메뉴 건너뛰기




Volumn 452, Issue 3, 2014, Pages 828-833

Amyloid precursor protein regulates migration and metalloproteinase gene expression in prostate cancer cells

Author keywords

Amyloid precursor protein; Epithelial mesenchymal transition; Metalloproteinase; Prostate cancer

Indexed keywords

ADAM PROTEIN; ADAM10 ENDOPEPTIDASE; ADAM17 PROTEIN; AMYLOID PRECURSOR PROTEIN; METALLOPROTEINASE; SMALL INTERFERING RNA; TRANSCRIPTION FACTOR SLUG; UNCLASSIFIED DRUG; VIMENTIN; ADAM10 PROTEIN, HUMAN; APP PROTEIN, HUMAN; MEMBRANE PROTEIN; SECRETASE; SNAIL FAMILY TRANSCRIPTION FACTORS; TRANSCRIPTION FACTOR; TUMOR NECROSIS FACTOR-ALPHA CONVERTASE;

EID: 84907545976     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2014.09.010     Document Type: Article
Times cited : (30)

References (39)
  • 1
    • 0030779677 scopus 로고    scopus 로고
    • Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives
    • M.P. Mattson Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives Physiol. Rev. 77 1997 1081 1132
    • (1997) Physiol. Rev. , vol.77 , pp. 1081-1132
    • Mattson, M.P.1
  • 2
    • 0034730466 scopus 로고    scopus 로고
    • Platelets as a peripheral district where to study pathogenetic mechanisms of alzheimer disease: The case of amyloid precursor protein
    • M. Di Luca, F. Colciaghi, L. Pastorino, B. Borroni, A. Padovani, and F. Cattabeni Platelets as a peripheral district where to study pathogenetic mechanisms of alzheimer disease: the case of amyloid precursor protein Eur. J. Pharmacol. 405 2000 277 283
    • (2000) Eur. J. Pharmacol. , vol.405 , pp. 277-283
    • Di Luca, M.1    Colciaghi, F.2    Pastorino, L.3    Borroni, B.4    Padovani, A.5    Cattabeni, F.6
  • 3
    • 0026047558 scopus 로고
    • Establishment of a new human cancer cell line secreting protease nexin-II/amyloid beta protein precursor derived from squamous-cell carcinoma of lung
    • H. Itoh, H. Kataoka, H. Koita, K. Nabeshima, T. Inoue, K. Kangawa, and M. Koono Establishment of a new human cancer cell line secreting protease nexin-II/amyloid beta protein precursor derived from squamous-cell carcinoma of lung Int. J. Cancer 49 1991 436 443
    • (1991) Int. J. Cancer , vol.49 , pp. 436-443
    • Itoh, H.1    Kataoka, H.2    Koita, H.3    Nabeshima, K.4    Inoue, T.5    Kangawa, K.6    Koono, M.7
  • 4
    • 0035313986 scopus 로고    scopus 로고
    • Amyloid beta protein precursor is involved in the growth of human colon carcinoma cell in vitro and in vivo
    • J.Y. Meng, H. Kataoka, H. Itoh, and M. Koono Amyloid beta protein precursor is involved in the growth of human colon carcinoma cell in vitro and in vivo Int. J. Cancer 92 2001 31 39
    • (2001) Int. J. Cancer , vol.92 , pp. 31-39
    • Meng, J.Y.1    Kataoka, H.2    Itoh, H.3    Koono, M.4
  • 5
    • 0242442605 scopus 로고    scopus 로고
    • Increased expression and processing of the Alzheimer amyloid precursor protein in pancreatic cancer may influence cellular proliferation
    • D.E. Hansel, A. Rahman, S. Wehner, V. Herzog, C.J. Yeo, and A. Maitra Increased expression and processing of the Alzheimer amyloid precursor protein in pancreatic cancer may influence cellular proliferation Cancer Res. 63 2003 7032 7037
    • (2003) Cancer Res. , vol.63 , pp. 7032-7037
    • Hansel, D.E.1    Rahman, A.2    Wehner, S.3    Herzog, V.4    Yeo, C.J.5    Maitra, A.6
  • 11
    • 77955917769 scopus 로고    scopus 로고
    • Knockdown of Efp by DNA-modified small interfering RNA inhibits breast cancer cell proliferation and in vivo tumor growth
    • K. Ueyama, K. Ikeda, W. Sato, N. Nakasato, K. Horie-Inoue, S. Takeda, and S. Inoue Knockdown of Efp by DNA-modified small interfering RNA inhibits breast cancer cell proliferation and in vivo tumor growth Cancer Gene Ther. 17 2010 624 632
    • (2010) Cancer Gene Ther. , vol.17 , pp. 624-632
    • Ueyama, K.1    Ikeda, K.2    Sato, W.3    Nakasato, N.4    Horie-Inoue, K.5    Takeda, S.6    Inoue, S.7
  • 12
    • 0032741143 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: Modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding
    • J. Schlöndorff, and C.P. Blobel Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding J. Cell Sci. 112 1999 3603 3617
    • (1999) J. Cell Sci. , vol.112 , pp. 3603-3617
    • Schlöndorff, J.1    Blobel, C.P.2
  • 14
    • 0032976525 scopus 로고    scopus 로고
    • Role for ADAM-family proteinases as membrane protein secretases
    • A.J. Turner, and N.M. Hooper Role for ADAM-family proteinases as membrane protein secretases Biochem. Soc. Trans. 27 1999 255 259
    • (1999) Biochem. Soc. Trans. , vol.27 , pp. 255-259
    • Turner, A.J.1    Hooper, N.M.2
  • 15
    • 0033867521 scopus 로고    scopus 로고
    • A ligand-induced extracellular cleavage regulates gamma-secretase-like proteolytic activation of Notch1
    • J.S. Mumm, E.H. Schroeter, M.T. Saxena, A. Griesemer, X. Tian, D.J. Pan, W.J. Ray, and R. Kopan A ligand-induced extracellular cleavage regulates gamma-secretase-like proteolytic activation of Notch1 Mol. Cell 5 2000 197 206
    • (2000) Mol. Cell , vol.5 , pp. 197-206
    • Mumm, J.S.1    Schroeter, E.H.2    Saxena, M.T.3    Griesemer, A.4    Tian, X.5    Pan, D.J.6    Ray, W.J.7    Kopan, R.8
  • 17
    • 0035955693 scopus 로고    scopus 로고
    • The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner
    • W.T. Kimberly, J.B. Zheng, S.Y. Guénette, and D.J. Selkoe The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner J. Biol. Chem. 276 2001 40288 40292
    • (2001) J. Biol. Chem. , vol.276 , pp. 40288-40292
    • Kimberly, W.T.1    Zheng, J.B.2    Guénette, S.Y.3    Selkoe, D.J.4
  • 18
    • 0343628678 scopus 로고    scopus 로고
    • Metalloprotease-disintegrin (ADAM) genes are widely and differentially expressed in the adult CNS
    • I. Kärkkäinen, E. Rybnikova, M. Pelto-Huikko, and A.P. Huovila Metalloprotease-disintegrin (ADAM) genes are widely and differentially expressed in the adult CNS Mol. Cell. Neurosci. 15 2000 547 560
    • (2000) Mol. Cell. Neurosci. , vol.15 , pp. 547-560
    • Kärkkäinen, I.1    Rybnikova, E.2    Pelto-Huikko, M.3    Huovila, A.P.4
  • 19
    • 0033793248 scopus 로고    scopus 로고
    • Coordinated expression of beta-amyloid precursor protein and the putative beta-secretase BACE and alpha-secretase ADAM10 in mouse and human brain
    • M. Marcinkiewicz, and N.G. Seidah Coordinated expression of beta-amyloid precursor protein and the putative beta-secretase BACE and alpha-secretase ADAM10 in mouse and human brain J. Neurochem. 75 2000 2133 2143
    • (2000) J. Neurochem. , vol.75 , pp. 2133-2143
    • Marcinkiewicz, M.1    Seidah, N.G.2
  • 20
    • 0035424693 scopus 로고    scopus 로고
    • Constitutive shedding of the amyloid precursor protein ectodomain is up-regulated by tumour necrosis factor-alpha converting enzyme
    • B.E. Slack, L.K. Ma, and C.C. Seah Constitutive shedding of the amyloid precursor protein ectodomain is up-regulated by tumour necrosis factor-alpha converting enzyme Biochem. J. 357 2001 787 794
    • (2001) Biochem. J. , vol.357 , pp. 787-794
    • Slack, B.E.1    Ma, L.K.2    Seah, C.C.3
  • 22
  • 23
    • 3042643033 scopus 로고    scopus 로고
    • The role of ADAM10 and ADAM17 in the ectodomain shedding of angiotensin converting enzyme and the amyloid precursor protein
    • T.M. Allinson, E.T. Parkin, T.P. Condon, S.L. Schwager, E.D. Sturrock, A.J. Turner, and N.M. Hooper The role of ADAM10 and ADAM17 in the ectodomain shedding of angiotensin converting enzyme and the amyloid precursor protein Eur. J. Biochem. 271 2004 2539 2547
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2539-2547
    • Allinson, T.M.1    Parkin, E.T.2    Condon, T.P.3    Schwager, S.L.4    Sturrock, E.D.5    Turner, A.J.6    Hooper, N.M.7
  • 25
    • 1642576128 scopus 로고    scopus 로고
    • Expression of the disintegrin metalloprotease, ADAM-10, in prostate cancer and its regulation by dihydrotestosterone, insulin-like growth factor I, and epidermal growth factor in the prostate cancer cell model LNCaP
    • D.R. McCulloch, P. Akl, H. Samaratunga, A.C. Herington, and D.M. Odorico Expression of the disintegrin metalloprotease, ADAM-10, in prostate cancer and its regulation by dihydrotestosterone, insulin-like growth factor I, and epidermal growth factor in the prostate cancer cell model LNCaP Clin. Cancer Res. 10 2004 314 323
    • (2004) Clin. Cancer Res. , vol.10 , pp. 314-323
    • McCulloch, D.R.1    Akl, P.2    Samaratunga, H.3    Herington, A.C.4    Odorico, D.M.5
  • 26
    • 13944268218 scopus 로고    scopus 로고
    • L1, a novel target of beta-catenin signaling, transforms cells and is expressed at the invasive front of colon cancers
    • N. Gavert, M. Conacci-Sorrell, D. Gast, A. Schneider, P. Altevogt, T. Brabletz, and A. Ben-Ze'ev L1, a novel target of beta-catenin signaling, transforms cells and is expressed at the invasive front of colon cancers J. Cell Biol. 168 2005 633 642
    • (2005) J. Cell Biol. , vol.168 , pp. 633-642
    • Gavert, N.1    Conacci-Sorrell, M.2    Gast, D.3    Schneider, A.4    Altevogt, P.5    Brabletz, T.6    Ben-Ze'Ev, A.7
  • 28
    • 3142779503 scopus 로고    scopus 로고
    • Expression of ADAMs (a disintegrin and metalloproteases) and TIMP-3 (tissue inhibitor of metalloproteinase-3) in human prostatic adenocarcinomas
    • D. Karan, F.C. Lin, M. Bryan, J. Ringel, N. Moniaux, M.F. Lin, and S.K. Batra Expression of ADAMs (a disintegrin and metalloproteases) and TIMP-3 (tissue inhibitor of metalloproteinase-3) in human prostatic adenocarcinomas Int. J. Oncol. 23 2003 1365 1371
    • (2003) Int. J. Oncol. , vol.23 , pp. 1365-1371
    • Karan, D.1    Lin, F.C.2    Bryan, M.3    Ringel, J.4    Moniaux, N.5    Lin, M.F.6    Batra, S.K.7
  • 30
    • 27644466636 scopus 로고    scopus 로고
    • Clinical significance of heparin-binding epidermal growth factor-like growth factor and a disintegrin and metalloprotease 17 expression in human ovarian cancer
    • Y. Tanaka, S. Miyamoto, S.O. Suzuki, E. Oki, H. Yagi, K. Sonoda, A. Yamazaki, H. Mizushima, Y. Maehara, E. Mekada, and H. Nakano Clinical significance of heparin-binding epidermal growth factor-like growth factor and a disintegrin and metalloprotease 17 expression in human ovarian cancer Clin. Cancer Res. 11 2005 4783 4792
    • (2005) Clin. Cancer Res. , vol.11 , pp. 4783-4792
    • Tanaka, Y.1    Miyamoto, S.2    Suzuki, S.O.3    Oki, E.4    Yagi, H.5    Sonoda, K.6    Yamazaki, A.7    Mizushima, H.8    Maehara, Y.9    Mekada, E.10    Nakano, H.11
  • 32
    • 33749489415 scopus 로고    scopus 로고
    • Aberrant expression of a disintegrin and metalloproteinase 17/tumor necrosis factor-alpha converting enzyme increases the malignant potential in human pancreatic ductal adenocarcinoma
    • J. Ringel, R. Jesnowski, N. Moniaux, J. Lüttges, J. Ringel, A. Choudhury, S.K. Batra, G. Klöppel, and M. Löhr Aberrant expression of a disintegrin and metalloproteinase 17/tumor necrosis factor-alpha converting enzyme increases the malignant potential in human pancreatic ductal adenocarcinoma Cancer Res. 66 2006 9045 9053
    • (2006) Cancer Res. , vol.66 , pp. 9045-9053
    • Ringel, J.1    Jesnowski, R.2    Moniaux, N.3    Lüttges, J.4    Ringel, J.5    Choudhury, A.6    Batra, S.K.7    Klöppel, G.8    Löhr, M.9
  • 35
    • 70450198396 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transitions in development and disease
    • J.P. Thiery, H. Acloque, R.Y. Huang, and M.A. Nieto Epithelial-mesenchymal transitions in development and disease Cell 139 2009 871 890
    • (2009) Cell , vol.139 , pp. 871-890
    • Thiery, J.P.1    Acloque, H.2    Huang, R.Y.3    Nieto, M.A.4
  • 36
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • D. Hanahan, and R.A. Weinberg Hallmarks of cancer: the next generation Cell 144 2011 646 674
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 37
    • 84865839326 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transitions: Insights from development
    • J. Lim, and J.P. Thiery Epithelial-mesenchymal transitions: insights from development Development 139 2012 3471 3486
    • (2012) Development , vol.139 , pp. 3471-3486
    • Lim, J.1    Thiery, J.P.2
  • 38
    • 23844528776 scopus 로고    scopus 로고
    • The Snail genes as inducers of cell movement and survival: Implications in development and cancer
    • A. Barrallo-Gimeno, and M.A. Nieto The Snail genes as inducers of cell movement and survival: implications in development and cancer Development 132 2005 3151 3161
    • (2005) Development , vol.132 , pp. 3151-3161
    • Barrallo-Gimeno, A.1    Nieto, M.A.2
  • 39
    • 34249289041 scopus 로고    scopus 로고
    • Snail, Zeb and bHLH factors in tumour progression: An alliance against the epithelial phenotype?
    • H. Peinado, D. Olmeda, and A. Cano Snail, Zeb and bHLH factors in tumour progression: an alliance against the epithelial phenotype? Nat. Rev. Cancer 7 2007 415 428
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 415-428
    • Peinado, H.1    Olmeda, D.2    Cano, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.