메뉴 건너뛰기




Volumn 47, Issue 2, 2011, Pages 305-315

Organ specific regulation of tumour invasiveness and gelatinolytic activity at the invasive front

Author keywords

Animal model; Gelatinolytic activity; Matrix metalloproteinases; Oral cancer; Skin cancer; Tumour invasiveness

Indexed keywords

GELATINASE A; GELATINASE B; MATRILYSIN; MATRIX METALLOPROTEINASE 14; MESSENGER RNA; UROKINASE; UROKINASE RECEPTOR; UVOMORULIN;

EID: 78650688657     PISSN: 09598049     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejca.2010.09.006     Document Type: Article
Times cited : (8)

References (34)
  • 1
    • 0036152352 scopus 로고    scopus 로고
    • Presentation, treatment, and outcome of oral cavity cancer: A National Cancer Data Base report
    • G.F. Funk, L.H. Karnell, and R.A. Robinson Presentation, treatment, and outcome of oral cavity cancer: a National Cancer Data Base report Head Neck 24 2002 165 180
    • (2002) Head Neck , vol.24 , pp. 165-180
    • Funk, G.F.1    Karnell, L.H.2    Robinson, R.A.3
  • 2
    • 60449092062 scopus 로고    scopus 로고
    • Nonmelanoma skin cancer of the head and neck I: Histopathology and clinical behavior
    • J.F. McGuire, N.N. Ge, and S. Dyson Nonmelanoma skin cancer of the head and neck I: histopathology and clinical behavior Am J Otolaryngol 30 2009 121 133
    • (2009) Am J Otolaryngol , vol.30 , pp. 121-133
    • McGuire, J.F.1    Ge, N.N.2    Dyson, S.3
  • 3
    • 0036329807 scopus 로고    scopus 로고
    • New insights into the role of extracellular matrix during tumor onset and progression
    • S.M. Pupa, S. Menard, S. Forti, and E. Tagliabue New insights into the role of extracellular matrix during tumor onset and progression J Cell Physiol 192 2002 259 267
    • (2002) J Cell Physiol , vol.192 , pp. 259-267
    • Pupa, S.M.1    Menard, S.2    Forti, S.3    Tagliabue, E.4
  • 5
    • 32944459251 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Roles in cancer and metastasis
    • B. Fingleton Matrix metalloproteinases: roles in cancer and metastasis Front Biosci 11 2006 479 491
    • (2006) Front Biosci , vol.11 , pp. 479-491
    • Fingleton, B.1
  • 6
    • 5444219883 scopus 로고    scopus 로고
    • Matrix metalloproteinases in cancer: From new functions to improved inhibition strategies
    • A.R. Folgueras, A.M. Pendas, L.M. Sanchez, and C. Lopez-Otin Matrix metalloproteinases in cancer: from new functions to improved inhibition strategies Int J Dev Biol 48 2004 411 424
    • (2004) Int J Dev Biol , vol.48 , pp. 411-424
    • Folgueras, A.R.1    Pendas, A.M.2    Sanchez, L.M.3    Lopez-Otin, C.4
  • 7
    • 0034650486 scopus 로고    scopus 로고
    • Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis
    • Q. Yu, and I. Stamenkovic Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis Genes Dev 14 2000 163 176
    • (2000) Genes Dev , vol.14 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2
  • 8
    • 34250312341 scopus 로고    scopus 로고
    • The biochemical, biological, and pathological kaleidoscope of cell surface substrates processed by matrix metalloproteinases
    • B. Cauwe, P.E. Van den Steen, and G. Opdenakker The biochemical, biological, and pathological kaleidoscope of cell surface substrates processed by matrix metalloproteinases Crit Rev Biochem Mol Biol 42 2007 113 185
    • (2007) Crit Rev Biochem Mol Biol , vol.42 , pp. 113-185
    • Cauwe, B.1    Van Den Steen, P.E.2    Opdenakker, G.3
  • 9
    • 0035147313 scopus 로고    scopus 로고
    • Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1
    • V. Noe, B. Fingleton, and K. Jacobs Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1 J Cell Sci 114 2001 111 118
    • (2001) J Cell Sci , vol.114 , pp. 111-118
    • Noe, V.1    Fingleton, B.2    Jacobs, K.3
  • 10
    • 31544441678 scopus 로고    scopus 로고
    • Loss of intercellular adhesion activates a transition from low- to high-grade human squamous cell carcinoma
    • A. Margulis, W. Zhang, and A. lt-Holland Loss of intercellular adhesion activates a transition from low- to high-grade human squamous cell carcinoma Int J Cancer 118 2006 821 831
    • (2006) Int J Cancer , vol.118 , pp. 821-831
    • Margulis, A.1    Zhang, W.2    Lt-Holland, A.3
  • 11
    • 36248960528 scopus 로고    scopus 로고
    • Imatinib inhibits colorectal cancer cell growth and suppresses stromal-induced growth stimulation, MT1-MMP expression and pro-MMP2 activation
    • X.N. Stahtea, A.E. Roussidis, and I. Kanakis Imatinib inhibits colorectal cancer cell growth and suppresses stromal-induced growth stimulation, MT1-MMP expression and pro-MMP2 activation Int J Cancer 121 2007 2808 2814
    • (2007) Int J Cancer , vol.121 , pp. 2808-2814
    • Stahtea, X.N.1    Roussidis, A.E.2    Kanakis, I.3
  • 12
    • 42049094423 scopus 로고    scopus 로고
    • Vascular endothelial growth factor stimulates organ-specific host matrix metalloproteinase-9 expression and ovarian cancer invasion
    • D. Belotti, C. Calcagno, and A. Garofalo Vascular endothelial growth factor stimulates organ-specific host matrix metalloproteinase-9 expression and ovarian cancer invasion Mol Cancer Res 6 2008 525 534
    • (2008) Mol Cancer Res , vol.6 , pp. 525-534
    • Belotti, D.1    Calcagno, C.2    Garofalo, A.3
  • 13
    • 69449103107 scopus 로고    scopus 로고
    • Collagen i regulates matrix metalloproteinase-2 activation in osteosarcoma cells independent of S100A4
    • R. Elenjord, J.B. Allen, and H.T. Johansen Collagen I regulates matrix metalloproteinase-2 activation in osteosarcoma cells independent of S100A4 FEBS J 276 2009 5275 5286
    • (2009) FEBS J , vol.276 , pp. 5275-5286
    • Elenjord, R.1    Allen, J.B.2    Johansen, H.T.3
  • 14
    • 0037052641 scopus 로고    scopus 로고
    • Matrix metalloproteinases in cancer: Prognostic markers and therapeutic targets
    • P. Vihinen, and V.M. Kahari Matrix metalloproteinases in cancer: prognostic markers and therapeutic targets Int J Cancer 99 2002 157 166
    • (2002) Int J Cancer , vol.99 , pp. 157-166
    • Vihinen, P.1    Kahari, V.M.2
  • 15
    • 0038148278 scopus 로고    scopus 로고
    • In situ zymography: A molecular pathology technique to localize endogenous protease activity in tissue sections
    • S.J. Yan, and E.A. Blomme In situ zymography: a molecular pathology technique to localize endogenous protease activity in tissue sections Vet Pathol 40 2003 227 236
    • (2003) Vet Pathol , vol.40 , pp. 227-236
    • Yan, S.J.1    Blomme, E.A.2
  • 16
    • 74049105606 scopus 로고    scopus 로고
    • Gelatin in situ zymography on fixed, paraffin-embedded tissue: Zinc and ethanol fixation preserve enzyme activity
    • E. Hadler-Olsen, P. Kanapathippillai, and E. Berg Gelatin in situ zymography on fixed, paraffin-embedded tissue: zinc and ethanol fixation preserve enzyme activity J Histochem Cytochem 58 2010 29 39
    • (2010) J Histochem Cytochem , vol.58 , pp. 29-39
    • Hadler-Olsen, E.1    Kanapathippillai, P.2    Berg, E.3
  • 17
    • 0026763180 scopus 로고
    • UT-MUC-1, a new mucoepidermoid carcinoma cell line, and its radiosensitivity
    • R. Grenman, K. Pekkola-Heino, and H. Joensuu UT-MUC-1, a new mucoepidermoid carcinoma cell line, and its radiosensitivity Arch Otolaryngol Head Neck Surg 118 1992 542 547
    • (1992) Arch Otolaryngol Head Neck Surg , vol.118 , pp. 542-547
    • Grenman, R.1    Pekkola-Heino, K.2    Joensuu, H.3
  • 18
    • 9944222565 scopus 로고    scopus 로고
    • Epithelial hyaluronic acid and CD44v6 are mutually involved in invasion of colorectal adenocarcinomas and linked to patient prognosis
    • M. Kobel, W. Weichert, and K. Cruwell Epithelial hyaluronic acid and CD44v6 are mutually involved in invasion of colorectal adenocarcinomas and linked to patient prognosis Virchows Arch 445 2004 456 464
    • (2004) Virchows Arch , vol.445 , pp. 456-464
    • Kobel, M.1    Weichert, W.2    Cruwell, K.3
  • 19
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method
    • K.J. Livak, and T.D. Schmittgen Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method Methods 25 2001 402 408
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 20
    • 19344366798 scopus 로고    scopus 로고
    • Gelatinase-mediated migration and invasion of cancer cells
    • M. Bjorklund, and E. Koivunen Gelatinase-mediated migration and invasion of cancer cells Biochim Biophys Acta 1755 2005 37 69
    • (2005) Biochim Biophys Acta , vol.1755 , pp. 37-69
    • Bjorklund, M.1    Koivunen, E.2
  • 23
    • 70349883764 scopus 로고    scopus 로고
    • Distinct progression-associated expression of tumor and stromal MMPs in HaCaT skin SCCs correlates with onset of invasion
    • S. Vosseler, W. Lederle, and K. Airola Distinct progression-associated expression of tumor and stromal MMPs in HaCaT skin SCCs correlates with onset of invasion Int J Cancer 125 2009 2296 2306
    • (2009) Int J Cancer , vol.125 , pp. 2296-2306
    • Vosseler, S.1    Lederle, W.2    Airola, K.3
  • 24
    • 10844266658 scopus 로고    scopus 로고
    • Microtubule-dependent matrix metalloproteinase-2/matrix metalloproteinase-9 exocytosis: Prerequisite in human melanoma cell invasion
    • E.M. Schnaeker, R. Ossig, and T. Ludwig Microtubule-dependent matrix metalloproteinase-2/matrix metalloproteinase-9 exocytosis: prerequisite in human melanoma cell invasion Cancer Res 64 2004 8924 8931
    • (2004) Cancer Res , vol.64 , pp. 8924-8931
    • Schnaeker, E.M.1    Ossig, R.2    Ludwig, T.3
  • 25
    • 38949121712 scopus 로고    scopus 로고
    • Intracellular co-localization of trypsin-2 and matrix metalloprotease-9: Possible proteolytic cascade of trypsin-2, MMP-9 and enterokinase in carcinoma
    • S.T. Vilen, P. Nyberg, and M. Hukkanen Intracellular co-localization of trypsin-2 and matrix metalloprotease-9: possible proteolytic cascade of trypsin-2, MMP-9 and enterokinase in carcinoma Exp Cell Res 314 2008 914 926
    • (2008) Exp Cell Res , vol.314 , pp. 914-926
    • Vilen, S.T.1    Nyberg, P.2    Hukkanen, M.3
  • 26
    • 0036172425 scopus 로고    scopus 로고
    • Shedding of the matrix metalloproteinases MMP-2, MMP-9, and MT1-MMP as membrane vesicle-associated components by endothelial cells
    • G. Taraboletti, S. D'Ascenzo, and P. Borsotti Shedding of the matrix metalloproteinases MMP-2, MMP-9, and MT1-MMP as membrane vesicle-associated components by endothelial cells Am J Pathol 160 2002 673 680
    • (2002) Am J Pathol , vol.160 , pp. 673-680
    • Taraboletti, G.1    D'Ascenzo, S.2    Borsotti, P.3
  • 27
    • 0029257171 scopus 로고
    • Urokinase/urokinase receptor system: Internalization/degradation of urokinase-serpin complexes: Mechanism and regulation
    • M. Conese, and F. Blasi Urokinase/urokinase receptor system: internalization/degradation of urokinase-serpin complexes: mechanism and regulation Biol Chem Hoppe Seyler 376 1995 143 155
    • (1995) Biol Chem Hoppe Seyler , vol.376 , pp. 143-155
    • Conese, M.1    Blasi, F.2
  • 28
    • 33646580678 scopus 로고    scopus 로고
    • Mislocalization and unconventional functions of cellular MMPs in cancer
    • A.Y. Strongin Mislocalization and unconventional functions of cellular MMPs in cancer Cancer Metastasis Rev 25 2006 87 98
    • (2006) Cancer Metastasis Rev , vol.25 , pp. 87-98
    • Strongin, A.Y.1
  • 29
    • 33646576168 scopus 로고    scopus 로고
    • Degradomics: Systems biology of the protease web. Pleiotropic roles of MMPs in cancer
    • C.M. Overall, and R.A. Dean Degradomics: systems biology of the protease web. Pleiotropic roles of MMPs in cancer Cancer Metastasis Rev 25 2006 69 75
    • (2006) Cancer Metastasis Rev , vol.25 , pp. 69-75
    • Overall, C.M.1    Dean, R.A.2
  • 30
    • 0001071353 scopus 로고    scopus 로고
    • Cancer invasion and tissue remodeling - Cooperation of protease systems and cell types
    • K. Dano, J. Romer, and B.S. Nielsen Cancer invasion and tissue remodeling - cooperation of protease systems and cell types APMIS 107 1999 120 127
    • (1999) APMIS , vol.107 , pp. 120-127
    • Dano, K.1    Romer, J.2    Nielsen, B.S.3
  • 31
    • 0033199235 scopus 로고    scopus 로고
    • Functional overlap between two classes of matrix-degrading proteases in wound healing
    • L.R. Lund, J. Romer, and T.H. Bugge Functional overlap between two classes of matrix-degrading proteases in wound healing EMBO J 18 1999 4645 4656
    • (1999) EMBO J , vol.18 , pp. 4645-4656
    • Lund, L.R.1    Romer, J.2    Bugge, T.H.3
  • 32
    • 0036906177 scopus 로고    scopus 로고
    • UPAR: A versatile signalling orchestrator
    • F. Blasi, and P. Carmeliet UPAR: a versatile signalling orchestrator Nat Rev Mol Cell Biol 3 2002 932 943
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 932-943
    • Blasi, F.1    Carmeliet, P.2
  • 33
    • 0036790977 scopus 로고    scopus 로고
    • Diversity, topographic differentiation, and positional memory in human fibroblasts
    • H.Y. Chang, J.T. Chi, and S. Dudoit Diversity, topographic differentiation, and positional memory in human fibroblasts Proc Natl Acad Sci USA 99 2002 12877 12882
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12877-12882
    • Chang, H.Y.1    Chi, J.T.2    Dudoit, S.3
  • 34
    • 34548175512 scopus 로고    scopus 로고
    • Signaling networks guiding epithelial-mesenchymal transitions during embryogenesis and cancer progression
    • A. Moustakas, and C.H. Heldin Signaling networks guiding epithelial-mesenchymal transitions during embryogenesis and cancer progression Cancer Sci 98 2007 1512 1520
    • (2007) Cancer Sci , vol.98 , pp. 1512-1520
    • Moustakas, A.1    Heldin, C.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.