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Volumn 9, Issue 1, 2010, Pages

Exogenous coenzyme Q10 modulates MMP-2 activity in MCF-7 cell line as a breast cancer cellular model

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCYSTEINE; BIOLOGICAL MARKER; BUTHIONINE SULFOXIMINE; GELATIN; GELATINASE A; HYDROGEN PEROXIDE; MATRIX METALLOPROTEINASE INHIBITOR; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; PEPSTATIN; REACTIVE OXYGEN METABOLITE; SERINE PROTEINASE INHIBITOR; UBIDECARENONE; DRUG DERIVATIVE; ENZYME INHIBITOR; GLUTAMATE CYSTEINE LIGASE; MMP2 PROTEIN, HUMAN; SCAVENGER; UBIQUINONE;

EID: 78649485564     PISSN: None     EISSN: 14752891     Source Type: Journal    
DOI: 10.1186/1475-2891-9-62     Document Type: Article
Times cited : (28)

References (41)
  • 1
    • 70449732503 scopus 로고    scopus 로고
    • Matrix metalloproteinases as novel biomarkers and potential therapeutic targets in human cancer
    • 10.1200/JCO.2009.23.5556. 19738110
    • Matrix metalloproteinases as novel biomarkers and potential therapeutic targets in human cancer. R Roy J Yang MA Moses, J Clin Oncol 2009 27 5287 97 10.1200/JCO.2009.23.5556 19738110
    • (2009) J Clin Oncol , vol.27 , pp. 5287-97
    • Roy, R.1    Yang, J.2    Moses, M.A.3
  • 2
    • 77953188481 scopus 로고    scopus 로고
    • The role of matrix metalloproteinase 2 on the survival of patients with non-small cell lung cancer: A systematic review with meta-analysis
    • 10.3109/07357901003735634. 20394501
    • The role of matrix metalloproteinase 2 on the survival of patients with non-small cell lung cancer: a systematic review with meta-analysis. Q Qian Q Wang P Zhan L Peng SZ Wei Y Shi, Cancer Invest 2010 28 661 9 10.3109/07357901003735634 20394501
    • (2010) Cancer Invest , vol.28 , pp. 661-9
    • Qian, Q.1    Wang, Q.2    Zhan, P.3    Peng, L.4    Wei, S.Z.5    Shi, Y.6
  • 3
    • 15244338619 scopus 로고    scopus 로고
    • Collagenases in cancer
    • 10.1016/j.biochi.2004.12.009. 15781314
    • Collagenases in cancer. R Ala-aho VM Kähäri, Biochimie 2005 87 273 86 10.1016/j.biochi.2004.12.009 15781314
    • (2005) Biochimie , vol.87 , pp. 273-86
    • Ala-Aho, R.1    Kähäri, V.M.2
  • 4
    • 0034855105 scopus 로고    scopus 로고
    • Hypoxia and oxidative stress in breast cancer Oxidative stress: Its effects on the growth, metastatic potential and response to therapy of breast cancer
    • 10.1186/bcr315. 11597322
    • Hypoxia and oxidative stress in breast cancer Oxidative stress: its effects on the growth, metastatic potential and response to therapy of breast cancer. NS Brown R Bicknell, Breast Cancer Res 2001 3 323 7 10.1186/bcr315 11597322
    • (2001) Breast Cancer Res , vol.3 , pp. 323-7
    • Brown, N.S.1    Bicknell, R.2
  • 5
    • 33846117134 scopus 로고    scopus 로고
    • The signaling mechanism of ROS in tumor progression
    • 10.1007/s10555-006-9037-8. 17160708
    • The signaling mechanism of ROS in tumor progression. WS Wu, Cancer Metastasis Rev 2006 25 695 705 10.1007/s10555-006-9037-8 17160708
    • (2006) Cancer Metastasis Rev , vol.25 , pp. 695-705
    • Wu, W.S.1
  • 6
    • 84923221754 scopus 로고    scopus 로고
    • Effect of the supplemental use of antioxidants vitamin C, vitamin E, and coenzyme Q10 for the prevention and treatment of cancer
    • 15523748
    • Effect of the supplemental use of antioxidants vitamin C, vitamin E, and coenzyme Q10 for the prevention and treatment of cancer. P Shekelle ML Hardy I Coulter J Udani M Spar K Oda, Evid Rep Technol Assess (Summ) 2003 75 1 3 15523748
    • (2003) Evid Rep Technol Assess (Summ) , vol.75 , pp. 1-3
    • Shekelle, P.1    Hardy, M.L.2    Coulter, I.3    Udani, J.4    Spar, M.5    Oda, K.6
  • 7
    • 34249688738 scopus 로고    scopus 로고
    • Ameliorating effect of coenzyme Q10, riboflavin and niacin in tamoxifen-treated postmenopausal breast cancer patients with special reference to lipids and lipoproteins
    • 10.1016/j.clinbiochem.2007.02.003. 17425952
    • Ameliorating effect of coenzyme Q10, riboflavin and niacin in tamoxifen-treated postmenopausal breast cancer patients with special reference to lipids and lipoproteins. S Yuvaraj VG Premkumar K Vijayasarathy SG Gangadaran P Sachdanandam, Clin Biochem 2007 40 623 8 10.1016/j.clinbiochem.2007.02.003 17425952
    • (2007) Clin Biochem , vol.40 , pp. 623-8
    • Yuvaraj, S.1    Premkumar, V.G.2    Vijayasarathy, K.3    Gangadaran, S.G.4    Sachdanandam, P.5
  • 8
    • 71549169241 scopus 로고    scopus 로고
    • Theaflavins retard human breast cancer cell migration by inhibiting NF-kappaB via p53-ROS cross-talk
    • 10.1016/j.febslet.2009.10.081. 19883646
    • Theaflavins retard human breast cancer cell migration by inhibiting NF-kappaB via p53-ROS cross-talk. A Adhikary S Mohanty L Lahiry DM Hossain S Chakraborty T Das, FEBS Lett 2010 584 7 14 10.1016/j.febslet.2009.10.081 19883646
    • (2010) FEBS Lett , vol.584 , pp. 7-14
    • Adhikary, A.1    Mohanty, S.2    Lahiry, L.3    Hossain, D.M.4    Chakraborty, S.5    Das, T.6
  • 9
    • 78349303095 scopus 로고    scopus 로고
    • Andrographolide Exhibits Anti-Invasive Activity against Colon Cancer Cells via Inhibition of MMP2 Activity
    • 20539971
    • Andrographolide Exhibits Anti-Invasive Activity against Colon Cancer Cells via Inhibition of MMP2 Activity. HP Chao CD Kuo JH Chiu SL Fu, Planta Med 2010 20539971
    • (2010) Planta Med
    • Chao, H.P.1    Kuo, C.D.2    Chiu, J.H.3    Fu, S.L.4
  • 10
    • 34248194299 scopus 로고    scopus 로고
    • The antioxidant role of coenzyme Q
    • Epub 2007 Mar 16. 10.1016/j.mito.2007.02.006. 17482888
    • The antioxidant role of coenzyme Q. M Bentinger K Brismar G Dallner, Mitochondrion 2007 Suppl 41 50 Epub 2007 Mar 16 10.1016/j.mito.2007.02.006 17482888
    • (2007) Mitochondrion , Issue.SUPPL. , pp. 1941-50
    • Bentinger, M.1    Brismar, K.2    Dallner, G.3
  • 11
    • 75749150806 scopus 로고    scopus 로고
    • Clinical aspects of coenzyme Q10: An update
    • 10.1016/j.nut.2009.08.008. 19932599
    • Clinical aspects of coenzyme Q10: an update. GP Littarru L Tiano, Nutrition 2010 26 250 4 10.1016/j.nut.2009.08.008 19932599
    • (2010) Nutrition , vol.26 , pp. 250-4
    • Littarru, G.P.1    Tiano, L.2
  • 12
    • 0033849560 scopus 로고    scopus 로고
    • Coenzyme Q10 concentrations and antioxidant status in tissues of breast cancer patients
    • 10.1016/S0009-9120(00)00067-9. 10936586
    • coenzyme Q10 concentrations and antioxidant status in tissues of breast cancer patients. O Portakal O Ozkaya M Erden Inal B Bozan M Kosan I Sayek, Clin Biochem 2000 33 279 284 10.1016/S0009-9120(00)00067-9 10936586
    • (2000) Clin Biochem , vol.33 , pp. 279-284
    • Portakal, O.1    Ozkaya, O.2    Erden Inal, M.3    Bozan, B.4    Kosan, M.5    Sayek, I.6
  • 13
    • 77749298641 scopus 로고    scopus 로고
    • Improved survival in patients with end-stage cancer treated with coenzyme Q(10) and other antioxidants: A pilot study
    • Improved survival in patients with end-stage cancer treated with coenzyme Q(10) and other antioxidants: a pilot study. N Hertz RE Lister, J Int Med Res 2010 38 293
    • (2010) J Int Med Res , vol.38 , pp. 293
    • Hertz, N.1    Lister, R.E.2
  • 14
    • 58149383747 scopus 로고    scopus 로고
    • Antiangiogenic and hypolipidemic activity of coenzyme Q10 supplementation to breast cancer patients undergoing Tamoxifen therapy
    • 10.1002/biof.5520320118. 19096111
    • Antiangiogenic and hypolipidemic activity of coenzyme Q10 supplementation to breast cancer patients undergoing Tamoxifen therapy. P Sachdanandam, Biofactors 2008 32 151 9 10.1002/biof.5520320118 19096111
    • (2008) Biofactors , vol.32 , pp. 151-9
    • Sachdanandam, P.1
  • 15
    • 33846990517 scopus 로고    scopus 로고
    • Effect of coenzyme Q10, riboflavin and niacin on serum CEA and CA 15-3 levels in breast cancer patients undergoing tamoxifen therapy
    • 10.1248/bpb.30.367. 17268082
    • Effect of coenzyme Q10, riboflavin and niacin on serum CEA and CA 15-3 levels in breast cancer patients undergoing tamoxifen therapy. VG Premkumar S Yuvaraj K Vijayasarathy SG Gangadaran P Sachdanandam, Biol Pharm Bull 2007 30 367 70 10.1248/bpb.30.367 17268082
    • (2007) Biol Pharm Bull , vol.30 , pp. 367-70
    • Premkumar, V.G.1    Yuvaraj, S.2    Vijayasarathy, K.3    Gangadaran, S.G.4    Sachdanandam, P.5
  • 16
    • 43449128829 scopus 로고    scopus 로고
    • Anti-angiogenic potential of CoenzymeQ10, riboflavin and niacin in breast cancer patients undergoing tamoxifen therapy
    • 10.1016/j.vph.2008.02.003. 18407793
    • Anti-angiogenic potential of CoenzymeQ10, riboflavin and niacin in breast cancer patients undergoing tamoxifen therapy. VG Premkumar S Yuvaraj S Sathish P Shanthi P Sachdanandam, Vascul Pharmacol 2008 48 191 201 10.1016/j.vph.2008. 02.003 18407793
    • (2008) Vascul Pharmacol , vol.48 , pp. 191-201
    • Premkumar, V.G.1    Yuvaraj, S.2    Sathish, S.3    Shanthi, P.4    Sachdanandam, P.5
  • 17
    • 31344435897 scopus 로고    scopus 로고
    • Low plasma coenzyme Q10 levels as an independent prognostic factor for melanoma progression
    • 10.1016/j.jaad.2005.08.031. 16443053
    • Low plasma coenzyme Q10 levels as an independent prognostic factor for melanoma progression. L Rusciani I Proietti A Rusciani A Paradisi G Sbordoni C Alfano, J Am Acad Dermatol 2006 54 234 41 10.1016/j.jaad.2005.08.031 16443053
    • (2006) J Am Acad Dermatol , vol.54 , pp. 234-41
    • Rusciani, L.1    Proietti, I.2    Rusciani, A.3    Paradisi, A.4    Sbordoni, G.5    Alfano, C.6
  • 18
    • 0032817034 scopus 로고    scopus 로고
    • Expression of the MMP-1 in human pancreatic carcinoma: Relationship with prognostic factor
    • 10430270
    • Expression of the MMP-1 in human pancreatic carcinoma: relationship with prognostic factor. T Ito M Ito J Shiozawa S Naito T Kanematsu I Sekine, Mod Pathol 1999 12 669 74 10430270
    • (1999) Mod Pathol , vol.12 , pp. 669-74
    • Ito, T.1    Ito, M.2    Shiozawa, J.3    Naito, S.4    Kanematsu, T.5    Sekine, I.6
  • 19
    • 65949107334 scopus 로고    scopus 로고
    • SCUBE2 suppresses breast tumor cell proliferation and confers a favorable prognosis in invasive breast cancer
    • 10.1158/0008-5472.CAN-08-3615. 19369267
    • SCUBE2 suppresses breast tumor cell proliferation and confers a favorable prognosis in invasive breast cancer. CJ Cheng YC Lin MT Tsai CS Chen MC Hsieh CL Chen, Cancer Res 2009 69 3634 41 10.1158/0008-5472.CAN-08-3615 19369267
    • (2009) Cancer Res , vol.69 , pp. 3634-41
    • Cheng, C.J.1    Lin, Y.C.2    Tsai, M.T.3    Chen, C.S.4    Hsieh, M.C.5    Chen, C.L.6
  • 20
    • 34948842470 scopus 로고    scopus 로고
    • Thiol supplementation inhibits metalloproteinase activity independent of glutathione status
    • 10.1016/j.bbrc.2007.09.018. 17900531
    • Thiol supplementation inhibits metalloproteinase activity independent of glutathione status. P Bogani M Canavesi TM Hagen F Visioli S Bellosta, Biochem Biophys Res Commun 2007 363 651 5 10.1016/j.bbrc.2007.09.018 17900531
    • (2007) Biochem Biophys Res Commun , vol.363 , pp. 651-5
    • Bogani, P.1    Canavesi, M.2    Hagen, T.M.3    Visioli, F.4    Bellosta, S.5
  • 21
    • 0033231162 scopus 로고    scopus 로고
    • Biologic and pharmacologic regulation of mammalian glutathione synthesis
    • 10.1016/S0891-5849(99)00176-8. 10569625
    • Biologic and pharmacologic regulation of mammalian glutathione synthesis. OW Griffith, Free Radic Biol Med 1999 27 922 35 10.1016/S0891-5849(99)00176-8 10569625
    • (1999) Free Radic Biol Med , vol.27 , pp. 922-35
    • Griffith, O.W.1
  • 22
    • 33749061028 scopus 로고    scopus 로고
    • Reduced nonprotein thiols inhibit activation and function of MMP-9: Implications for chemoprevention
    • 10.1016/j.freeradbiomed.2006.07.014. 17015178
    • Reduced nonprotein thiols inhibit activation and function of MMP-9: implications for chemoprevention. P Pei MP Horan R Hille CF Hemann SP Schwendeman SR Mallery, Free Radic Biol Med 2006 41 1315 24 10.1016/j. freeradbiomed.2006.07.014 17015178
    • (2006) Free Radic Biol Med , vol.41 , pp. 1315-24
    • Pei, P.1    Horan, M.P.2    Hille, R.3    Hemann, C.F.4    Schwendeman, S.P.5    Mallery, S.R.6
  • 23
    • 39149084984 scopus 로고    scopus 로고
    • Rapid expression and activation of MMP-2 and MMP-9 upon exposure of human breast cancer cells (MCF-7) to fibronectin in serum free medium
    • Epub 2007 Dec 27. 10.1016/j.lfs.2007.12.013. 18243246
    • Rapid expression and activation of MMP-2 and MMP-9 upon exposure of human breast cancer cells (MCF-7) to fibronectin in serum free medium. S Das A Banerji E Frei A Chatterjee, Life Sci 2008 82 467 76 Epub 2007 Dec 27 10.1016/j.lfs.2007.12.013 18243246
    • (2008) Life Sci , vol.82 , pp. 467-76
    • Das, S.1    Banerji, A.2    Frei, E.3    Chatterjee, A.4
  • 24
    • 0026526252 scopus 로고
    • A microplate assay for the detection of oxidative products using 2′,7′-dichlorofluorescin-diacetate
    • 10.1016/0022-1759(92)90008-H. 1431161
    • A microplate assay for the detection of oxidative products using 2′,7′-dichlorofluorescin-diacetate. AR Rosenkranz S Schmaldienst KM Stuhlmeier W Chen W Knapp GJ Zlabinger, J Immunol Methods 1992 156 39 45 10.1016/0022-1759(92)90008-H 1431161
    • (1992) J Immunol Methods , vol.156 , pp. 39-45
    • Rosenkranz, A.R.1    Schmaldienst, S.2    Stuhlmeier, K.M.3    Chen, W.4    Knapp, W.5    Zlabinger, G.J.6
  • 25
    • 0032546792 scopus 로고    scopus 로고
    • Disruption of redox homeostasis in the transforming growth factor-alpha/c-myc transgenic mouse model of accelerated hepatocarcinogenesis
    • 10.1074/jbc.273.25.15846. 9624185
    • Disruption of redox homeostasis in the transforming growth factor-alpha/c-myc transgenic mouse model of accelerated hepatocarcinogenesis. VM Factor A Kiss JT Woitach PJ Wirth SS Thorgeirsson, J Biol Chem 1998 273 15846 53 10.1074/jbc.273.25.15846 9624185
    • (1998) J Biol Chem , vol.273 , pp. 15846-53
    • Factor, V.M.1    Kiss, A.2    Woitach, J.T.3    Wirth, P.J.4    Thorgeirsson, S.S.5
  • 26
    • 77950540855 scopus 로고    scopus 로고
    • Matrix metalloproteinase activity assays: Importance of zymography
    • 10.1016/j.vascn.2010.02.011. 20176119
    • Matrix metalloproteinase activity assays: Importance of zymography. K Kupai G Szucs I Hajdu C Csonka T Csont, J Pharmacol Toxicol Methods 2010 61 205 9 10.1016/j.vascn.2010.02.011 20176119
    • (2010) J Pharmacol Toxicol Methods , vol.61 , pp. 205-9
    • Kupai, K.1    Szucs, G.2    Hajdu, I.3    Csonka, C.4    Csont, T.5
  • 27
    • 28444486500 scopus 로고    scopus 로고
    • Determination of gelatinase A using a modified indirect hemagglutination assay in human prostate cancer screening and assessment of its correlation with prostate-specific antigen parameters
    • 10.1111/j.1442-2042.2005.01094.x. 16045556
    • Determination of gelatinase A using a modified indirect hemagglutination assay in human prostate cancer screening and assessment of its correlation with prostate-specific antigen parameters. MR Khorramizadeh M Pezeshki A Ghahary H Zeraati A Berahmeh, Int J Urol 2005 12 637 43 10.1111/j.1442-2042.2005.01094.x 16045556
    • (2005) Int J Urol , vol.12 , pp. 637-43
    • Khorramizadeh, M.R.1    Pezeshki, M.2    Ghahary, A.3    Zeraati, H.4    Berahmeh, A.5
  • 28
    • 39149084984 scopus 로고    scopus 로고
    • Rapid expression and activation of MMP-2 and MMP-9 upon exposure of human breast cancer cells (MCF-7) to fibronectin in serum free medium
    • 10.1016/j.lfs.2007.12.013. 18243246
    • Rapid expression and activation of MMP-2 and MMP-9 upon exposure of human breast cancer cells (MCF-7) to fibronectin in serum free medium. S Das A Banerji E Frei A Chatterjee, Life Sci 2008 82 467 76 10.1016/j.lfs.2007.12.013 18243246
    • (2008) Life Sci , vol.82 , pp. 467-76
    • Das, S.1    Banerji, A.2    Frei, E.3    Chatterjee, A.4
  • 29
    • 0141925744 scopus 로고    scopus 로고
    • Down-regulation of glutathione and Bcl-2 synthesis in mouse B16 melanoma cells avoids their survival during interaction with the vascular endothelium
    • 10.1074/jbc.M303753200. 12881529
    • Down-regulation of glutathione and Bcl-2 synthesis in mouse B16 melanoma cells avoids their survival during interaction with the vascular endothelium. A Ortega P Ferrer J Carretero E Obrador M Asensi JA Pellicer, J Biol Chem 2003 278 39591 9 10.1074/jbc.M303753200 12881529
    • (2003) J Biol Chem , vol.278 , pp. 39591-9
    • Ortega, A.1    Ferrer, P.2    Carretero, J.3    Obrador, E.4    Asensi, M.5    Pellicer, J.A.6
  • 30
    • 4043161974 scopus 로고    scopus 로고
    • Mitochondrial redox control of matrix metalloproteinases
    • 10.1016/j.freeradbiomed.2004.06.008. 15304253
    • Mitochondrial redox control of matrix metalloproteinases. KK Nelson JA Melendez, Free Radic Biol Med 2004 37 768 84 10.1016/j.freeradbiomed.2004.06.008 15304253
    • (2004) Free Radic Biol Med , vol.37 , pp. 768-84
    • Nelson, K.K.1    Melendez, J.A.2
  • 31
    • 33744983072 scopus 로고    scopus 로고
    • Cytotoxic response of breast cancer cell lines, MCF 7 and T 47 D to triphala and its modification by antioxidants
    • 10.1016/j.canlet.2005.07.013. 16135398
    • Cytotoxic response of breast cancer cell lines, MCF 7 and T 47 D to triphala and its modification by antioxidants. T Sandhya KP Mishra, Cancer Lett 2006 238 304 13 10.1016/j.canlet.2005.07.013 16135398
    • (2006) Cancer Lett , vol.238 , pp. 304-13
    • Sandhya, T.1    Mishra, K.P.2
  • 32
    • 57749196001 scopus 로고    scopus 로고
    • Changes in matrix metalloproteinases activities in normal and transformed mouse fibroblasts under effect of antioxidants
    • 19062520
    • Changes in matrix metalloproteinases activities in normal and transformed mouse fibroblasts under effect of antioxidants. IV Voronkina KM Kirpichnikova LV Smagina IA Gamali Tsitologiia 2008 50 877 81 19062520
    • (2008) Tsitologiia , vol.50 , pp. 877-81
    • Voronkina, I.V.1    Kirpichnikova, K.M.2    Smagina, L.V.3    Gamali, I.A.4
  • 33
    • 34948842470 scopus 로고    scopus 로고
    • Thiol supplementation inhibits metalloproteinase activity independent of glutathione status
    • 10.1016/j.bbrc.2007.09.018. 17900531
    • Thiol supplementation inhibits metalloproteinase activity independent of glutathione status. P Bogani M Canavesi TM Hagen F Visioli S Bellosta, Biochem Biophys Res Commun 2007 363 651 5 10.1016/j.bbrc.2007.09.018 17900531
    • (2007) Biochem Biophys Res Commun , vol.363 , pp. 651-5
    • Bogani, P.1    Canavesi, M.2    Hagen, T.M.3    Visioli, F.4    Bellosta, S.5
  • 34
    • 9244222705 scopus 로고    scopus 로고
    • Reduction-oxidation (redox) state regulation of extracellular matrix metalloproteinases and tissue inhibitors in cardiac normal and transformed fibroblast cells
    • 10.1002/(SICI)1097-4644(19960401) 61:1<139::AID-JCB15>3.0.CO;2-J. 8726363
    • Reduction-oxidation (redox) state regulation of extracellular matrix metalloproteinases and tissue inhibitors in cardiac normal and transformed fibroblast cells. SC Tyagi S Kumar S Borders, J Cell Biochem 1996 61 139 51 10.1002/(SICI)1097-4644(19960401)61:1<139::AID-JCB15>3.0.CO;2-J 8726363
    • (1996) J Cell Biochem , vol.61 , pp. 139-51
    • Tyagi, S.C.1    Kumar, S.2    Borders, S.3
  • 35
    • 17744409665 scopus 로고    scopus 로고
    • The protein thiol metallothionein as an antioxidant and protectant against antineoplastic drugs
    • 10.1016/S0009-2797(97)00165-8. 9679559
    • The protein thiol metallothionein as an antioxidant and protectant against antineoplastic drugs. JS Lazo SM Kuo ES Woo BR Pitt, Chem Biol Interact 1998 111-112 255 262 10.1016/S0009-2797(97)00165-8 9679559
    • (1998) Chem Biol Interact , vol.111-112 , pp. 255-262
    • Lazo, J.S.1    Kuo, S.M.2    Woo, E.S.3    Pitt, B.R.4
  • 36
    • 0030614809 scopus 로고    scopus 로고
    • Hydrogen peroxide (H2O2) increases the steady-state mRNA levels of collagenase/MMP-1 in human dermal fibroblasts
    • 10.1016/S0891-5849(96)00404-2. 8981044
    • Hydrogen peroxide (H2O2) increases the steady-state mRNA levels of collagenase/MMP-1 in human dermal fibroblasts. P Brenneisen K Briviba M Wlaschek J Wenk K Scharffetter-Kochanek, Free Radic Biol Med 1997 22 515 24 10.1016/S0891-5849(96)00404-2 8981044
    • (1997) Free Radic Biol Med , vol.22 , pp. 515-24
    • Brenneisen, P.1    Briviba, K.2    Wlaschek, M.3    Wenk, J.4    Scharffetter-Kochanek, K.5
  • 37
    • 0033520497 scopus 로고    scopus 로고
    • Stable overexpression of manganese superoxide dismutase in mitochondria identifies hydrogen peroxide as a major oxidant in the AP-1-mediated induction of matrix-degrading metalloprotease-1
    • 10.1074/jbc.274.36.25869. 10464329
    • Stable overexpression of manganese superoxide dismutase in mitochondria identifies hydrogen peroxide as a major oxidant in the AP-1-mediated induction of matrix-degrading metalloprotease-1. J Wenk P Brenneisen M Wlaschek A Poswig K Briviba TD Oberley, J Biol Chem 1999 274 25869 76 10.1074/jbc.274.36.25869 10464329
    • (1999) J Biol Chem , vol.274 , pp. 25869-76
    • Wenk, J.1    Brenneisen, P.2    Wlaschek, M.3    Poswig, A.4    Briviba, K.5    Oberley, T.D.6
  • 38
    • 58149387518 scopus 로고    scopus 로고
    • Functions of coenzyme Q10 in inflammation and gene expression
    • 10.1002/biof.5520320121. 19096114
    • Functions of coenzyme Q10 in inflammation and gene expression. C Schmelzer I Lindner G Rimbach P Niklowitz T Menke F Döring, Biofactors 2008 32 179 83 10.1002/biof.5520320121 19096114
    • (2008) Biofactors , vol.32 , pp. 179-83
    • Schmelzer, C.1    Lindner, I.2    Rimbach, G.3    Niklowitz, P.4    Menke, T.5    Döring, F.6
  • 39
    • 0032546792 scopus 로고    scopus 로고
    • Disruption of redox homeostasis in the transforming growth factor-alpha/c-myc transgenic mouse model of accelerated hepatocarcinogenesis
    • 10.1074/jbc.273.25.15846. 9624185
    • Disruption of redox homeostasis in the transforming growth factor-alpha/c-myc transgenic mouse model of accelerated hepatocarcinogenesis. VM Factor A Kiss JT Woitach PJ Wirth SS Thorgeirsson, J Biol Chem 1998 273 15846 53 10.1074/jbc.273.25.15846 9624185
    • (1998) J Biol Chem , vol.273 , pp. 15846-53
    • Factor, V.M.1    Kiss, A.2    Woitach, J.T.3    Wirth, P.J.4    Thorgeirsson, S.S.5
  • 40
    • 34248184025 scopus 로고    scopus 로고
    • Coenzyme Q10 - Its role as a prooxidant in the formation of superoxide anion/hydrogen peroxide and the regulation of the metabolome
    • Epub 2007 Mar 30. 10.1016/j.mito.2007.03.005. 17482887
    • Coenzyme Q10 - its role as a prooxidant in the formation of superoxide anion/hydrogen peroxide and the regulation of the metabolome. AW Linnane M Kios L Vitetta, Mitochondrion 2007 Suppl 51 61 Epub 2007 Mar 30 10.1016/j.mito.2007. 03.005 17482887
    • (2007) Mitochondrion , Issue.SUPPL. , pp. 1951-61
    • Linnane, A.W.1    Kios, M.2    Vitetta, L.3


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