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Volumn 34, Issue 8, 2013, Pages 1843-1851

Induction of heme oxygenase-1 and inhibition of TPA-induced matrix metalloproteinase-9 expression by andrographolide in MCF-7 human breast cancer cells

Author keywords

[No Author keywords available]

Indexed keywords

ANDROGRAPHOLIDE; BILIRUBIN; CARBON MONOXIDE; GELATINASE B; HEME OXYGENASE 1; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; IRON; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROTEIN KINASE B; SMALL INTERFERING RNA; TRANSCRIPTION FACTOR AP 1;

EID: 84881493942     PISSN: 01433334     EISSN: 14602180     Source Type: Journal    
DOI: 10.1093/carcin/bgt131     Document Type: Article
Times cited : (64)

References (53)
  • 1
    • 0003964363 scopus 로고    scopus 로고
    • American Cancer Society, American Cancer Society, Atlanta, GA
    • American Cancer Society. (2007) Cancer Facts & Figures 2007. American Cancer Society, Atlanta, GA.
    • (2007) Cancer Facts & Figures 2007
  • 2
    • 49849103925 scopus 로고    scopus 로고
    • Heme oxygenase-1 inhibits breast cancer invasion via suppressing the expression of matrix metalloproteinase-9
    • Lin, C.W. et al. (2008) Heme oxygenase-1 inhibits breast cancer invasion via suppressing the expression of matrix metalloproteinase-9. Mol. Cancer Ther., 7, 1195-1206.
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 1195-1206
    • Lin, C.W.1
  • 3
    • 78650424066 scopus 로고    scopus 로고
    • Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting
    • Gialeli, C. et al. (2011) Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting. FEBS J., 278, 16-27.
    • (2011) FEBS J. , vol.278 , pp. 16-27
    • Gialeli, C.1
  • 4
    • 0036716282 scopus 로고    scopus 로고
    • Strategies for MMP inhibition in cancer: innovations for the post-trial era
    • Overall, C.M. et al. (2002) Strategies for MMP inhibition in cancer: innovations for the post-trial era. Nat. Rev. Cancer, 2, 657-672.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 657-672
    • Overall, C.M.1
  • 5
    • 70449732503 scopus 로고    scopus 로고
    • Matrix metalloproteinases as novel biomarkers and potential therapeutic targets in human cancer
    • Roy, R. et al. (2009) Matrix metalloproteinases as novel biomarkers and potential therapeutic targets in human cancer. J. Clin. Oncol., 27, 5287-5297.
    • (2009) J. Clin. Oncol. , vol.27 , pp. 5287-5297
    • Roy, R.1
  • 6
    • 9344271530 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase (MMP)-2 and MMP-9 in breast cancer with a special reference to activator protein-2, HER2, and prognosis
    • Pellikainen, J.M. et al. (2004) Expression of matrix metalloproteinase (MMP)-2 and MMP-9 in breast cancer with a special reference to activator protein-2, HER2, and prognosis. Clin. Cancer Res., 10, 7621-7628.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 7621-7628
    • Pellikainen, J.M.1
  • 7
    • 79960913880 scopus 로고    scopus 로고
    • Absence of Thy-1 results in TGF-ß induced MMP-9 expression and confers a profibrotic phenotype to human lung fibroblasts
    • Ramírez, G. et al. (2011) Absence of Thy-1 results in TGF-ß induced MMP-9 expression and confers a profibrotic phenotype to human lung fibroblasts. Lab. Invest., 91, 1206-1218.
    • (2011) Lab. Invest. , vol.91 , pp. 1206-1218
    • Ramírez, G.1
  • 8
    • 79958018646 scopus 로고    scopus 로고
    • 3-Deoxysappanchalcone inhibits tumor necrosis factor-a-induced matrix metalloproteinase-9 expression in human keratinocytes through activated protein-1 inhibition and nuclear factorkappa B DNA binding activity
    • Youn, U.J. et al. (2011) 3-Deoxysappanchalcone inhibits tumor necrosis factor-a-induced matrix metalloproteinase-9 expression in human keratinocytes through activated protein-1 inhibition and nuclear factorkappa B DNA binding activity. Biol. Pharm. Bull., 34, 890-893.
    • (2011) Biol. Pharm. Bull. , vol.34 , pp. 890-893
    • Youn, U.J.1
  • 9
    • 77949425064 scopus 로고    scopus 로고
    • Melittin suppresses PMA-induced tumor cell invasion by inhibiting NF-kappaB and AP-1-dependent MMP-9 expression
    • Park, J.H. et al. (2010) Melittin suppresses PMA-induced tumor cell invasion by inhibiting NF-kappaB and AP-1-dependent MMP-9 expression. Mol. Cells, 29, 209-215.
    • (2010) Mol. Cells , vol.29 , pp. 209-215
    • Park, J.H.1
  • 10
    • 84860437626 scopus 로고    scopus 로고
    • Selective inhibition of MMP-9 gene expression by mangiferin in PMA-stimulated human astroglioma cells: involvement of PI3K/Akt and MAPK signaling pathways
    • Jung, J.S. et al. (2012) Selective inhibition of MMP-9 gene expression by mangiferin in PMA-stimulated human astroglioma cells: involvement of PI3K/Akt and MAPK signaling pathways. Pharmacol. Res., 66, 95-103.
    • (2012) Pharmacol. Res. , vol.66 , pp. 95-103
    • Jung, J.S.1
  • 11
    • 79958723466 scopus 로고    scopus 로고
    • Pachymic acid impairs breast cancer cell invasion by suppressing nuclear factor-κB-dependent matrix metalloproteinase-9 expression
    • Ling, H. et al. (2011) Pachymic acid impairs breast cancer cell invasion by suppressing nuclear factor-κB-dependent matrix metalloproteinase-9 expression. Breast Cancer Res. Treat., 126, 609-620.
    • (2011) Breast Cancer Res. Treat. , vol.126 , pp. 609-620
    • Ling, H.1
  • 12
    • 38849178686 scopus 로고    scopus 로고
    • Lucidenic acid inhibits PMA-induced invasion of human hepatoma cells through inactivating MAPK/ERK signal transduction pathway and reducing binding activities of NF-kappaB and AP-1
    • Weng, C.J. et al. (2008) Lucidenic acid inhibits PMA-induced invasion of human hepatoma cells through inactivating MAPK/ERK signal transduction pathway and reducing binding activities of NF-kappaB and AP-1. Carcinogenesis, 29, 147-156.
    • (2008) Carcinogenesis , vol.29 , pp. 147-156
    • Weng, C.J.1
  • 13
    • 50249134405 scopus 로고    scopus 로고
    • Recent advances in plant hepatoprotectives: a chemical and biological profile of some important leads
    • Negi, A.S. et al. (2008) Recent advances in plant hepatoprotectives: a chemical and biological profile of some important leads. Med. Res. Rev., 28, 746-772.
    • (2008) Med. Res. Rev. , vol.28 , pp. 746-772
    • Negi, A.S.1
  • 14
    • 34247607597 scopus 로고    scopus 로고
    • Colds and influenza: a review of diagnosis and conventional, botanical, and nutritional considerations
    • Roxas, M. et al. (2007) Colds and influenza: a review of diagnosis and conventional, botanical, and nutritional considerations. Altern. Med. Rev., 12, 25-48.
    • (2007) Altern. Med. Rev. , vol.12 , pp. 25-48
    • Roxas, M.1
  • 15
    • 80052811947 scopus 로고    scopus 로고
    • Andrographolide inhibits oral squamous cell carcinogenesis through NF-κB inactivation
    • Wang, L.J. et al. (2011) Andrographolide inhibits oral squamous cell carcinogenesis through NF-κB inactivation. J. Dent. Res., 90, 1246-1252.
    • (2011) J. Dent. Res. , vol.90 , pp. 1246-1252
    • Wang, L.J.1
  • 16
    • 82355190327 scopus 로고    scopus 로고
    • Inhibition of TNF-a-Induced Inflammation by andrographolide via down-regulation of the PI3K/Akt signaling pathway
    • Chen, H.W. et al. (2011) Inhibition of TNF-a-Induced Inflammation by andrographolide via down-regulation of the PI3K/Akt signaling pathway. J. Nat. Prod., 74, 2408-2413.
    • (2011) J. Nat. Prod. , vol.74 , pp. 2408-2413
    • Chen, H.W.1
  • 17
    • 68949083038 scopus 로고    scopus 로고
    • Potency of andrographolide as an antitumor compound in BHC-induced liver damage
    • Trivedi, N.P. et al. (2009) Potency of andrographolide as an antitumor compound in BHC-induced liver damage. Integr. Cancer Ther., 8, 177-189.
    • (2009) Integr. Cancer Ther. , vol.8 , pp. 177-189
    • Trivedi, N.P.1
  • 18
    • 67349136453 scopus 로고    scopus 로고
    • Synthesis and evaluation of antibacterial activities of andrographolide analogues
    • Jiang, X. et al. (2009) Synthesis and evaluation of antibacterial activities of andrographolide analogues. Eur. J. Med. Chem., 44, 2936-2943.
    • (2009) Eur. J. Med. Chem. , vol.44 , pp. 2936-2943
    • Jiang, X.1
  • 19
    • 77349091801 scopus 로고    scopus 로고
    • Inhibitory effects of andrographolide on migration and invasion in human non-small cell lung cancer A549 cells via downregulation of PI3K/Akt signaling pathway
    • Lee, Y.C. et al. (2010) Inhibitory effects of andrographolide on migration and invasion in human non-small cell lung cancer A549 cells via downregulation of PI3K/Akt signaling pathway. Eur. J. Pharmacol., 632, 23-32.
    • (2010) Eur. J. Pharmacol. , vol.632 , pp. 23-32
    • Lee, Y.C.1
  • 20
    • 48849109817 scopus 로고    scopus 로고
    • Inhibition of cell-cycle progression in human colorectal carcinoma Lovo cells by andrographolide
    • Shi, M.D. et al. (2008) Inhibition of cell-cycle progression in human colorectal carcinoma Lovo cells by andrographolide. Chem. Biol. Interact., 174, 201-210.
    • (2008) Chem. Biol. Interact. , vol.174 , pp. 201-210
    • Shi, M.D.1
  • 21
    • 84055193133 scopus 로고    scopus 로고
    • Andrographolide induces apoptosis in B16F-10 melanoma cells by inhibiting NF-κB-mediated bcl-2 activation and modulating p53-induced caspase-3 gene expression
    • Pratheeshkumar, P. et al. (2012) Andrographolide induces apoptosis in B16F-10 melanoma cells by inhibiting NF-κB-mediated bcl-2 activation and modulating p53-induced caspase-3 gene expression. Immunopharmacol. Immunotoxicol., 34, 143-151.
    • (2012) Immunopharmacol. Immunotoxicol. , vol.34 , pp. 143-151
    • Pratheeshkumar, P.1
  • 22
    • 0034529932 scopus 로고    scopus 로고
    • Heme oxygenase: colors of defense against cellular stress
    • Otterbein, L.E. et al. (2000) Heme oxygenase: colors of defense against cellular stress. Am. J. Physiol. Lung Cell. Mol. Physiol., 279, L1029-L1037.
    • (2000) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.279
    • Otterbein, L.E.1
  • 23
    • 33750838526 scopus 로고    scopus 로고
    • Heme oxygenase-1 as a potential therapeutic target for hepatoprotection
    • Farombi, E.O. et al. (2006) Heme oxygenase-1 as a potential therapeutic target for hepatoprotection. J. Biochem. Mol. Biol., 39, 479-491.
    • (2006) J. Biochem. Mol. Biol. , vol.39 , pp. 479-491
    • Farombi, E.O.1
  • 24
    • 35848942608 scopus 로고    scopus 로고
    • Heme oxygenase-1 in tumors: is it a false friend?
    • Jozkowicz, A. et al. (2007) Heme oxygenase-1 in tumors: is it a false friend? Antioxid. Redox Signal., 9, 2099-2117.
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 2099-2117
    • Jozkowicz, A.1
  • 25
    • 84855189088 scopus 로고    scopus 로고
    • Heme oxygenase 1 (HO-1) challenges the angiogenic switch in prostate cancer
    • Ferrando, M. et al. (2011) Heme oxygenase 1 (HO-1) challenges the angiogenic switch in prostate cancer. Angiogenesis, 14, 467-479.
    • (2011) Angiogenesis , vol.14 , pp. 467-479
    • Ferrando, M.1
  • 26
    • 28744447937 scopus 로고    scopus 로고
    • Heme oxygenase-1 inhibits rat and human breast cancer cell proliferation: mutual cross inhibition with indoleamine 2,3-dioxygenase
    • Hill, M. et al. (2005) Heme oxygenase-1 inhibits rat and human breast cancer cell proliferation: mutual cross inhibition with indoleamine 2,3-dioxygenase. FASEB J., 19, 1957-1968.
    • (2005) FASEB J. , vol.19 , pp. 1957-1968
    • Hill, M.1
  • 27
    • 0141457852 scopus 로고    scopus 로고
    • Andrographolide, a potential cancer therapeutic agent isolated from Andrographis paniculata
    • Rajagopal, S. et al. (2003) Andrographolide, a potential cancer therapeutic agent isolated from Andrographis paniculata. J. Exp. Ther. Oncol., 3, 147-158.
    • (2003) J. Exp. Ther. Oncol. , vol.3 , pp. 147-158
    • Rajagopal, S.1
  • 28
    • 77954551049 scopus 로고    scopus 로고
    • Induction of heme oxygenase 1 and inhibition of tumor necrosis factor alpha-induced intercellular adhesion molecule expression by andrographolide in EA.hy926 cells
    • Yu, A.L. et al. (2010) Induction of heme oxygenase 1 and inhibition of tumor necrosis factor alpha-induced intercellular adhesion molecule expression by andrographolide in EA.hy926 cells. J. Agric. Food Chem., 58, 7641-7648.
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 7641-7648
    • Yu, A.L.1
  • 29
    • 84870445676 scopus 로고    scopus 로고
    • Docosahexaenoic acid inhibition of inflammation is partially via cross-talk between Nrf2/heme oxygenase 1 and IKK/NF-κB pathways
    • Yang, Y.C. et al. (2013) Docosahexaenoic acid inhibition of inflammation is partially via cross-talk between Nrf2/heme oxygenase 1 and IKK/NF-κB pathways. J. Nutr. Biochem., 24, 204-212.
    • (2013) J. Nutr. Biochem. , vol.24 , pp. 204-212
    • Yang, Y.C.1
  • 30
    • 0035710229 scopus 로고    scopus 로고
    • An overview of real-time quantitative PCR: applications to quantify cytokine gene expression
    • Giulietti, A. et al. (2001) An overview of real-time quantitative PCR: applications to quantify cytokine gene expression. Methods, 25, 386-401.
    • (2001) Methods , vol.25 , pp. 386-401
    • Giulietti, A.1
  • 31
    • 0347355025 scopus 로고    scopus 로고
    • Contribution of conjugated linoleic acid to the suppression of inflammatory responses through the regulation of the NF-kappaB pathway
    • Cheng, W.L. et al. (2004) Contribution of conjugated linoleic acid to the suppression of inflammatory responses through the regulation of the NF-kappaB pathway. J. Agric. Food Chem., 52, 71-78.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 71-78
    • Cheng, W.L.1
  • 32
    • 3142765979 scopus 로고    scopus 로고
    • Silibinin inhibits the invasion of human lung cancer cells via decreased productions of urokinase-plasminogen activator and matrix metalloproteinase-2
    • Chu, S.C. et al. (2004) Silibinin inhibits the invasion of human lung cancer cells via decreased productions of urokinase-plasminogen activator and matrix metalloproteinase-2. Mol. Carcinog., 40, 143-149.
    • (2004) Mol. Carcinog. , vol.40 , pp. 143-149
    • Chu, S.C.1
  • 33
    • 79959982911 scopus 로고    scopus 로고
    • Epigenetic mechanisms for silencing glutathione S-transferase m2 expression by hypermethylated specificity protein 1 binding in lung cancer
    • Tang, S.C. et al. (2011) Epigenetic mechanisms for silencing glutathione S-transferase m2 expression by hypermethylated specificity protein 1 binding in lung cancer. Cancer, 117, 3209-3221.
    • (2011) Cancer , vol.117 , pp. 3209-3221
    • Tang, S.C.1
  • 34
    • 34447634510 scopus 로고    scopus 로고
    • Phorbol 12-myristate 13-acetate (PMA)-induced migration of glioblastoma cells is mediated via p38MAPK/Hsp27 pathway
    • Nomura, N. et al. (2007) Phorbol 12-myristate 13-acetate (PMA)-induced migration of glioblastoma cells is mediated via p38MAPK/Hsp27 pathway. Biochem. Pharmacol., 74, 690-701.
    • (2007) Biochem. Pharmacol. , vol.74 , pp. 690-701
    • Nomura, N.1
  • 35
    • 33748990105 scopus 로고    scopus 로고
    • Protein kinase C and downstream signaling pathways in a three-dimensional model of phorbol ester-induced angiogenesis
    • Taylor, C.J. et al. (2006) Protein kinase C and downstream signaling pathways in a three-dimensional model of phorbol ester-induced angiogenesis. Angiogenesis, 9, 39-51.
    • (2006) Angiogenesis , vol.9 , pp. 39-51
    • Taylor, C.J.1
  • 36
    • 0344845283 scopus 로고    scopus 로고
    • Induction of myofibroblast MMP-9 transcription in three-dimensional collagen I gel cultures: regulation by NF-kappaB, AP-1 and Sp1
    • Takahra, T. et al. (2004) Induction of myofibroblast MMP-9 transcription in three-dimensional collagen I gel cultures: regulation by NF-kappaB, AP-1 and Sp1. Int. J. Biochem. Cell Biol., 36, 353-363.
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 353-363
    • Takahra, T.1
  • 37
    • 84862555961 scopus 로고    scopus 로고
    • Resveratrol chemosensitizes breast cancer cells to melphalan by cell cycle arrest
    • Casanova, F. et al. (2012) Resveratrol chemosensitizes breast cancer cells to melphalan by cell cycle arrest. J. Cell. Biochem., 113, 2586-2596.
    • (2012) J. Cell. Biochem. , vol.113 , pp. 2586-2596
    • Casanova, F.1
  • 38
    • 84860719243 scopus 로고    scopus 로고
    • Quercetin inhibits human breast cancer cell proliferation and induces apoptosis via Bcl-2 and Bax regulation
    • Duo, J. et al. (2012) Quercetin inhibits human breast cancer cell proliferation and induces apoptosis via Bcl-2 and Bax regulation. Mol. Med. Rep., 5, 1453-1456.
    • (2012) Mol. Med. Rep. , vol.5 , pp. 1453-1456
    • Duo, J.1
  • 39
    • 84857381831 scopus 로고    scopus 로고
    • Andrographolide and its analogues: versatile bioactive molecules for combating inflammation and cancer
    • Lim, J.C. et al. (2012) Andrographolide and its analogues: versatile bioactive molecules for combating inflammation and cancer. Clin. Exp. Pharmacol. Physiol., 39, 300-310.
    • (2012) Clin. Exp. Pharmacol. Physiol. , vol.39 , pp. 300-310
    • Lim, J.C.1
  • 40
    • 79952838142 scopus 로고    scopus 로고
    • Andrographolide, an herbal medicine, inhibits interleukin-6 expression and suppresses prostate cancer cell growth
    • Chun, J.Y. et al. (2010) Andrographolide, an herbal medicine, inhibits interleukin-6 expression and suppresses prostate cancer cell growth. Genes Cancer, 1, 868-876.
    • (2010) Genes Cancer , vol.1 , pp. 868-876
    • Chun, J.Y.1
  • 41
    • 78349303095 scopus 로고    scopus 로고
    • Andrographolide exhibits anti-invasive activity against colon cancer cells via inhibition of MMP2 activity
    • Chao, H.P. et al. (2010) Andrographolide exhibits anti-invasive activity against colon cancer cells via inhibition of MMP2 activity. Planta Med., 76, 1827-1833.
    • (2010) Planta Med. , vol.76 , pp. 1827-1833
    • Chao, H.P.1
  • 42
    • 79960065523 scopus 로고    scopus 로고
    • Andrographolide inhibits human umbilical vein endothelial cell invasion and migration by regulating MMP-2 and MMP-9 during angiogenesis
    • Pratheeshkumar, P. et al. (2011) Andrographolide inhibits human umbilical vein endothelial cell invasion and migration by regulating MMP-2 and MMP-9 during angiogenesis. J. Environ. Pathol. Toxicol. Oncol., 30, 33-41.
    • (2011) J. Environ. Pathol. Toxicol. Oncol. , vol.30 , pp. 33-41
    • Pratheeshkumar, P.1
  • 43
    • 0033602019 scopus 로고    scopus 로고
    • Regulation of motility and protease expression in PKC-mediated induction of MCF-7 breast cancer cell invasiveness
    • Johnson, M.D. et al. (1999) Regulation of motility and protease expression in PKC-mediated induction of MCF-7 breast cancer cell invasiveness. Exp. Cell Res., 247, 105-113.
    • (1999) Exp. Cell Res. , vol.247 , pp. 105-113
    • Johnson, M.D.1
  • 44
    • 74649086132 scopus 로고    scopus 로고
    • Suppression of PMA-induced tumor cell invasion and metastasis by aqueous extract isolated from Prunella vulgaris via the inhibition of NF-kappaB-dependent MMP-9 expression
    • Choi, J.H. et al. (2010) Suppression of PMA-induced tumor cell invasion and metastasis by aqueous extract isolated from Prunella vulgaris via the inhibition of NF-kappaB-dependent MMP-9 expression. Food Chem. Toxicol., 48, 564-571.
    • (2010) Food Chem. Toxicol. , vol.48 , pp. 564-571
    • Choi, J.H.1
  • 45
    • 33747515210 scopus 로고    scopus 로고
    • Circulating MMP2 and MMP9 in breast cancer - potential role in classification of patients into low risk, high risk, benign disease and breast cancer categories
    • Somiari, S.B. et al. (2006) Circulating MMP2 and MMP9 in breast cancer - potential role in classification of patients into low risk, high risk, benign disease and breast cancer categories. Int. J. Cancer, 119, 1403-1411.
    • (2006) Int. J. Cancer , vol.119 , pp. 1403-1411
    • Somiari, S.B.1
  • 46
    • 84862798490 scopus 로고    scopus 로고
    • 4-Ketopinoresinol, a novel naturally occurring ARE activator, induces the Nrf2/HO-1 axis and protects against oxidative stress-induced cell injury via activation of PI3K/AKT signaling
    • Chen, H.H. et al. (2012) 4-Ketopinoresinol, a novel naturally occurring ARE activator, induces the Nrf2/HO-1 axis and protects against oxidative stress-induced cell injury via activation of PI3K/AKT signaling. Free Radic. Biol. Med., 52, 1054-1066.
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 1054-1066
    • Chen, H.H.1
  • 47
    • 34250193619 scopus 로고    scopus 로고
    • Colonic expression of heme oxygenase-1 is associated with a better long-term survival in patients with colorectal cancer
    • Becker, J.C. et al. (2007) Colonic expression of heme oxygenase-1 is associated with a better long-term survival in patients with colorectal cancer. Scand. J. Gastroenterol., 42, 852-858.
    • (2007) Scand. J. Gastroenterol. , vol.42 , pp. 852-858
    • Becker, J.C.1
  • 48
    • 4344599417 scopus 로고    scopus 로고
    • Immunohistochemical analysis of heme oxygenase- 1 in preneoplastic and neoplastic lesions during chemical hepatocarcinogenesis
    • Caballero, F. et al. (2004) Immunohistochemical analysis of heme oxygenase- 1 in preneoplastic and neoplastic lesions during chemical hepatocarcinogenesis. Int. J. Exp. Pathol., 85, 213-222.
    • (2004) Int. J. Exp. Pathol. , vol.85 , pp. 213-222
    • Caballero, F.1
  • 49
    • 84868022009 scopus 로고    scopus 로고
    • Osteopontin increases heme oxygenase-1 expression and subsequently induces cell migration and invasion in glioma cells
    • Lu, D.Y. et al. (2012) Osteopontin increases heme oxygenase-1 expression and subsequently induces cell migration and invasion in glioma cells. Neuro. Oncol., 14, 1367-1378.
    • (2012) Neuro. Oncol. , vol.14 , pp. 1367-1378
    • Lu, D.Y.1
  • 50
    • 84877575206 scopus 로고    scopus 로고
    • TRC8 suppresses tumorigenesis through targeting heme oxygenase-1 for ubiquitination and degradation
    • Lin, P.H. et al. (2013) TRC8 suppresses tumorigenesis through targeting heme oxygenase-1 for ubiquitination and degradation. Oncogene, 32, 2325-2334.
    • (2013) Oncogene , vol.32 , pp. 2325-2334
    • Lin, P.H.1
  • 51
    • 52049090987 scopus 로고    scopus 로고
    • Interactive relations between nitric oxide (NO) and carbon monoxide (CO): heme oxygenase-1/CO pathway is a key modulator in NO-mediated antiapoptosis and anti-inflammation
    • Chung, H.T. et al. (2013) Interactive relations between nitric oxide (NO) and carbon monoxide (CO): heme oxygenase-1/CO pathway is a key modulator in NO-mediated antiapoptosis and anti-inflammation. Methods Enzymol., 441, 329-338.
    • (2013) Methods Enzymol. , vol.441 , pp. 329-338
    • Chung, H.T.1
  • 52
    • 84862778861 scopus 로고    scopus 로고
    • Antioxidant roles of heme oxygenase, carbon monoxide, and bilirubin in cerebral circulation during seizures
    • Parfenova, H. et al. (2012) Antioxidant roles of heme oxygenase, carbon monoxide, and bilirubin in cerebral circulation during seizures. J. Cereb. Blood Flow Metab., 32, 1024-1034.
    • (2012) J. Cereb. Blood Flow Metab. , vol.32 , pp. 1024-1034
    • Parfenova, H.1
  • 53
    • 67650141677 scopus 로고    scopus 로고
    • Kalopanaxsaponin A inhibits PMA-induced invasion by reducing matrix metalloproteinase-9 via PI3K/Akt- and PKCdeltamediated signaling in MCF-7 human breast cancer cells
    • Park, S.K. et al. (2009) Kalopanaxsaponin A inhibits PMA-induced invasion by reducing matrix metalloproteinase-9 via PI3K/Akt- and PKCdeltamediated signaling in MCF-7 human breast cancer cells. Carcinogenesis, 30, 1225-1233.
    • (2009) Carcinogenesis , vol.30 , pp. 1225-1233
    • Park, S.K.1


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