메뉴 건너뛰기




Volumn 1693, Issue 1, 2004, Pages 37-45

Overexpression of antioxidant enzyme peroxiredoxin 5 protects human tendon cells against apoptosis and loss of cellular function during oxidative stress

Author keywords

Antioxidant; Collagen synthesis; Hydrogen peroxide (H2O2); Tendon cell; Transfection

Indexed keywords

ENZYME; HYDROGEN PEROXIDE; LIPOCORTIN 5; PEROXIREDOXIN; PEROXIREDOXIN 5; UNCLASSIFIED DRUG;

EID: 3242796654     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2004.04.006     Document Type: Article
Times cited : (107)

References (46)
  • 1
    • 0026339892 scopus 로고
    • Histopathological changes preceding spontaneous rupture of a tendon. a controlled study of 891 patients
    • Kannus P., Jozsa L. Histopathological changes preceding spontaneous rupture of a tendon. A controlled study of 891 patients. J. Bone Jt. Surg., Am. 73:1991;1507-1525
    • (1991) J. Bone Jt. Surg., Am. , vol.73 , pp. 1507-1525
    • Kannus, P.1    Jozsa, L.2
  • 4
    • 0029085387 scopus 로고
    • Exercise loading of tendons and the development of overuse injuries. a review of current literature
    • Archambault J.M., Wiley J.P., Bray R.C. Exercise loading of tendons and the development of overuse injuries. A review of current literature. Sports Med. 20:1995;77-89
    • (1995) Sports Med. , vol.20 , pp. 77-89
    • Archambault, J.M.1    Wiley, J.P.2    Bray, R.C.3
  • 6
    • 0038359753 scopus 로고    scopus 로고
    • Involvement of cytochrome c release and caspase-3 activation in the oxidative stress-induced apoptosis in human tendon fibroblasts
    • Yuan J., Murrell G.A., Trickett A., Wang M.X. Involvement of cytochrome c release and caspase-3 activation in the oxidative stress-induced apoptosis in human tendon fibroblasts. Biochim. Biophys. Acta. 1641:2003;35-41
    • (2003) Biochim. Biophys. Acta , vol.1641 , pp. 35-41
    • Yuan, J.1    Murrell, G.A.2    Trickett, A.3    Wang, M.X.4
  • 7
    • 0000385805 scopus 로고    scopus 로고
    • Isoforms of mammalian peroxiredoxin that reduce peroxides in presence of thioredoxin
    • Chae H.Z., Kang S.W., Rhee S.G. Isoforms of mammalian peroxiredoxin 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
  • 9
    • 0036287739 scopus 로고    scopus 로고
    • Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein
    • Fujii J., Ikeda Y. Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein. Redox Rep. 7:2002;123-130
    • (2002) Redox Rep. , vol.7 , pp. 123-130
    • Fujii, J.1    Ikeda, Y.2
  • 11
    • 0029560827 scopus 로고
    • Early events in erythroid differentiation: Accumulation of the acidic peroxidoxin (PRP/TSA/NKEF-B)
    • Rabilloud T., Berthier R., Vincon M., Ferbus D., Goubin G., Lawrence J.J. Early events in erythroid differentiation: accumulation of the acidic peroxidoxin (PRP/TSA/NKEF-B). Biochem. J. 312:1995;699-705
    • (1995) Biochem. J. , vol.312 , pp. 699-705
    • Rabilloud, T.1    Berthier, R.2    Vincon, M.3    Ferbus, D.4    Goubin, G.5    Lawrence, J.J.6
  • 12
    • 0027247446 scopus 로고
    • A human cDNA corresponding to a gene overexpressed during cell proliferation encodes a product sharing homology with amoebic and bacterial proteins
    • Prosperi M.T., Ferbus D., Karczinski I., Goubin G. 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
  • 13
    • 0028283906 scopus 로고
    • Cloning and sequence analysis of candidate human natural killer-enhancing factor genes
    • Shau H., Butterfield L.H., Chiu R., Kim A. Cloning and sequence analysis of candidate human natural killer-enhancing factor genes. Immunogenetics. 40:1994;129-134
    • (1994) Immunogenetics , vol.40 , pp. 129-134
    • Shau, H.1    Butterfield, L.H.2    Chiu, R.3    Kim, A.4
  • 14
    • 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
  • 15
    • 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
  • 16
    • 0001015125 scopus 로고    scopus 로고
    • Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate
    • Seo M.S., Kang S.W., Kim K., Baines I.C., Lee T.H., Rhee S.G. 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
  • 17
    • 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
  • 19
    • 0035943382 scopus 로고    scopus 로고
    • Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 a resolution
    • Declercq J.P., Evrard C., Clippe A., Stricht D.V., Bernard A., Knoops B. Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 A resolution. J. Mol. Biol. 311:2001;751-759
    • (2001) J. Mol. Biol. , vol.311 , pp. 751-759
    • Declercq, J.P.1    Evrard, C.2    Clippe, A.3    Stricht, D.V.4    Bernard, A.5    Knoops, B.6
  • 20
    • 0032030837 scopus 로고    scopus 로고
    • Dual-color flow cytometric detection of fluorescent proteins using single-laser (488-nm) excitation
    • Lybarger L., Dempsey D., Patterson G.H., Piston D.W., Kain S.R., Chervenak R. Dual-color flow cytometric detection of fluorescent proteins using single-laser (488-nm) excitation. Cytometry. 31:1998;147-152
    • (1998) Cytometry , vol.31 , pp. 147-152
    • Lybarger, L.1    Dempsey, D.2    Patterson, G.H.3    Piston, D.W.4    Kain, S.R.5    Chervenak, R.6
  • 22
    • 0034607753 scopus 로고    scopus 로고
    • N-methyl-D-aspartate receptor mediated toxicity in nonneuronal cell lines: Characterization using fluorescent measures of cell viability and reactive oxygen species production
    • Anegawa N.J., Guttmann R.P., Grant E.R., Anand R., Lindstrom J., Lynch D.R. N-methyl-D-aspartate receptor mediated toxicity in nonneuronal cell lines: characterization using fluorescent measures of cell viability and reactive oxygen species production. Brain Res. Mol. Brain Res. 77:2000;163-175
    • (2000) Brain Res. Mol. Brain Res. , vol.77 , pp. 163-175
    • Anegawa, N.J.1    Guttmann, R.P.2    Grant, E.R.3    Anand, R.4    Lindstrom, J.5    Lynch, D.R.6
  • 24
    • 0029043888 scopus 로고
    • A novel assay for apoptosis. Flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled Annexin V
    • Vermes I., Haanen C., Steffens-Nakken H., Reutelingsperger C. A novel assay for apoptosis. Flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled Annexin V. J. Immunol. Methods. 184:1995;39-51
    • (1995) J. Immunol. Methods , vol.184 , pp. 39-51
    • Vermes, I.1    Haanen, C.2    Steffens-Nakken, H.3    Reutelingsperger, C.4
  • 25
    • 0025194321 scopus 로고
    • A microassay to quantitate collagen synthesis by cells in culture
    • Diegelmann R.F., Bryson G.R., Flood L.C., Graham M.F. A microassay to quantitate collagen synthesis by cells in culture. Anal. Biochem. 186:1990;296-300
    • (1990) Anal. Biochem. , vol.186 , pp. 296-300
    • Diegelmann, R.F.1    Bryson, G.R.2    Flood, L.C.3    Graham, M.F.4
  • 27
    • 0018850985 scopus 로고
    • A simple, rapid, and sensitive DNA assay procedure
    • Labarca C., Paigen K. A simple, rapid, and sensitive DNA assay procedure. Anal. Biochem. 102:1980;344-352
    • (1980) Anal. Biochem. , vol.102 , pp. 344-352
    • Labarca, C.1    Paigen, K.2
  • 28
    • 0032053707 scopus 로고    scopus 로고
    • Oxygen radicals and signaling
    • Finkel T. 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
  • 30
    • 0031884519 scopus 로고    scopus 로고
    • Translational control: A general mechanism for gene regulation during T cell activation
    • Garcia-Sanz J.A., Mikulits W., Livingstone A., Lefkovits I., Mullner E.W. Translational control: a general mechanism for gene regulation during T cell activation. FASEB J. 12:1998;299-306
    • (1998) FASEB J. , vol.12 , pp. 299-306
    • Garcia-Sanz, J.A.1    Mikulits, W.2    Livingstone, A.3    Lefkovits, I.4    Mullner, E.W.5
  • 33
    • 0026586560 scopus 로고
    • An insight into Dupuytren's contracture
    • (discussion 161)
    • Murrell G.A. An insight into Dupuytren's contracture. Ann. R. Coll. Surg. Engl. 74:1992;156-160. (discussion 161)
    • (1992) Ann. R. Coll. Surg. Engl. , vol.74 , pp. 156-160
    • Murrell, G.A.1
  • 34
    • 0035425182 scopus 로고    scopus 로고
    • Thioredoxin peroxidase-1 (peroxiredoxin-1) is increased in thioredoxin-1 transfected cells and results in enhanced protection against apoptosis caused by hydrogen peroxide but not by other agents including dexamethasone, etoposide, and doxorubicin
    • Berggren M.I., Husbeck B., Samulitis B., Baker A.F., Gallegos A., Powis G. Thioredoxin peroxidase-1 (peroxiredoxin-1) is increased in thioredoxin-1 transfected cells and results in enhanced protection against apoptosis caused by hydrogen peroxide but not by other agents including dexamethasone, etoposide, and doxorubicin. Arch. Biochem. Biophys. 392:2001;103-109
    • (2001) Arch. Biochem. Biophys. , vol.392 , pp. 103-109
    • Berggren, M.I.1    Husbeck, B.2    Samulitis, B.3    Baker, A.F.4    Gallegos, A.5    Powis, G.6
  • 35
    • 0034674703 scopus 로고    scopus 로고
    • Role of peroxiredoxins in regulating intracellular hydrogen peroxide and hydrogen peroxide-induced apoptosis in thyroid cells
    • Kim H., Lee T.H., Park E.S., Suh J.M., Park S.J., Chung H.K., Kwon O.Y., Kim Y.K., Ro H.K., Shong M. Role of peroxiredoxins in regulating intracellular hydrogen peroxide and hydrogen peroxide-induced apoptosis in thyroid cells. J. Biol. Chem. 275:2000;18266-18270
    • (2000) J. Biol. Chem. , vol.275 , pp. 18266-18270
    • Kim, H.1    Lee, T.H.2    Park, E.S.3    Suh, J.M.4    Park, S.J.5    Chung, H.K.6    Kwon, O.Y.7    Kim, Y.K.8    Ro, H.K.9    Shong, M.10
  • 37
    • 0030805979 scopus 로고    scopus 로고
    • Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12
    • Link A.J., Robison K., Church G.M. Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 18:1997;1259-1313
    • (1997) Electrophoresis , vol.18 , pp. 1259-1313
    • Link, A.J.1    Robison, K.2    Church, G.M.3
  • 38
    • 0025996014 scopus 로고
    • Reconstitution of Ca(2+)-dependent K+ transport in erythrocyte membrane vesicles requires a cytoplasmic protein
    • Moore R.B., Mankad M.V., Shriver S.K., Mankad V.N., Plishker G.A. Reconstitution of Ca(2+)-dependent K+ transport in erythrocyte membrane vesicles requires a cytoplasmic protein. J. Biol. Chem. 266:1991;18964-18968
    • (1991) J. Biol. Chem. , vol.266 , pp. 18964-18968
    • Moore, R.B.1    Mankad, M.V.2    Shriver, S.K.3    Mankad, V.N.4    Plishker, G.A.5
  • 39
    • 0001445231 scopus 로고    scopus 로고
    • Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin
    • Chae H.Z., Kim H.J., Kang S.W., Rhee S.G. Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin. Diabetes Res. Clin. Pract. 45:1999;101-112
    • (1999) Diabetes Res. Clin. Pract. , vol.45 , pp. 101-112
    • Chae, H.Z.1    Kim, H.J.2    Kang, S.W.3    Rhee, S.G.4
  • 40
    • 0346056899 scopus 로고    scopus 로고
    • Overexpression of human peroxiredoxin 5 in subcellular compartments of Chinese hamster ovary cells: Effects on cytotoxicity and DNA damage caused by peroxides
    • Banmeyer I., Marchand C., Verhaeghe C., Vucic B., Rees J.F., Knoops B. Overexpression of human peroxiredoxin 5 in subcellular compartments of Chinese hamster ovary cells: effects on cytotoxicity and DNA damage caused by peroxides. Free Radic. Biol. Med. 36:2004;65-77
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 65-77
    • Banmeyer, I.1    Marchand, C.2    Verhaeghe, C.3    Vucic, B.4    Rees, J.F.5    Knoops, B.6
  • 41
    • 0028243182 scopus 로고
    • Tendon degeneration and chronic shoulder pain: Changes in the collagen composition of the human rotator cuff tendons in rotator cuff tendinitis
    • Riley G.P., Harrall R.L., Constant C.R., Chard M.D., Cawston T.E., Hazleman B.L. Tendon degeneration and chronic shoulder pain: changes in the collagen composition of the human rotator cuff tendons in rotator cuff tendinitis. Ann. Rheum. Dis. 53:1994;359-366
    • (1994) Ann. Rheum. Dis. , vol.53 , pp. 359-366
    • Riley, G.P.1    Harrall, R.L.2    Constant, C.R.3    Chard, M.D.4    Cawston, T.E.5    Hazleman, B.L.6
  • 43
    • 0034995893 scopus 로고    scopus 로고
    • Oxidative stress regulates collagen synthesis and matrix metalloproteinase activity in cardiac fibroblasts
    • Siwik D.A., Pagano P.J., Colucci W.S. Oxidative stress regulates collagen synthesis and matrix metalloproteinase activity in cardiac fibroblasts. Am. J. Physiol., Cell Physiol. 280:2001;C53-C60
    • (2001) Am. J. Physiol., Cell Physiol. , vol.280 , pp. 53-C60
    • Siwik, D.A.1    Pagano, P.J.2    Colucci, W.S.3
  • 44
    • 0037085011 scopus 로고    scopus 로고
    • Alzheimer's disease and oxygen radicals: New insights
    • Pratico D. Alzheimer's disease and oxygen radicals: new insights. Biochem. Pharmacol. 63:2002;563-567
    • (2002) Biochem. Pharmacol. , vol.63 , pp. 563-567
    • Pratico, D.1
  • 46
    • 0032704101 scopus 로고    scopus 로고
    • Antioxidants, oxidative stress, and degenerative neurological disorders
    • Floyd R.A. Antioxidants, oxidative stress, and degenerative neurological disorders. Proc. Soc. Exp. Biol. Med. 222:1999;236-245
    • (1999) Proc. Soc. Exp. Biol. Med. , vol.222 , pp. 236-245
    • Floyd, R.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.