메뉴 건너뛰기




Volumn 45, Issue 6, 2012, Pages 764-776

ErbB2-Driven Breast Cancer Cell Invasion Depends on a Complex Signaling Network Activating Myeloid Zinc Finger-1-Dependent Cathepsin B Expression

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN B; CATHEPSIN L; EPIDERMAL GROWTH FACTOR RECEPTOR 2; P21 ACTIVATED KINASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; ZINC FINGER 1 PROTEIN;

EID: 84859085199     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2012.01.029     Document Type: Article
Times cited : (104)

References (42)
  • 1
    • 49649094763 scopus 로고    scopus 로고
    • Cathepsin L is responsible for processing and activation of proheparanase through multiple cleavages of a linker segment
    • Abboud-Jarrous G., Atzmon R., Peretz T., Palermo C., Gadea B.B., Joyce J.A., Vlodavsky I. Cathepsin L is responsible for processing and activation of proheparanase through multiple cleavages of a linker segment. J. Biol. Chem. 2008, 283:18167-18176.
    • (2008) J. Biol. Chem. , vol.283 , pp. 18167-18176
    • Abboud-Jarrous, G.1    Atzmon, R.2    Peretz, T.3    Palermo, C.4    Gadea, B.B.5    Joyce, J.A.6    Vlodavsky, I.7
  • 2
    • 0032538973 scopus 로고    scopus 로고
    • PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in the formation of filopodia
    • Abo A., Qu J., Cammarano M.S., Dan C., Fritsch A., Baud V., Belisle B., Minden A. PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in the formation of filopodia. EMBO J. 1998, 17:6527-6540.
    • (1998) EMBO J. , vol.17 , pp. 6527-6540
    • Abo, A.1    Qu, J.2    Cammarano, M.S.3    Dan, C.4    Fritsch, A.5    Baud, V.6    Belisle, B.7    Minden, A.8
  • 3
    • 0035959808 scopus 로고    scopus 로고
    • HER2/Neu-mediated activation of the ETS transcription factor ER81 and its target gene MMP-1
    • Bosc D.G., Goueli B.S., Janknecht R. HER2/Neu-mediated activation of the ETS transcription factor ER81 and its target gene MMP-1. Oncogene 2001, 20:6215-6224.
    • (2001) Oncogene , vol.20 , pp. 6215-6224
    • Bosc, D.G.1    Goueli, B.S.2    Janknecht, R.3
  • 4
    • 4544286160 scopus 로고    scopus 로고
    • Enhanced cathepsin L expression is mediated by different Ras effector pathways in fibroblasts and epithelial cells
    • Collette J., Ulku A.S., Der C.J., Jones A., Erickson A.H. Enhanced cathepsin L expression is mediated by different Ras effector pathways in fibroblasts and epithelial cells. Int. J. Cancer 2004, 112:190-199.
    • (2004) Int. J. Cancer , vol.112 , pp. 190-199
    • Collette, J.1    Ulku, A.S.2    Der, C.J.3    Jones, A.4    Erickson, A.H.5
  • 5
    • 74049164266 scopus 로고    scopus 로고
    • The vulnerability of the heart as a pluricellular paracrine organ: lessons from unexpected triggers of heart failure in targeted ErbB2 anticancer therapy
    • De Keulenaer G.W., Doggen K., Lemmens K. The vulnerability of the heart as a pluricellular paracrine organ: lessons from unexpected triggers of heart failure in targeted ErbB2 anticancer therapy. Circ. Res. 2010, 106:35-46.
    • (2010) Circ. Res. , vol.106 , pp. 35-46
    • De Keulenaer, G.W.1    Doggen, K.2    Lemmens, K.3
  • 6
    • 41749103541 scopus 로고    scopus 로고
    • Presenilin regulates extracellular regulated kinase (Erk) activity by a protein kinase C alpha dependent mechanism
    • Dehvari N., Isacsson O., Winblad B., Cedazo-Minguez A., Cowburn R.F. Presenilin regulates extracellular regulated kinase (Erk) activity by a protein kinase C alpha dependent mechanism. Neurosci. Lett. 2008, 436:77-80.
    • (2008) Neurosci. Lett. , vol.436 , pp. 77-80
    • Dehvari, N.1    Isacsson, O.2    Winblad, B.3    Cedazo-Minguez, A.4    Cowburn, R.F.5
  • 8
    • 0035888069 scopus 로고    scopus 로고
    • Truncated ErbB2 receptor enhances ErbB1 signaling and induces reversible, ERK-independent loss of epithelial morphology
    • Egeblad M., Mortensen O.H., Jäättelä M. Truncated ErbB2 receptor enhances ErbB1 signaling and induces reversible, ERK-independent loss of epithelial morphology. Int. J. Cancer 2001, 94:185-191.
    • (2001) Int. J. Cancer , vol.94 , pp. 185-191
    • Egeblad, M.1    Mortensen, O.H.2    Jäättelä, M.3
  • 10
    • 33846643454 scopus 로고    scopus 로고
    • Cysteine cathepsins and the cutting edge of cancer invasion
    • Gocheva V., Joyce J.A. Cysteine cathepsins and the cutting edge of cancer invasion. Cell Cycle 2007, 6:60-64.
    • (2007) Cell Cycle , vol.6 , pp. 60-64
    • Gocheva, V.1    Joyce, J.A.2
  • 12
    • 0030944455 scopus 로고    scopus 로고
    • ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling
    • Graus-Porta D., Beerli R.R., Daly J.M., Hynes N.E. ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling. EMBO J. 1997, 16:1647-1655.
    • (1997) EMBO J. , vol.16 , pp. 1647-1655
    • Graus-Porta, D.1    Beerli, R.R.2    Daly, J.M.3    Hynes, N.E.4
  • 13
    • 1342323632 scopus 로고    scopus 로고
    • ErbB receptors: directing key signaling networks throughout life
    • Holbro T., Hynes N.E. ErbB receptors: directing key signaling networks throughout life. Annu. Rev. Pharmacol. Toxicol. 2004, 44:195-217.
    • (2004) Annu. Rev. Pharmacol. Toxicol. , vol.44 , pp. 195-217
    • Holbro, T.1    Hynes, N.E.2
  • 16
    • 24644476507 scopus 로고    scopus 로고
    • Crosstalk mechanisms between the mitogen-activated protein kinase pathways and Smad signaling downstream of TGF-beta: implications for carcinogenesis
    • Javelaud D., Mauviel A. Crosstalk mechanisms between the mitogen-activated protein kinase pathways and Smad signaling downstream of TGF-beta: implications for carcinogenesis. Oncogene 2005, 24:5742-5750.
    • (2005) Oncogene , vol.24 , pp. 5742-5750
    • Javelaud, D.1    Mauviel, A.2
  • 17
    • 10044296973 scopus 로고    scopus 로고
    • Cysteine cathepsins in human cancer
    • Jedeszko C., Sloane B.F. Cysteine cathepsins in human cancer. Biol. Chem. 2004, 385:1017-1027.
    • (2004) Biol. Chem. , vol.385 , pp. 1017-1027
    • Jedeszko, C.1    Sloane, B.F.2
  • 19
  • 20
    • 62949128915 scopus 로고    scopus 로고
    • Lysosomal involvement in cell death and cancer
    • Kirkegaard T., Jäättelä M. Lysosomal involvement in cell death and cancer. Biochim. Biophys. Acta 2009, 1793:746-754.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 746-754
    • Kirkegaard, T.1    Jäättelä, M.2
  • 21
    • 0025845425 scopus 로고
    • Cathepsin B efficiently activates the soluble and the tumor cell receptor-bound form of the proenzyme urokinase-type plasminogen activator (Pro-uPA)
    • Kobayashi H., Schmitt M., Goretzki L., Chucholowski N., Calvete J., Kramer M., Günzler W.A., Jänicke F., Graeff H. Cathepsin B efficiently activates the soluble and the tumor cell receptor-bound form of the proenzyme urokinase-type plasminogen activator (Pro-uPA). J. Biol. Chem. 1991, 266:5147-5152.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5147-5152
    • Kobayashi, H.1    Schmitt, M.2    Goretzki, L.3    Chucholowski, N.4    Calvete, J.5    Kramer, M.6    Günzler, W.A.7    Jänicke, F.8    Graeff, H.9
  • 22
    • 78149466325 scopus 로고    scopus 로고
    • The protein kinase Pak4 disrupts mammary acinar architecture and promotes mammary tumorigenesis
    • Liu Y., Chen N., Cui X., Zheng X., Deng L., Price S., Karantza V., Minden A. The protein kinase Pak4 disrupts mammary acinar architecture and promotes mammary tumorigenesis. Oncogene 2010, 29:5883-5894.
    • (2010) Oncogene , vol.29 , pp. 5883-5894
    • Liu, Y.1    Chen, N.2    Cui, X.3    Zheng, X.4    Deng, L.5    Price, S.6    Karantza, V.7    Minden, A.8
  • 23
    • 34347226346 scopus 로고    scopus 로고
    • Protein kinase Calpha determines HER2 fate in breast carcinoma cells with HER2 protein overexpression without gene amplification
    • Magnifico A., Albano L., Campaner S., Campiglio M., Pilotti S., Ménard S., Tagliabue E. Protein kinase Calpha determines HER2 fate in breast carcinoma cells with HER2 protein overexpression without gene amplification. Cancer Res. 2007, 67:5308-5317.
    • (2007) Cancer Res. , vol.67 , pp. 5308-5317
    • Magnifico, A.1    Albano, L.2    Campaner, S.3    Campiglio, M.4    Pilotti, S.5    Ménard, S.6    Tagliabue, E.7
  • 24
    • 34547922452 scopus 로고    scopus 로고
    • Targeting the function of the HER2 oncogene in human cancer therapeutics
    • Moasser M.M. Targeting the function of the HER2 oncogene in human cancer therapeutics. Oncogene 2007, 26:6577-6592.
    • (2007) Oncogene , vol.26 , pp. 6577-6592
    • Moasser, M.M.1
  • 25
    • 33749017931 scopus 로고    scopus 로고
    • Cysteine cathepsins: multifunctional enzymes in cancer
    • Mohamed M.M., Sloane B.F. Cysteine cathepsins: multifunctional enzymes in cancer. Nat. Rev. Cancer 2006, 6:764-775.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 764-775
    • Mohamed, M.M.1    Sloane, B.F.2
  • 26
    • 0345086465 scopus 로고    scopus 로고
    • Cloning and chromosomal localization of human Cdc42-binding protein kinase beta
    • Moncrieff C.L., Bailey M.E., Morrison N., Johnson K.J. Cloning and chromosomal localization of human Cdc42-binding protein kinase beta. Genomics 1999, 57:297-300.
    • (1999) Genomics , vol.57 , pp. 297-300
    • Moncrieff, C.L.1    Bailey, M.E.2    Morrison, N.3    Johnson, K.J.4
  • 27
    • 77249096023 scopus 로고    scopus 로고
    • Myeloid zinc finger 1 induces migration, invasion, and in vivo metastasis through Axl gene expression in solid cancer
    • Mudduluru G., Vajkoczy P., Allgayer H. Myeloid zinc finger 1 induces migration, invasion, and in vivo metastasis through Axl gene expression in solid cancer. Mol. Cancer Res. 2010, 8:159-169.
    • (2010) Mol. Cancer Res. , vol.8 , pp. 159-169
    • Mudduluru, G.1    Vajkoczy, P.2    Allgayer, H.3
  • 28
    • 31644439702 scopus 로고    scopus 로고
    • Herceptin: mechanisms of action and resistance
    • Nahta R., Esteva F.J. Herceptin: mechanisms of action and resistance. Cancer Lett. 2006, 232:123-138.
    • (2006) Cancer Lett. , vol.232 , pp. 123-138
    • Nahta, R.1    Esteva, F.J.2
  • 29
    • 0037474329 scopus 로고    scopus 로고
    • Regulation of myeloid zinc finger protein 2A transactivation activity through phosphorylation by mitogen-activated protein kinases
    • Ogawa H., Murayama A., Nagata S., Fukunaga R. Regulation of myeloid zinc finger protein 2A transactivation activity through phosphorylation by mitogen-activated protein kinases. J. Biol. Chem. 2003, 278:2921-2927.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2921-2927
    • Ogawa, H.1    Murayama, A.2    Nagata, S.3    Fukunaga, R.4
  • 30
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl M.W. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 2001, 29:e45.
    • (2001) Nucleic Acids Res. , vol.29
    • Pfaffl, M.W.1
  • 34
    • 3843095048 scopus 로고    scopus 로고
    • Extracellular S100A4(mts1) stimulates invasive growth of mouse endothelial cells and modulates MMP-13 matrix metalloproteinase activity
    • Schmidt-Hansen B., Ornås D., Grigorian M., Klingelhöfer J., Tulchinsky E., Lukanidin E., Ambartsumian N. Extracellular S100A4(mts1) stimulates invasive growth of mouse endothelial cells and modulates MMP-13 matrix metalloproteinase activity. Oncogene 2004, 23:5487-5495.
    • (2004) Oncogene , vol.23 , pp. 5487-5495
    • Schmidt-Hansen, B.1    Ornås, D.2    Grigorian, M.3    Klingelhöfer, J.4    Tulchinsky, E.5    Lukanidin, E.6    Ambartsumian, N.7
  • 35
    • 0028273525 scopus 로고
    • Membrane association of cathepsin B can be induced by transfection of human breast epithelial cells with c-Ha-ras oncogene
    • Sloane B.F., Moin K., Sameni M., Tait L.R., Rozhin J., Ziegler G. Membrane association of cathepsin B can be induced by transfection of human breast epithelial cells with c-Ha-ras oncogene. J. Cell Sci. 1994, 107:373-384.
    • (1994) J. Cell Sci. , vol.107 , pp. 373-384
    • Sloane, B.F.1    Moin, K.2    Sameni, M.3    Tait, L.R.4    Rozhin, J.5    Ziegler, G.6
  • 37
  • 39
    • 1242273590 scopus 로고    scopus 로고
    • Truncated ErbB2 receptor (p95ErbB2) is regulated by heregulin through heterodimer formation with ErbB3 yet remains sensitive to the dual EGFR/ErbB2 kinase inhibitor GW572016
    • Xia W., Liu L.H., Ho P., Spector N.L. Truncated ErbB2 receptor (p95ErbB2) is regulated by heregulin through heterodimer formation with ErbB3 yet remains sensitive to the dual EGFR/ErbB2 kinase inhibitor GW572016. Oncogene 2004, 23:646-653.
    • (2004) Oncogene , vol.23 , pp. 646-653
    • Xia, W.1    Liu, L.H.2    Ho, P.3    Spector, N.L.4
  • 40
    • 0034008432 scopus 로고    scopus 로고
    • Transcription of human cathepsin B is mediated by Sp1 and Ets family factors in glioma
    • Yan S., Berquin I.M., Troen B.R., Sloane B.F. Transcription of human cathepsin B is mediated by Sp1 and Ets family factors in glioma. DNA Cell Biol. 2000, 19:79-91.
    • (2000) DNA Cell Biol. , vol.19 , pp. 79-91
    • Yan, S.1    Berquin, I.M.2    Troen, B.R.3    Sloane, B.F.4
  • 42
    • 75449085701 scopus 로고    scopus 로고
    • ErbB2-enhanced invasiveness of H-Ras MCF10A breast cells requires MMP-13 and uPA upregulation via p38 MAPK signaling
    • Yong H.Y., Kim I.Y., Kim J.S., Moon A. ErbB2-enhanced invasiveness of H-Ras MCF10A breast cells requires MMP-13 and uPA upregulation via p38 MAPK signaling. Int. J. Oncol. 2010, 36:501-507.
    • (2010) Int. J. Oncol. , vol.36 , pp. 501-507
    • Yong, H.Y.1    Kim, I.Y.2    Kim, J.S.3    Moon, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.