 scopus 로고    scopus 로고
    • Hypothesis: UK consumption of dietary lipid hydroperoxides-A possible contribution to atherosclerosis
    • Wolff S., and Nourooz-Zadeh J. Hypothesis: UK consumption of dietary lipid hydroperoxides-A possible contribution to atherosclerosis. Atherosclerosis 119 (1996) 261-263
    • (1996) Atherosclerosis , vol.119 , pp. 261-263
    • Wolff, S.1    Nourooz-Zadeh, J.2
  • 37
    • 0033543516 scopus 로고    scopus 로고
    • Hydroperoxide assay with the Ferric-Xylenol orange complex
    • Gay C., Collins J., and Gebicki J. Hydroperoxide assay with the Ferric-Xylenol orange complex. Anal. Biochem. 273 (1999) 149-155
    • (1999) Anal. Biochem. , vol.273 , pp. 149-155
    • Gay, C.1    Collins, J.2    Gebicki, J.3
  • 38
    • 0028426899 scopus 로고
    • Oxidative damage to plasma proteins in adult respiratory distress syndrome
    • Quinlan G.J., Evans T.W., and Gutteridge J.M.C. Oxidative damage to plasma proteins in adult respiratory distress syndrome. Free Radic. Res. 20 (1994) 289-298
    • (1994) Free Radic. Res. , vol.20 , pp. 289-298
    • Quinlan, G.J.1    Evans, T.W.2    Gutteridge, J.M.C.3
  • 39
    • 1842685103 scopus 로고    scopus 로고
    • Markers of protein oxidation: different oxidants give rise to variable yields of bound and released carbonyl products
    • Headlam H.A., and Davies M.J. Markers of protein oxidation: different oxidants give rise to variable yields of bound and released carbonyl products. Free Radic. Biol. Med. 36 (2004) 1175-1184
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 1175-1184
    • Headlam, H.A.1    Davies, M.J.2
  • 41
    • 0034915429 scopus 로고    scopus 로고
    • Inhibition of protein oxidation by the macrophage synthesised antioxidant 7,8-dihydroneopterin
    • Duggan S., Rait C., Gebicki J.M., and Gieseg S.P. Inhibition of protein oxidation by the macrophage synthesised antioxidant 7,8-dihydroneopterin. Redox Rep. 6 (2001) 188-190
    • (2001) Redox Rep. , vol.6 , pp. 188-190
    • Duggan, S.1    Rait, C.2    Gebicki, J.M.3    Gieseg, S.P.4
  • 42
    • 0037218567 scopus 로고    scopus 로고
    • Cell-mediated reduction of protein and peptide hydroperoxides to reactive free radicals
    • Headlam H.A., and Davies M.J. Cell-mediated reduction of protein and peptide hydroperoxides to reactive free radicals. Free Radic. Biol. Med. 34 (2003) 44-55
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 44-55
    • Headlam, H.A.1    Davies, M.J.2
  • 43
    • 0027935268 scopus 로고
    • The redox couple between glutathione and ascorbic acid: a chemical and physiological perspective
    • Winkler B.S., Orselli S.M., and Rex T.S. The redox couple between glutathione and ascorbic acid: a chemical and physiological perspective. Free Radic. Biol. Med. 7 (1994) 333-349
    • (1994) Free Radic. Biol. Med. , vol.7 , pp. 333-349
    • Winkler, B.S.1    Orselli, S.M.2    Rex, T.S.3
  • 44
    • 0036591861 scopus 로고    scopus 로고
    • Beta-scission of side-chain alkoxyl radicals on peptides and proteins results in the loss of side-chains as aldehydes and ketones
    • Headlam H.A., and Davies M.J. Beta-scission of side-chain alkoxyl radicals on peptides and proteins results in the loss of side-chains as aldehydes and ketones. Free Radic. Biol. Med. 32 (2002) 1171-1184
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 1171-1184
    • Headlam, H.A.1    Davies, M.J.2
  • 46
    • 0030890790 scopus 로고    scopus 로고
    • Processing/activation of at least four interleukin-1 beta converting enzyme-like proteases occurs during the execution phase of apoptosis in human monocytic tumor cells
    • Macfarlane M., Cain K., Sun X.M., Alnemri E.S., and Cohen G.M. Processing/activation of at least four interleukin-1 beta converting enzyme-like proteases occurs during the execution phase of apoptosis in human monocytic tumor cells. J. Cell Biol. 137 (1997) 469-479
    • (1997) J. Cell Biol. , vol.137 , pp. 469-479
    • Macfarlane, M.1    Cain, K.2    Sun, X.M.3    Alnemri, E.S.4    Cohen, G.M.5
  • 47
    • 2442540299 scopus 로고    scopus 로고
    • Pro-apoptotic proteins released from the mitochondria regulate the protein composition and caspase-processing activity of the native Apaf-1/Caspase-9 apoptosome complex
    • Twiddy D., Brown D.G., Adrain C., Jukes R., Martin S.J., Cohen G.M., Macfarlane M., and Cain K. Pro-apoptotic proteins released from the mitochondria regulate the protein composition and caspase-processing activity of the native Apaf-1/Caspase-9 apoptosome complex. J. Biol. Chem. 279 (2004) 19665-19682
    • (2004) J. Biol. Chem. , vol.279 , pp. 19665-19682
    • Twiddy, D.1    Brown, D.G.2    Adrain, C.3    Jukes, R.4    Martin, S.J.5    Cohen, G.M.6    Macfarlane, M.7    Cain, K.8
  • 49
    • 0032422402 scopus 로고    scopus 로고
    • Redox regulation of the caspases during apoptosis
    • Hampton M.B., Fadeel B., and Orrenius S. Redox regulation of the caspases during apoptosis. Ann. N.Y. Acad. Sci. 854 (1998) 328-335
    • (1998) Ann. N.Y. Acad. Sci. , vol.854 , pp. 328-335
    • Hampton, M.B.1    Fadeel, B.2    Orrenius, S.3
  • 51
    • 22544444514 scopus 로고    scopus 로고
    • Caspase-independent cell death
    • Kroemer G., and Martin S.J. Caspase-independent cell death. Nat. Med. 11 (2005) 725-730
    • (2005) Nat. Med. , vol.11 , pp. 725-730
    • Kroemer, G.1    Martin, S.J.2
  • 52
    • 0038352072 scopus 로고    scopus 로고
    • Bcr-Induced apoptosis involves differential regulation of C-16 and C-24-ceramide formation and sphingolipid-dependent activation of the proteasome
    • Kroesen B.J., Jacobs S., Pettus B.J., Sietsma H., Kok J.W., Hannun Y.A., and De Leij L.F.M.H. Bcr-Induced apoptosis involves differential regulation of C-16 and C-24-ceramide formation and sphingolipid-dependent activation of the proteasome. J. Biol. Chem. 278 (2003) 14723-14731
    • (2003) J. Biol. Chem. , vol.278 , pp. 14723-14731
    • Kroesen, B.J.1    Jacobs, S.2    Pettus, B.J.3    Sietsma, H.4    Kok, J.W.5    Hannun, Y.A.6    De Leij, L.F.M.H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.