메뉴 건너뛰기




Volumn 79, Issue 6, 2010, Pages 810-816

Effects of cisplatin on matrix metalloproteinase-2 in transformed thyroid cells

Author keywords

AKT PKB; Cisplatin; ERK1 2; MMP 2; PC E1Araf; PKC

Indexed keywords

CISPLATIN; GELATINASE A; PEPTIDE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; PROTEIN KINASE C ZETA; SMALL INTERFERING RNA;

EID: 74149089295     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2009.10.013     Document Type: Article
Times cited : (10)

References (32)
  • 1
    • 34547582326 scopus 로고    scopus 로고
    • Platinum complexes can inhibit matrix metalloproteinase activity: platinum-diethyl[(methylsulfinyl)methyl]phosphonate complexes as inhibitors of MMP-2, -3, -9, and -12
    • Sasanelli R., Boccarelli A., Giordano D., Laforgia M., Natile G., Cardellicchio C., et al. Platinum complexes can inhibit matrix metalloproteinase activity: platinum-diethyl[(methylsulfinyl)methyl]phosphonate complexes as inhibitors of MMP-2, -3, -9, and -12. J Med Chem 50 (2007) 3434-3441
    • (2007) J Med Chem , vol.50 , pp. 3434-3441
    • Sasanelli, R.1    Boccarelli, A.2    Giordano, D.3    Laforgia, M.4    Natile, G.5    Cardellicchio, C.6
  • 2
    • 0032748446 scopus 로고    scopus 로고
    • Nonenzymatic interactions between proteinases and the cell surface: novel roles in normal and malignant cell physiology
    • Mignatti P., and Rifkin D.B. Nonenzymatic interactions between proteinases and the cell surface: novel roles in normal and malignant cell physiology. Adv Cancer Res 78 (2000) 103-157
    • (2000) Adv Cancer Res , vol.78 , pp. 103-157
    • Mignatti, P.1    Rifkin, D.B.2
  • 4
    • 2542495145 scopus 로고    scopus 로고
    • Inhibition of NFkappaB increases the efficacy of cisplatin in in vitro and in vivo ovarian cancer models
    • Mabuchi S., Ohmichi M., Nishio Y., Kimura A., Ohta T., Saito M., et al. Inhibition of NFkappaB increases the efficacy of cisplatin in in vitro and in vivo ovarian cancer models. J Biol Chem 279 (2004) 23477-23485
    • (2004) J Biol Chem , vol.279 , pp. 23477-23485
    • Mabuchi, S.1    Ohmichi, M.2    Nishio, Y.3    Kimura, A.4    Ohta, T.5    Saito, M.6
  • 5
    • 74149094565 scopus 로고
    • Effect of anticancer drugs on invasive capacity of human small-cell lung cancer cells in vitro
    • Morikawa T., Shibuya M., Sakai S., and Kudo S. Effect of anticancer drugs on invasive capacity of human small-cell lung cancer cells in vitro. Nippon Ika Daigaku Zasshi 64 (1995) 320-328
    • (1995) Nippon Ika Daigaku Zasshi , vol.64 , pp. 320-328
    • Morikawa, T.1    Shibuya, M.2    Sakai, S.3    Kudo, S.4
  • 6
    • 0041363324 scopus 로고    scopus 로고
    • Essential role for ERK Mitogen-activated protein kinase in matrix metalloprotease-9 regulation in rat cortical astocytes
    • Arai K., Lee S.R., and Lo H. Essential role for ERK Mitogen-activated protein kinase in matrix metalloprotease-9 regulation in rat cortical astocytes. Glia 43 (2003) 254-264
    • (2003) Glia , vol.43 , pp. 254-264
    • Arai, K.1    Lee, S.R.2    Lo, H.3
  • 7
    • 34547183458 scopus 로고    scopus 로고
    • MMP-2 role in breast cancer brain metastasis development and its regulation by TIMP 2 and ERK1/2
    • Mendes O., Kim H.T., Lungu G., and Stoica G. MMP-2 role in breast cancer brain metastasis development and its regulation by TIMP 2 and ERK1/2. Clin Exp Metastasis 24 (2007) 341-351
    • (2007) Clin Exp Metastasis , vol.24 , pp. 341-351
    • Mendes, O.1    Kim, H.T.2    Lungu, G.3    Stoica, G.4
  • 8
    • 0033556368 scopus 로고    scopus 로고
    • Enhanced production and activation of progelatinase A mediated by membrane-type 1 matrix metalloproteinase in human papillary thyroid carcinomas
    • Nakamura H., Ueno H., Yamashita K., Shimada T., Yamamoto E., Fujimoto N., et al. Enhanced production and activation of progelatinase A mediated by membrane-type 1 matrix metalloproteinase in human papillary thyroid carcinomas. Cancer Res 59 (1999) 467-473
    • (1999) Cancer Res , vol.59 , pp. 467-473
    • Nakamura, H.1    Ueno, H.2    Yamashita, K.3    Shimada, T.4    Yamamoto, E.5    Fujimoto, N.6
  • 10
    • 0027473687 scopus 로고
    • The Adenovirus E1A gene blocks the differentiation of a thyroid epithelial cell line, however the neoplastic phenotype is achieved only after cooperation with other oncogenes
    • Berlingieri M.T., Santoro M., Battaglia C., Grieco M., and Fusco A. The Adenovirus E1A gene blocks the differentiation of a thyroid epithelial cell line, however the neoplastic phenotype is achieved only after cooperation with other oncogenes. Oncogene 8 (1993) 249-255
    • (1993) Oncogene , vol.8 , pp. 249-255
    • Berlingieri, M.T.1    Santoro, M.2    Battaglia, C.3    Grieco, M.4    Fusco, A.5
  • 11
  • 12
    • 25844505737 scopus 로고    scopus 로고
    • Differential functions of PKC-delta and PKC-zeta in cisplatin response of normal and transformed thyroid cells
    • Urso L., Muscella A., Calabriso N., Ciccarese A., Fanizzi F.P., Storelli C., et al. Differential functions of PKC-delta and PKC-zeta in cisplatin response of normal and transformed thyroid cells. Biochem Biophys Res Commun 337 (2005) 297-305
    • (2005) Biochem Biophys Res Commun , vol.337 , pp. 297-305
    • Urso, L.1    Muscella, A.2    Calabriso, N.3    Ciccarese, A.4    Fanizzi, F.P.5    Storelli, C.6
  • 13
    • 49649086716 scopus 로고    scopus 로고
    • PKC-epsilon-dependent cytosol-to-membrane translocation of pendrin in rat thyroid PC Cl3 cells
    • Muscella A., Marsigliante S., Verri T., Urso L., Dimitri C., Bottà G., et al. PKC-epsilon-dependent cytosol-to-membrane translocation of pendrin in rat thyroid PC Cl3 cells. J Cell Physiol 217 (2008) 103-112
    • (2008) J Cell Physiol , vol.217 , pp. 103-112
    • Muscella, A.1    Marsigliante, S.2    Verri, T.3    Urso, L.4    Dimitri, C.5    Bottà, G.6
  • 14
    • 12344334474 scopus 로고    scopus 로고
    • Angiotensin II induces focal adhesion kinase/paxillin phosphorylation and cell migration in human umbilical vein endothelial cells
    • Montiel M., Pérez de la Blanca E., and Jiménez E. Angiotensin II induces focal adhesion kinase/paxillin phosphorylation and cell migration in human umbilical vein endothelial cells. Biochem Biophys Res Commun 327 (2005) 971-978
    • (2005) Biochem Biophys Res Commun , vol.327 , pp. 971-978
    • Montiel, M.1    Pérez de la Blanca, E.2    Jiménez, E.3
  • 15
    • 0041845231 scopus 로고    scopus 로고
    • Use of RNA interference-mediated gene silencing and adenoviral overexpression to elucidate the roles of AKT/protein kinase B isoforms in insulin actions
    • Katome T., Obata T., Matsushima R., Masuyama N., Cantley L.C., Gotoh Y., et al. Use of RNA interference-mediated gene silencing and adenoviral overexpression to elucidate the roles of AKT/protein kinase B isoforms in insulin actions. J Biol Chem 278 (2003) 28312-28323
    • (2003) J Biol Chem , vol.278 , pp. 28312-28323
    • Katome, T.1    Obata, T.2    Matsushima, R.3    Masuyama, N.4    Cantley, L.C.5    Gotoh, Y.6
  • 16
    • 28244439312 scopus 로고    scopus 로고
    • Differential response of normal, dedifferentiated and transformed thyroid cell lines to cisplatin treatment
    • Muscella A., Urso L., Calabriso N., Ciccarese A., Migoni D., Fanizzi F.P., et al. Differential response of normal, dedifferentiated and transformed thyroid cell lines to cisplatin treatment. Biochem Pharmacol 71 (2005) 50-60
    • (2005) Biochem Pharmacol , vol.71 , pp. 50-60
    • Muscella, A.1    Urso, L.2    Calabriso, N.3    Ciccarese, A.4    Migoni, D.5    Fanizzi, F.P.6
  • 17
    • 37849021234 scopus 로고    scopus 로고
    • [Pt(O,O′-acac)(gamma-acac)(DMS)], a new Pt compound exerting fast cytotoxicity in MCF-7 breast cancer cells via the mitochondrial apoptotic pathway
    • Muscella A., Calabriso N., Fanizzi F.P., De Pascali S.A., Urso L., et al. [Pt(O,O′-acac)(gamma-acac)(DMS)], a new Pt compound exerting fast cytotoxicity in MCF-7 breast cancer cells via the mitochondrial apoptotic pathway. Br J Pharmacol 153 (2008) 34-49
    • (2008) Br J Pharmacol , vol.153 , pp. 34-49
    • Muscella, A.1    Calabriso, N.2    Fanizzi, F.P.3    De Pascali, S.A.4    Urso, L.5
  • 18
    • 34249031768 scopus 로고    scopus 로고
    • New platinum(II) complexes containing both an O,O′-chelated acetylacetonate ligand and a sulfur ligand in the platinum coordination sphere induce apoptosis in HeLa cervical carcinoma cells
    • Muscella A., Calabriso N., De Pascali S.A., Urso L., Ciccarese A., Fanizzi F.P., et al. New platinum(II) complexes containing both an O,O′-chelated acetylacetonate ligand and a sulfur ligand in the platinum coordination sphere induce apoptosis in HeLa cervical carcinoma cells. Biochem Pharmacol 74 (2007) 28-40
    • (2007) Biochem Pharmacol , vol.74 , pp. 28-40
    • Muscella, A.1    Calabriso, N.2    De Pascali, S.A.3    Urso, L.4    Ciccarese, A.5    Fanizzi, F.P.6
  • 19
    • 0032211804 scopus 로고    scopus 로고
    • ECM signalling: orchestrating cell behaviour and misbehaviour
    • Lukashev M.E., and Werb Z. ECM signalling: orchestrating cell behaviour and misbehaviour. Trends Cell Biol 8 (1998) 437-441
    • (1998) Trends Cell Biol , vol.8 , pp. 437-441
    • Lukashev, M.E.1    Werb, Z.2
  • 20
    • 0031784501 scopus 로고    scopus 로고
    • Proteolytic mechanisms in corneal ulceration and repair
    • Fini M.E., Cook J.R., and Mohan R. Proteolytic mechanisms in corneal ulceration and repair. Arch Dermatol Res 90 (1998) S12-S23
    • (1998) Arch Dermatol Res , vol.90
    • Fini, M.E.1    Cook, J.R.2    Mohan, R.3
  • 22
    • 0037449202 scopus 로고    scopus 로고
    • Specific blockade of the ERK pathway inhibits the invasiveness of tumor cells: down-regulation of matrix metalloproteinase-3/-9/-14 and CD44
    • Tanimura S., Asato K., Fujishiro S.H., and Kohno M. Specific blockade of the ERK pathway inhibits the invasiveness of tumor cells: down-regulation of matrix metalloproteinase-3/-9/-14 and CD44. Biochem Biophys Res Commun 304 (2003) 801-806
    • (2003) Biochem Biophys Res Commun , vol.304 , pp. 801-806
    • Tanimura, S.1    Asato, K.2    Fujishiro, S.H.3    Kohno, M.4
  • 23
    • 0036076333 scopus 로고    scopus 로고
    • FGF-2 and TPA induce matrix metalloproteinase-9 secretion in MCF-7 cells through PKC activation of the Ras/ERK pathway
    • Liu J.F., Crépin M., Liu J.M., and Ledoux D. FGF-2 and TPA induce matrix metalloproteinase-9 secretion in MCF-7 cells through PKC activation of the Ras/ERK pathway. Biochem Biophys Res Commun 93 (2002) 1174-1182
    • (2002) Biochem Biophys Res Commun , vol.93 , pp. 1174-1182
    • Liu, J.F.1    Crépin, M.2    Liu, J.M.3    Ledoux, D.4
  • 24
    • 0037031833 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drugs inhibit matrix metalloproteinase-2 via suppression of the ERK/Sp1-mediated transcription
    • Pan M.R., and Hung W.C. Nonsteroidal anti-inflammatory drugs inhibit matrix metalloproteinase-2 via suppression of the ERK/Sp1-mediated transcription. J Biol Chem 277 (2002) 32775-32780
    • (2002) J Biol Chem , vol.277 , pp. 32775-32780
    • Pan, M.R.1    Hung, W.C.2
  • 25
    • 0141594869 scopus 로고    scopus 로고
    • Laminin alpha 3 LG4 module induces matrix metalloproteinase-1 through mitogen-activated protein kinase signaling
    • Utani A., Momota Y., Endo H., Kasuya Y., Beck K., Nomizu M., et al. Laminin alpha 3 LG4 module induces matrix metalloproteinase-1 through mitogen-activated protein kinase signaling. J Biol Chem 278 (2003) 34483-34490
    • (2003) J Biol Chem , vol.278 , pp. 34483-34490
    • Utani, A.1    Momota, Y.2    Endo, H.3    Kasuya, Y.4    Beck, K.5    Nomizu, M.6
  • 26
    • 0032883939 scopus 로고    scopus 로고
    • Fibronectin upregulates gelatinase B (MMP-9) and induces coordinated expression of gelatinase A (MMP-2) and its activator MT1-MMP by human T lymphocyte cell lines. A process repressed through RAS/MAP kinase signaling pathways
    • Esparza J., Vilardell C., Calvo J., Juan M., Vives J., Yagüe J., et al. Fibronectin upregulates gelatinase B (MMP-9) and induces coordinated expression of gelatinase A (MMP-2) and its activator MT1-MMP by human T lymphocyte cell lines. A process repressed through RAS/MAP kinase signaling pathways. Blood 94 (1999) 2754-2766
    • (1999) Blood , vol.94 , pp. 2754-2766
    • Esparza, J.1    Vilardell, C.2    Calvo, J.3    Juan, M.4    Vives, J.5    Yagüe, J.6
  • 29
    • 1542467581 scopus 로고    scopus 로고
    • Osteopontin inhibits interleukin-1 beta-stimulated increases in matrix metalloproteinase activity in adult rat cardiac fibroblasts: role of protein kinase C-zeta
    • Xie Z., Singh M., Siwik D.A., Joyner W.L., and Singh K. Osteopontin inhibits interleukin-1 beta-stimulated increases in matrix metalloproteinase activity in adult rat cardiac fibroblasts: role of protein kinase C-zeta. J Biol Chem 278 (2003) 48546-48552
    • (2003) J Biol Chem , vol.278 , pp. 48546-48552
    • Xie, Z.1    Singh, M.2    Siwik, D.A.3    Joyner, W.L.4    Singh, K.5
  • 30
    • 17144398831 scopus 로고    scopus 로고
    • Possible future issues in the treatment of glioblastomas: special emphasis on cell migration and the resistance of migrating glioblastoma cells to apoptosis
    • Lefranc F., Brotchi J., and Kiss R. Possible future issues in the treatment of glioblastomas: special emphasis on cell migration and the resistance of migrating glioblastoma cells to apoptosis. J Clin Oncol 23 (2005) 2411-2422
    • (2005) J Clin Oncol , vol.23 , pp. 2411-2422
    • Lefranc, F.1    Brotchi, J.2    Kiss, R.3
  • 31
    • 10044256495 scopus 로고    scopus 로고
    • Involvement of metalloproteinases 2/9 in epidermal growth factor receptor transactivation in pressure-induced myogenic tone in mouse mesenteric resistance arteries
    • Lucchesi P.A., Sabri A., Belmadani S., and Matrougui K. Involvement of metalloproteinases 2/9 in epidermal growth factor receptor transactivation in pressure-induced myogenic tone in mouse mesenteric resistance arteries. Circulation 110 (2004) 3587-3593
    • (2004) Circulation , vol.110 , pp. 3587-3593
    • Lucchesi, P.A.1    Sabri, A.2    Belmadani, S.3    Matrougui, K.4
  • 32
    • 0037693895 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry
    • Visse R., and Nagase H. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ Res 92 (2003) 827-839
    • (2003) Circ Res , vol.92 , pp. 827-839
    • Visse, R.1    Nagase, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.