메뉴 건너뛰기




Volumn 105, Issue 51, 2008, Pages 20470-20475

Antioxidant activity of growth hormone-releasing hormone antagonists in LNCaP human prostate cancer line

Author keywords

Antioxidative activity; GHRH; Oxidative stress; ROS

Indexed keywords

ANTIOXIDANT; CASPASE 3; CYCLINE; CYCLOOXYGENASE 2; CYTOCHROME C OXIDASE; CYTOCHROME C OXIDASE IV; GROWTH HORMONE RELEASING FACTOR; HORMONE ANTAGONIST; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; JMR 132; LIPID; NUCLEAR FACTOR KAPPA B P50; PROTEIN P53; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 58149479262     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0811209106     Document Type: Article
Times cited : (57)

References (89)
  • 1
    • 0033485288 scopus 로고    scopus 로고
    • Antagonistic analogs of growth hormone-releasing hormone: New potential antitumor agents
    • Schally, Varga JL (1999) Antagonistic analogs of growth hormone-releasing hormone: New potential antitumor agents. Trends Endocrinol Metab 10:383-391.
    • (1999) Trends Endocrinol Metab , vol.10 , pp. 383-391
    • Schally, V.J.L.1
  • 2
    • 45549089546 scopus 로고    scopus 로고
    • New approaches to the therapy of various tumors based on peptide analogues
    • Schally AV (2008) New approaches to the therapy of various tumors based on peptide analogues. Horm Metab Res 40:315-322.
    • (2008) Horm Metab Res , vol.40 , pp. 315-322
    • Schally, A.V.1
  • 3
    • 37349032876 scopus 로고    scopus 로고
    • Antagonists of growth-hormone- releasing hormone: An emerging new therapy for cancer
    • Schally AV, Varga JL, Engel JB (2008) Antagonists of growth-hormone- releasing hormone: An emerging new therapy for cancer. Nat Clin Pract Endocrinol Metab 4:33-43.
    • (2008) Nat Clin Pract Endocrinol Metab , vol.4 , pp. 33-43
    • Schally, A.V.1    Varga, J.L.2    Engel, J.B.3
  • 4
    • 44349126257 scopus 로고    scopus 로고
    • Knocking down gene expression for growth hormone-releasing hormone inhibits proliferation of human cancer cell lines
    • Barabutis N, Schally AV (2008) Knocking down gene expression for growth hormone-releasing hormone inhibits proliferation of human cancer cell lines. Br J Cancer 98:1790-1796.
    • (2008) Br J Cancer , vol.98 , pp. 1790-1796
    • Barabutis, N.1    Schally, A.V.2
  • 5
    • 28444478741 scopus 로고    scopus 로고
    • The expression of the pituitary growth hormone-releasing hormone receptor and its splice variants in normal and neoplastic human tissues
    • Havt A, et al. (2005) The expression of the pituitary growth hormone-releasing hormone receptor and its splice variants in normal and neoplastic human tissues. Proc Natl Acad Sci USA 102:17424-17429.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17424-17429
    • Havt, A.1
  • 6
    • 0033592985 scopus 로고    scopus 로고
    • Growth hormone-releasing hormone: An autocrine growth factor for small cell lung carcinoma
    • Kiaris H, Schally AV, Varga JL, Groot K, Armatis P (1999) Growth hormone-releasing hormone: An autocrine growth factor for small cell lung carcinoma. Proc Natl Acad Sci USA 96:14894-14898.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14894-14898
    • Kiaris, H.1    Schally, A.V.2    Varga, J.L.3    Groot, K.4    Armatis, P.5
  • 7
    • 20444447682 scopus 로고    scopus 로고
    • Extrapituitary effects of the growth hormone-releasing hormone
    • Kiaris H, Schally AV, Kalofoutis A (2005) Extrapituitary effects of the growth hormone-releasing hormone. Vitam Horm 70:1-24.
    • (2005) Vitam Horm , vol.70 , pp. 1-24
    • Kiaris, H.1    Schally, A.V.2    Kalofoutis, A.3
  • 8
    • 0034641750 scopus 로고    scopus 로고
    • Isolation and sequencing of cDNAs for splice variants of growth hormone-releasing hormone receptors from human cancers
    • Rekasi Z, Czompoly T, Schally AV, Halmos G (2000) Isolation and sequencing of cDNAs for splice variants of growth hormone-releasing hormone receptors from human cancers. Proc Natl Acad Sci USA 97:10561-10566.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10561-10566
    • Rekasi, Z.1    Czompoly, T.2    Schally, A.V.3    Halmos, G.4
  • 9
    • 34248387305 scopus 로고    scopus 로고
    • Stimulation of proliferation of MCF-7 breast cancer cells by a transfected splice variant of growth hormone-releasing hormone receptor
    • Barabutis N, et al. (2007) Stimulation of proliferation of MCF-7 breast cancer cells by a transfected splice variant of growth hormone-releasing hormone receptor. Proc Natl Acad Sci USA 104:5575-5579.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 5575-5579
    • Barabutis, N.1
  • 10
    • 0041633498 scopus 로고    scopus 로고
    • Growth hormone-releasing hormone and extra-pituitary tumorigenesis: Therapeutic and diagnostic applications of growth hormone-releasing hormone antagonists
    • Kiaris H, Koutsilieris M, Kalofoutis A, Schally AV (2003) Growth hormone-releasing hormone and extra-pituitary tumorigenesis: Therapeutic and diagnostic applications of growth hormone-releasing hormone antagonists. Expert Opin Investig Drugs 12:1385-1394.
    • (2003) Expert Opin Investig Drugs , vol.12 , pp. 1385-1394
    • Kiaris, H.1    Koutsilieris, M.2    Kalofoutis, A.3    Schally, A.V.4
  • 12
    • 0037453207 scopus 로고    scopus 로고
    • GH-RH antagonist (MZ-4-71) inhibits VEGF secretion and proliferation of murine endothelial cells
    • Siejka A, et al. (2003) GH-RH antagonist (MZ-4-71) inhibits VEGF secretion and proliferation of murine endothelial cells. Life Sci 72:2473-2479.
    • (2003) Life Sci , vol.72 , pp. 2473-2479
    • Siejka, A.1
  • 13
    • 40749109041 scopus 로고    scopus 로고
    • Biochemistry: Radicals by reduction
    • Jarrett JT (2008) Biochemistry: Radicals by reduction. Nature 452:163-164.
    • (2008) Nature , vol.452 , pp. 163-164
    • Jarrett, J.T.1
  • 14
    • 41649096518 scopus 로고    scopus 로고
    • Induction of oxidative stress as a mechanism of action of chemopreventive agents against cancer
    • Rigas B, Sun Y (2008) Induction of oxidative stress as a mechanism of action of chemopreventive agents against cancer. Br J Cancer 98:1157-1160.
    • (2008) Br J Cancer , vol.98 , pp. 1157-1160
    • Rigas, B.1    Sun, Y.2
  • 15
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • Balaban RS, Nemoto S, Finkel T (2005) Mitochondria, oxidants, and aging. Cell 120:483-495.
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 16
    • 8344260568 scopus 로고    scopus 로고
    • Ferritin heavy chain upregulation by NF-kappaB inhibits TNFalpha-induced apoptosis by suppressing reactive oxygen species
    • Pham CG, et al. (2004) Ferritin heavy chain upregulation by NF-kappaB inhibits TNFalpha-induced apoptosis by suppressing reactive oxygen species. Cell 119:529-542.
    • (2004) Cell , vol.119 , pp. 529-542
    • Pham, C.G.1
  • 17
    • 0035984912 scopus 로고    scopus 로고
    • ROS, stress-activated kinases and stress signaling in cancer
    • Benhar M, Engelberg D, Levitzki A (2002) ROS, stress-activated kinases and stress signaling in cancer. EMBO Rep 3:420-425.
    • (2002) EMBO Rep , vol.3 , pp. 420-425
    • Benhar, M.1    Engelberg, D.2    Levitzki, A.3
  • 18
    • 33748165596 scopus 로고    scopus 로고
    • Reactive oxygen species in cancer cells: Live by the sword, die by the sword
    • Schumacker PT (2006) Reactive oxygen species in cancer cells: Live by the sword, die by the sword. Cancer Cell 10:175-176.
    • (2006) Cancer Cell , vol.10 , pp. 175-176
    • Schumacker, P.T.1
  • 20
    • 44449126104 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS) in multistage carcinogenesis
    • Panayiotidis M (2008) Reactive oxygen species (ROS) in multistage carcinogenesis. Cancer Lett 266:3-5.
    • (2008) Cancer Lett , vol.266 , pp. 3-5
    • Panayiotidis, M.1
  • 21
    • 43249112094 scopus 로고    scopus 로고
    • ROS-generating mitochondrial DNA mutations can regulate tumor cell metastasis
    • Ishikawa K, et al. (2008) ROS-generating mitochondrial DNA mutations can regulate tumor cell metastasis. Science 320:661-664.
    • (2008) Science , vol.320 , pp. 661-664
    • Ishikawa, K.1
  • 22
    • 48649109203 scopus 로고    scopus 로고
    • Hepatocyte necrosis induced by oxidative stress and IL-1 alpha release mediate carcinogen-induced compensatory proliferation and liver tumorigenesis
    • Sakurai T, et al. (2008) Hepatocyte necrosis induced by oxidative stress and IL-1 alpha release mediate carcinogen-induced compensatory proliferation and liver tumorigenesis. Cancer Cell 14:156-165.
    • (2008) Cancer Cell , vol.14 , pp. 156-165
    • Sakurai, T.1
  • 23
    • 40949159866 scopus 로고    scopus 로고
    • Oxidative stress is inherent in prostate cancer cells and is required for aggressive phenotype
    • Kumar B, Koul S, Khandrika L, Meacham RB, Koul HK (2008) Oxidative stress is inherent in prostate cancer cells and is required for aggressive phenotype. Cancer Res 68:1777-1785.
    • (2008) Cancer Res , vol.68 , pp. 1777-1785
    • Kumar, B.1    Koul, S.2    Khandrika, L.3    Meacham, R.B.4    Koul, H.K.5
  • 24
    • 33748146888 scopus 로고    scopus 로고
    • Selective killing of oncogenically transformed cells through a ROS-mediated mechanism by beta-phenylethyl isothiocyanate
    • Trachootham D, et al. (2006) Selective killing of oncogenically transformed cells through a ROS-mediated mechanism by beta-phenylethyl isothiocyanate. Cancer Cell 10:241-252.
    • (2006) Cancer Cell , vol.10 , pp. 241-252
    • Trachootham, D.1
  • 25
    • 38549145044 scopus 로고    scopus 로고
    • Diagnosing and exploiting cancer's addiction to blocks in apoptosis
    • Letai AG (2008) Diagnosing and exploiting cancer's addiction to blocks in apoptosis. Nat Rev Cancer 8:121-132.
    • (2008) Nat Rev Cancer , vol.8 , pp. 121-132
    • Letai, A.G.1
  • 26
    • 33847392378 scopus 로고    scopus 로고
    • Wild-type p53: Tumors can't stand it
    • Kastan MB (2007) Wild-type p53: Tumors can't stand it. Cell 128:837-840.
    • (2007) Cell , vol.128 , pp. 837-840
    • Kastan, M.B.1
  • 27
    • 42449123761 scopus 로고    scopus 로고
    • Expansion and evolution of cell death programmes
    • Degterev A, Yuan J (2008) Expansion and evolution of cell death programmes. Nat Rev Mol Cell Biol 9:378-390.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 378-390
    • Degterev, A.1    Yuan, J.2
  • 28
    • 44449160071 scopus 로고    scopus 로고
    • Superoxide dismutase 1 (SOD1) is essential for H2O2-mediated oxidation and inactivation of phosphatases in growth factor signaling
    • Juarez JC, et al. (2008) Superoxide dismutase 1 (SOD1) is essential for H2O2-mediated oxidation and inactivation of phosphatases in growth factor signaling. Proc Natl Acad Sci USA 105:7147-7152.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 7147-7152
    • Juarez, J.C.1
  • 29
    • 0036605993 scopus 로고    scopus 로고
    • Disruption of the NAD(P)H:quinone oxidoreductase 1 (NQO1) gene in mice causes myelogenous hyperplasia
    • Long DJ 2nd, et al. (2002) Disruption of the NAD(P)H:quinone oxidoreductase 1 (NQO1) gene in mice causes myelogenous hyperplasia. Cancer Res 62:3030-3036.
    • (2002) Cancer Res , vol.62 , pp. 3030-3036
    • Long 2nd, D.J.1
  • 30
    • 33645052709 scopus 로고    scopus 로고
    • Genetic polymorphisms in antioxidant enzymes modulate hepatic iron accumulation and hepatocellular carcinoma development in patients with alcohol-induced cirrhosis
    • Sutton A, et al. (2006) Genetic polymorphisms in antioxidant enzymes modulate hepatic iron accumulation and hepatocellular carcinoma development in patients with alcohol-induced cirrhosis. Cancer Res 66:2844-2852.
    • (2006) Cancer Res , vol.66 , pp. 2844-2852
    • Sutton, A.1
  • 31
    • 36249026245 scopus 로고    scopus 로고
    • The mitochondrial thioredoxin system regulates nitric oxide-induced HIF-1alpha protein
    • Zhou J, Eleni C, Spyrou G, Brune B (2008) The mitochondrial thioredoxin system regulates nitric oxide-induced HIF-1alpha protein. Free Radic Biol Med 44:91-98.
    • (2008) Free Radic Biol Med , vol.44 , pp. 91-98
    • Zhou, J.1    Eleni, C.2    Spyrou, G.3    Brune, B.4
  • 32
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge W (2002) Free radicals in the physiological control of cell function. Physiol Rev 82:47-95.
    • (2002) Physiol Rev , vol.82 , pp. 47-95
    • Droge, W.1
  • 33
    • 42249088093 scopus 로고    scopus 로고
    • Reconciling the chemistry and biology of reactive oxygen species
    • Winterbourn CC (2008) Reconciling the chemistry and biology of reactive oxygen species. Nat Chem Biol 4:278-286.
    • (2008) Nat Chem Biol , vol.4 , pp. 278-286
    • Winterbourn, C.C.1
  • 34
    • 46649090918 scopus 로고    scopus 로고
    • Protein tyrosine nitration - Functional alteration or just a biomarker?
    • Souza JM, Peluffo G, Radi R (2008) Protein tyrosine nitration - Functional alteration or just a biomarker? Free Radic Biol Med 45:357-366.
    • (2008) Free Radic Biol Med , vol.45 , pp. 357-366
    • Souza, J.M.1    Peluffo, G.2    Radi, R.3
  • 35
    • 33646589634 scopus 로고    scopus 로고
    • Subcellular localization of tyrosine-nitrated proteins is dictated by reactive oxygen species generating enzymes and by proximity to nitric oxide synthase
    • Heijnen HF, et al. (2006) Subcellular localization of tyrosine-nitrated proteins is dictated by reactive oxygen species generating enzymes and by proximity to nitric oxide synthase. Free Radic Biol Med 40:1903-1913.
    • (2006) Free Radic Biol Med , vol.40 , pp. 1903-1913
    • Heijnen, H.F.1
  • 37
    • 42649144101 scopus 로고    scopus 로고
    • Oxidative and nitrative protein modifications in Parkinson's disease
    • Danielson SR, Andersen JK (2008) Oxidative and nitrative protein modifications in Parkinson's disease. Free Radic Biol Med 44:1787-1794.
    • (2008) Free Radic Biol Med , vol.44 , pp. 1787-1794
    • Danielson, S.R.1    Andersen, J.K.2
  • 38
    • 0027499362 scopus 로고
    • Molecular cloning and expression of a human anterior pituitary receptor for growth hormone-releasing hormone
    • Gaylinn BD, et al. (1993) Molecular cloning and expression of a human anterior pituitary receptor for growth hormone-releasing hormone. Mol Endocrinol 7:77-84.
    • (1993) Mol Endocrinol , vol.7 , pp. 77-84
    • Gaylinn, B.D.1
  • 39
    • 0027458399 scopus 로고
    • Development of a radioimmunoassay for some agonists of growth hormone-releasing hormone
    • Groot K, et al. (1993) Development of a radioimmunoassay for some agonists of growth hormone-releasing hormone. Int J Pept Protein Res 41:162-168.
    • (1993) Int J Pept Protein Res , vol.41 , pp. 162-168
    • Groot, K.1
  • 40
    • 0037011989 scopus 로고    scopus 로고
    • Expression of prostate specific antigen (PSA) is negatively regulated by p53
    • Gurova KV, et al. (2002) Expression of prostate specific antigen (PSA) is negatively regulated by p53. Oncogene 21:153-157.
    • (2002) Oncogene , vol.21 , pp. 153-157
    • Gurova, K.V.1
  • 41
    • 0141482040 scopus 로고    scopus 로고
    • Antisense therapy targeting MDM2 oncogene in prostate cancer: Effects on proliferation, apoptosis, multiple gene expression, and chemotherapy
    • Zhang Z, Li M, Wang H, Agrawal S, Zhang R (2003) Antisense therapy targeting MDM2 oncogene in prostate cancer: Effects on proliferation, apoptosis, multiple gene expression, and chemotherapy. Proc Natl Acad Sci USA 100:11636-11641.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11636-11641
    • Zhang, Z.1    Li, M.2    Wang, H.3    Agrawal, S.4    Zhang, R.5
  • 44
    • 28644447272 scopus 로고    scopus 로고
    • The antioxidant function of the p53 tumor suppressor
    • Sablina AA, et al. (2005) The antioxidant function of the p53 tumor suppressor. Nat Med 11:1306-1313.
    • (2005) Nat Med , vol.11 , pp. 1306-1313
    • Sablina, A.A.1
  • 45
    • 28644448262 scopus 로고    scopus 로고
    • Savior and slayer: The two faces of p53
    • Bensaad K, Vousden KH (2005) Savior and slayer: The two faces of p53. Nat Med 11:1278-1279.
    • (2005) Nat Med , vol.11 , pp. 1278-1279
    • Bensaad, K.1    Vousden, K.H.2
  • 46
    • 33745863668 scopus 로고    scopus 로고
    • Autocrine/paracrine regulation of breast cancer cell proliferation by growth hormone releasing hormone via Ras, Raf, and mitogen-activated protein kinase
    • Siriwardana G, Bradford A, Coy D, Zeitler P (2006) Autocrine/paracrine regulation of breast cancer cell proliferation by growth hormone releasing hormone via Ras, Raf, and mitogen-activated protein kinase. Mol Endocrinol 20:2010-2019.
    • (2006) Mol Endocrinol , vol.20 , pp. 2010-2019
    • Siriwardana, G.1    Bradford, A.2    Coy, D.3    Zeitler, P.4
  • 47
    • 0034457676 scopus 로고    scopus 로고
    • Growth hormone-releasing hormone stimulates mitogen-activated protein kinase
    • Pombo CM, Zalvide J, Gaylinn BD, Dieguez C (2000) Growth hormone-releasing hormone stimulates mitogen-activated protein kinase. Endocrinology 141:2113-2119.
    • (2000) Endocrinology , vol.141 , pp. 2113-2119
    • Pombo, C.M.1    Zalvide, J.2    Gaylinn, B.D.3    Dieguez, C.4
  • 48
    • 0034871822 scopus 로고    scopus 로고
    • Peptides derived from pro-growth hormone-releasing hormone activate p38 mitogen-activated protein kinase in GH3 pituitary cells
    • Steinmetz R, Zeng P, King DW, Walvoord E, Pescovitz OH (2001) Peptides derived from pro-growth hormone-releasing hormone activate p38 mitogen-activated protein kinase in GH3 pituitary cells. Endocrine 15:119-127.
    • (2001) Endocrine , vol.15 , pp. 119-127
    • Steinmetz, R.1    Zeng, P.2    King, D.W.3    Walvoord, E.4    Pescovitz, O.H.5
  • 49
    • 0033919689 scopus 로고    scopus 로고
    • Stimulation of mitogen-activated protein kinase pathway in rat somatotrophs by growth hormone-releasing hormone
    • Zeitler P, Siriwardana G (2000) Stimulation of mitogen-activated protein kinase pathway in rat somatotrophs by growth hormone-releasing hormone. Endocrine 12:257-264.
    • (2000) Endocrine , vol.12 , pp. 257-264
    • Zeitler, P.1    Siriwardana, G.2
  • 50
    • 33846811520 scopus 로고    scopus 로고
    • p38alpha MAP kinase as a sensor of reactive oxygen species in tumorigenesis
    • Dolado I, et al. (2007) p38alpha MAP kinase as a sensor of reactive oxygen species in tumorigenesis. Cancer Cell 11:191-205.
    • (2007) Cancer Cell , vol.11 , pp. 191-205
    • Dolado, I.1
  • 51
    • 0030034524 scopus 로고    scopus 로고
    • Transcriptional activation of the human proliferating-cell nuclear antigen promoter by p53
    • Morris GF, Bischoff JR, Mathews MB (1996) Transcriptional activation of the human proliferating-cell nuclear antigen promoter by p53. Proc Natl Acad Sci USA 93:895-899.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 895-899
    • Morris, G.F.1    Bischoff, J.R.2    Mathews, M.B.3
  • 52
    • 33747823839 scopus 로고    scopus 로고
    • L2DTL/CDT2 and PCNA interact with p53 and regulate p53 polyubiquitination and protein stability through MDM2 and CUL4A/DDB1 complexes
    • Banks, et al. (2006) L2DTL/CDT2 and PCNA interact with p53 and regulate p53 polyubiquitination and protein stability through MDM2 and CUL4A/DDB1 complexes. Cell Cycle 5:1719-1729.
    • (2006) Cell Cycle , vol.5 , pp. 1719-1729
    • Banks1
  • 53
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
    • D'Autreaux B, Toledano MB (2007) ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis. Nat Rev Mol Cell Biol 8:813-824.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 813-824
    • D'Autreaux, B.1    Toledano, M.B.2
  • 54
    • 0036311835 scopus 로고    scopus 로고
    • Antagonism of endogenous growth hormone-releasing hormone (GHRH) leads to reduced proliferation and apoptosis in MDA231 breast cancer cells
    • Zeitler P, Siriwardana G (2002) Antagonism of endogenous growth hormone-releasing hormone (GHRH) leads to reduced proliferation and apoptosis in MDA231 breast cancer cells. Endocrine 18:85-90.
    • (2002) Endocrine , vol.18 , pp. 85-90
    • Zeitler, P.1    Siriwardana, G.2
  • 55
    • 14744277399 scopus 로고    scopus 로고
    • Antagonist of growth hormone-releasing hormone induces apoptosis in LNCaP human prostate cancer cells through a Ca2+-dependent pathway
    • Rekasi Z, et al. (2005) Antagonist of growth hormone-releasing hormone induces apoptosis in LNCaP human prostate cancer cells through a Ca2+-dependent pathway. Proc Natl Acad Sci USA 102:3435-3440.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3435-3440
    • Rekasi, Z.1
  • 56
    • 0032582793 scopus 로고    scopus 로고
    • Ras promotes cell survival in Drosophila by downregulating hid expression
    • Kurada P, White K (1998) Ras promotes cell survival in Drosophila by downregulating hid expression. Cell 95:319-329.
    • (1998) Cell , vol.95 , pp. 319-329
    • Kurada, P.1    White, K.2
  • 57
    • 0034103549 scopus 로고    scopus 로고
    • The p42/p44 MAP kinase pathway prevents apoptosis induced by anchorage and serum removal
    • Le Gall M, et al. (2000) The p42/p44 MAP kinase pathway prevents apoptosis induced by anchorage and serum removal. Mol Biol Cell 11:1103-1112.
    • (2000) Mol Biol Cell , vol.11 , pp. 1103-1112
    • Le Gall, M.1
  • 58
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-kappaB signaling
    • Hayden MS, Ghosh S (2008) Shared principles in NF-kappaB signaling. Cell 132:344-362.
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 59
    • 4544342570 scopus 로고    scopus 로고
    • Nuclear factor-kappaB: The enemy within
    • Aggarwal BB (2004) Nuclear factor-kappaB: The enemy within. Cancer Cell 6:203-208.
    • (2004) Cancer Cell , vol.6 , pp. 203-208
    • Aggarwal, B.B.1
  • 60
    • 36248973110 scopus 로고    scopus 로고
    • NF-kappa B-mediated adaptive resistance to ionizing radiation
    • Ahmed KM, Li JJ (2008) NF-kappa B-mediated adaptive resistance to ionizing radiation. Free Radic Biol Med 44:1-13.
    • (2008) Free Radic Biol Med , vol.44 , pp. 1-13
    • Ahmed, K.M.1    Li, J.J.2
  • 61
    • 0037449777 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of I kappa B alpha activates NF kappa B through a redox-regulated and c-Src-dependent mechanism following hypoxia/reoxygenation
    • Fan C, Li Q, Ross D, Engelhardt JF (2003) Tyrosine phosphorylation of I kappa B alpha activates NF kappa B through a redox-regulated and c-Src-dependent mechanism following hypoxia/reoxygenation. J Biol Chem 278:2072-2080.
    • (2003) J Biol Chem , vol.278 , pp. 2072-2080
    • Fan, C.1    Li, Q.2    Ross, D.3    Engelhardt, J.F.4
  • 62
    • 37849045126 scopus 로고    scopus 로고
    • Exercise and immobilization in aging animals: The involvement of oxidative stress and NF-kappaB activation
    • Bar-Shai M, Carmeli E, Ljubuncic P, Reznick AZ (2008) Exercise and immobilization in aging animals: The involvement of oxidative stress and NF-kappaB activation. Free Radic Biol Med 44:202-214.
    • (2008) Free Radic Biol Med , vol.44 , pp. 202-214
    • Bar-Shai, M.1    Carmeli, E.2    Ljubuncic, P.3    Reznick, A.Z.4
  • 63
    • 0034628544 scopus 로고    scopus 로고
    • Overexpression of the wild-type p53 gene inhibits NF-kappaB activity and synergizes with aspirin to induce apoptosis in human colon cancer cells
    • Shao J, et al. (2000) Overexpression of the wild-type p53 gene inhibits NF-kappaB activity and synergizes with aspirin to induce apoptosis in human colon cancer cells. Oncogene 19:726-736.
    • (2000) Oncogene , vol.19 , pp. 726-736
    • Shao, J.1
  • 64
    • 0034699513 scopus 로고    scopus 로고
    • Superoxide dismutase as a target for the selective killing of cancer cells
    • Huang, Feng L, Oldham EA, Keating MJ, Plunkett W (2000) Superoxide dismutase as a target for the selective killing of cancer cells. Nature 407:390-395.
    • (2000) Nature , vol.407 , pp. 390-395
    • Huang1    Feng, L.2    Oldham, E.A.3    Keating, M.J.4    Plunkett, W.5
  • 65
    • 0141866708 scopus 로고    scopus 로고
    • Superoxide dismutase 1 knock-down induces senescence in human fibroblasts
    • Blander G, de Oliveira RM, Conboy CM, Haigis M, Guarente L (2003) Superoxide dismutase 1 knock-down induces senescence in human fibroblasts. J Biol Chem 278:38966-38969.
    • (2003) J Biol Chem , vol.278 , pp. 38966-38969
    • Blander, G.1    de Oliveira, R.M.2    Conboy, C.M.3    Haigis, M.4    Guarente, L.5
  • 66
    • 44349157832 scopus 로고    scopus 로고
    • Cycling hypoxia and free radicals regulate angiogenesis and radiotherapy response
    • Dewhirst MW, Cao Y, Moeller B (2008) Cycling hypoxia and free radicals regulate angiogenesis and radiotherapy response. Nat Rev Cancer 8:425-437.
    • (2008) Nat Rev Cancer , vol.8 , pp. 425-437
    • Dewhirst, M.W.1    Cao, Y.2    Moeller, B.3
  • 67
    • 0037044722 scopus 로고    scopus 로고
    • Glutathione peroxidase-1 protects from CD95-induced apoptosis
    • Gouaze V, et al. (2002) Glutathione peroxidase-1 protects from CD95-induced apoptosis. J Biol Chem 277:42867-42874.
    • (2002) J Biol Chem , vol.277 , pp. 42867-42874
    • Gouaze, V.1
  • 68
    • 0141994844 scopus 로고    scopus 로고
    • Glutathione peroxidase 1 is regulated by the c-Abl and Arg tyrosine kinases
    • Cao C, Leng Y, Huang W, Liu X, Kufe D (2003) Glutathione peroxidase 1 is regulated by the c-Abl and Arg tyrosine kinases. J Biol Chem 278:39609-39614.
    • (2003) J Biol Chem , vol.278 , pp. 39609-39614
    • Cao, C.1    Leng, Y.2    Huang, W.3    Liu, X.4    Kufe, D.5
  • 69
    • 33846000687 scopus 로고    scopus 로고
    • p53 suppresses the Nrf2-dependent transcription of antioxidant response genes
    • Faraonio R, et al. (2006) p53 suppresses the Nrf2-dependent transcription of antioxidant response genes. J Biol Chem 281:39776-39784.
    • (2006) J Biol Chem , vol.281 , pp. 39776-39784
    • Faraonio, R.1
  • 70
    • 33747348720 scopus 로고    scopus 로고
    • Cyclooxygenase-2-dependent neuronal death proceeds via superoxide anion generation
    • Im JY, Kim D, Paik SG, Han PL (2006) Cyclooxygenase-2-dependent neuronal death proceeds via superoxide anion generation. Free Radic Biol Med 41:960-972.
    • (2006) Free Radic Biol Med , vol.41 , pp. 960-972
    • Im, J.Y.1    Kim, D.2    Paik, S.G.3    Han, P.L.4
  • 71
    • 0345803000 scopus 로고    scopus 로고
    • Alterations in subcellular localization of p38 MAPK potentiates endothelin-stimulated COX-2 expression in glomerular mesangial cells
    • Pratt PF, Bokemeyer D, Foschi M, Sorokin A, Dunn MJ (2003) Alterations in subcellular localization of p38 MAPK potentiates endothelin-stimulated COX-2 expression in glomerular mesangial cells. J Biol Chem 278:51928-51936.
    • (2003) J Biol Chem , vol.278 , pp. 51928-51936
    • Pratt, P.F.1    Bokemeyer, D.2    Foschi, M.3    Sorokin, A.4    Dunn, M.J.5
  • 72
    • 47049086972 scopus 로고    scopus 로고
    • COX2 expression and Erk1/Erk2 activity mediate Cot-induced cell migration
    • Rodriguez C, et al. (2008) COX2 expression and Erk1/Erk2 activity mediate Cot-induced cell migration. Cell Signal. 20:1625-1631.
    • (2008) Cell Signal , vol.20 , pp. 1625-1631
    • Rodriguez, C.1
  • 73
    • 0033781454 scopus 로고    scopus 로고
    • Modulation of protein kinase activity and gene expression by reactive oxygen species and their role in vascular physiology and pathophysiology
    • Griendling KK, Sorescu D, Lassegue B, Ushio-Fukai M (2000) Modulation of protein kinase activity and gene expression by reactive oxygen species and their role in vascular physiology and pathophysiology. Arterioscler Thromb Vasc Biol 20:2175-2183.
    • (2000) Arterioscler Thromb Vasc Biol , vol.20 , pp. 2175-2183
    • Griendling, K.K.1    Sorescu, D.2    Lassegue, B.3    Ushio-Fukai, M.4
  • 74
    • 0142043984 scopus 로고    scopus 로고
    • Redox signaling and the MAP kinase pathways
    • Torres M, Forman HJ (2003) Redox signaling and the MAP kinase pathways. Biofactors 17:287-296.
    • (2003) Biofactors , vol.17 , pp. 287-296
    • Torres, M.1    Forman, H.J.2
  • 75
    • 2642551439 scopus 로고    scopus 로고
    • Angiotensin II and endothelin-1 regulate MAP kinases through different redox-dependent mechanisms in human vascular smooth muscle cells
    • Touyz RM, Yao G, Viel E, Amiri F, Schiffrin EL (2004) Angiotensin II and endothelin-1 regulate MAP kinases through different redox-dependent mechanisms in human vascular smooth muscle cells. J Hypertens 22:1141-1149.
    • (2004) J Hypertens , vol.22 , pp. 1141-1149
    • Touyz, R.M.1    Yao, G.2    Viel, E.3    Amiri, F.4    Schiffrin, E.L.5
  • 76
    • 0037088584 scopus 로고    scopus 로고
    • Hydrogen peroxide stimulates c-Src-mediated big mitogen-activated protein kinase 1 (BMK1) and the MEF2C signaling pathway in PC12 cells: Potential role in cell survival following oxidative insults
    • Suzaki Y, et al. (2002) Hydrogen peroxide stimulates c-Src-mediated big mitogen-activated protein kinase 1 (BMK1) and the MEF2C signaling pathway in PC12 cells: Potential role in cell survival following oxidative insults. J Biol Chem 277:9614 -9621.
    • (2002) J Biol Chem , vol.277 , pp. 9614-9621
    • Suzaki, Y.1
  • 77
    • 22044443715 scopus 로고    scopus 로고
    • H2O2-induced phosphorylation of ERK1/2 and PKB requires tyrosine kinase activity of insulin receptor and c-Src
    • Mehdi MZ, Pandey NR, Pandey SK, Srivastava AK (2005) H2O2-induced phosphorylation of ERK1/2 and PKB requires tyrosine kinase activity of insulin receptor and c-Src. Antioxid Redox Signal 7:1014-1020.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 1014-1020
    • Mehdi, M.Z.1    Pandey, N.R.2    Pandey, S.K.3    Srivastava, A.K.4
  • 78
    • 0042847291 scopus 로고    scopus 로고
    • Neurotoxic mechanisms caused by the Alzheimer's disease-linked Swedish amyloid precursor protein mutation: Oxidative stress, caspases, and the JNK pathway
    • Marques CA, et al. (2003) Neurotoxic mechanisms caused by the Alzheimer's disease-linked Swedish amyloid precursor protein mutation: Oxidative stress, caspases, and the JNK pathway. J Biol Chem 278:28294-28302.
    • (2003) J Biol Chem , vol.278 , pp. 28294-28302
    • Marques, C.A.1
  • 79
    • 11844272574 scopus 로고    scopus 로고
    • Atrial natriuretic peptide induces mitogen-activated protein kinase phosphatase-1 in human endothelial cells via Rac1 and NAD(P)H oxidase/Nox2-activation
    • Furst R, et al. (2005) Atrial natriuretic peptide induces mitogen-activated protein kinase phosphatase-1 in human endothelial cells via Rac1 and NAD(P)H oxidase/Nox2-activation. Circ Res 96:43-53.
    • (2005) Circ Res , vol.96 , pp. 43-53
    • Furst, R.1
  • 80
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • Bedard K, Krause KH (2007) The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology. Physiol Rev 87:245-313.
    • (2007) Physiol Rev , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 81
    • 39949085776 scopus 로고    scopus 로고
    • Oxidative stress and vascular disease in diabetes: Is the dichotomization of insulin signaling still valid?
    • Avogaro A, de Kreutzenberg SV, Fadini GP (2008) Oxidative stress and vascular disease in diabetes: Is the dichotomization of insulin signaling still valid? Free Radic Biol Med 44:1209-1215.
    • (2008) Free Radic Biol Med , vol.44 , pp. 1209-1215
    • Avogaro, A.1    de Kreutzenberg, S.V.2    Fadini, G.P.3
  • 82
    • 36148955406 scopus 로고    scopus 로고
    • Externally applied pressure activates pancreatic stellate cells through the generation of intracellular reactive oxygen species
    • Asaumi H, Watanabe S, Taguchi M, Tashiro M, Otsuki M (2007) Externally applied pressure activates pancreatic stellate cells through the generation of intracellular reactive oxygen species. Am J Physiol Gastrointest Liver Physiol 293:G972-G978.
    • (2007) Am J Physiol Gastrointest Liver Physiol , vol.293
    • Asaumi, H.1    Watanabe, S.2    Taguchi, M.3    Tashiro, M.4    Otsuki, M.5
  • 83
    • 33750471197 scopus 로고    scopus 로고
    • Mutual cross-talk between reactive oxygen species and nuclear factor-kappa B: Molecular basis and biological significance
    • Bubici C, Papa S, Dean K, Franzoso G (2006) Mutual cross-talk between reactive oxygen species and nuclear factor-kappa B: Molecular basis and biological significance. Oncogene 25:6731-6748.
    • (2006) Oncogene , vol.25 , pp. 6731-6748
    • Bubici, C.1    Papa, S.2    Dean, K.3    Franzoso, G.4
  • 84
    • 28844473846 scopus 로고    scopus 로고
    • Radical medicine: Treating ageing to cure disease
    • Finkel T (2005) Radical medicine: Treating ageing to cure disease. Nat Rev Mol Cell Biol 6:971-976.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 971-976
    • Finkel, T.1
  • 85
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • Finkel T, Holbrook NJ (2000) Oxidants, oxidative stress and the biology of ageing. Nature 408:239-247.
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 86
    • 33645860825 scopus 로고    scopus 로고
    • Reactive oxygen species have a causal role in multiple forms of insulin resistance
    • Houstis N, Rosen ED, Lander ES (2006) Reactive oxygen species have a causal role in multiple forms of insulin resistance. Nature 440:944-948.
    • (2006) Nature , vol.440 , pp. 944-948
    • Houstis, N.1    Rosen, E.D.2    Lander, E.S.3
  • 87
    • 0036796875 scopus 로고    scopus 로고
    • Oxidative stress and stress-activated signaling pathways: A unifying hypothesis of type 2 diabetes
    • Evans JL, Goldfine ID, Maddux BA, Grodsky GM (2002) Oxidative stress and stress-activated signaling pathways: A unifying hypothesis of type 2 diabetes. Endocr Rev 23:599-622.
    • (2002) Endocr Rev , vol.23 , pp. 599-622
    • Evans, J.L.1    Goldfine, I.D.2    Maddux, B.A.3    Grodsky, G.M.4
  • 88
    • 17644413217 scopus 로고    scopus 로고
    • Reactive oxygen and nitrogen species: Weapons of neuronal destruction in models of Parkinson's disease
    • Przedborski S, Ischiropoulos H (2005) Reactive oxygen and nitrogen species: Weapons of neuronal destruction in models of Parkinson's disease. Antioxid Redox Signal 7:685-693.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 685-693
    • Przedborski, S.1    Ischiropoulos, H.2
  • 89
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin MT, Beal MF (2006) Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443:787-795.
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.