메뉴 건너뛰기




Volumn 1824, Issue 1, 2012, Pages 123-132

Live-cell imaging of tumor proteolysis: Impact of cellular and non-cellular microenvironment

Author keywords

3D culture; Functional imaging; Lysosomal proteases; Organotypic models; Proteolytic networks; Tumor microenvironment

Indexed keywords

COLLAGENASE 3; CYSTEINE PROTEINASE; GELATINASE A; GELATINASE B; MATRIX METALLOPROTEINASE 14; STROMELYSIN 3; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TISSUE INHIBITOR OF METALLOPROTEINASE 2;

EID: 82755189529     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2011.07.025     Document Type: Review
Times cited : (22)

References (176)
  • 2
    • 34347221894 scopus 로고    scopus 로고
    • Expanding the complexity of the human degradome: Polyserases and their tandem serine protease domains
    • S. Cal, A. Moncada-Pazos, and C. Lopez-Otin Expanding the complexity of the human degradome: polyserases and their tandem serine protease domains Front. Biosci. 12 2007 4661 4669
    • (2007) Front. Biosci. , vol.12 , pp. 4661-4669
    • Cal, S.1    Moncada-Pazos, A.2    Lopez-Otin, C.3
  • 4
  • 6
    • 0037169361 scopus 로고    scopus 로고
    • Cancer modeling in the modern era: Progress and challenges
    • DOI 10.1016/S0092-8674(02)00621-9
    • T. Van Dyke, and T. Jacks Cancer modeling in the modern era: progress and challenges Cell 108 2002 135 144 (Pubitemid 34161134)
    • (2002) Cell , vol.108 , Issue.2 , pp. 135-144
    • Van Dyke, T.1    Jacks, T.2
  • 7
    • 0036467484 scopus 로고    scopus 로고
    • Technologically advanced cancer modeling in mice
    • DOI 10.1016/S0959-437X(01)00272-6
    • D.A. Tuveson, and T. Jacks Technologically advanced cancer modeling in mice Curr. Opin. Genet. Dev. 12 2002 105 110 (Pubitemid 34094998)
    • (2002) Current Opinion in Genetics and Development , vol.12 , Issue.1 , pp. 105-110
    • Tuveson, D.A.1    Jacks, T.2
  • 8
    • 78650424066 scopus 로고    scopus 로고
    • Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting
    • C. Gialeli, A.D. Theocharis, and N.K. Karamanos Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting FEBS J. 278 2011 16 27
    • (2011) FEBS J. , vol.278 , pp. 16-27
    • Gialeli, C.1    Theocharis, A.D.2    Karamanos, N.K.3
  • 9
    • 70350417461 scopus 로고    scopus 로고
    • Matrix invasion by tumour cells: A focus on MT1-MMP trafficking to invadopodia
    • R. Poincloux, F. Lizarraga, and P. Chavrier Matrix invasion by tumour cells: a focus on MT1-MMP trafficking to invadopodia J. Cell Sci. 122 2009 3015 3024
    • (2009) J. Cell Sci. , vol.122 , pp. 3015-3024
    • Poincloux, R.1    Lizarraga, F.2    Chavrier, P.3
  • 10
    • 79955022479 scopus 로고    scopus 로고
    • Type II transmembrane serine protease (TTSP) deregulation in cancer
    • S.L. Webb, A.J. Sanders, M.D. Mason, and W.G. Jiang Type II transmembrane serine protease (TTSP) deregulation in cancer Front. Biosci. 16 2011 539 552
    • (2011) Front. Biosci. , vol.16 , pp. 539-552
    • Webb, S.L.1    Sanders, A.J.2    Mason, M.D.3    Jiang, W.G.4
  • 11
    • 0034722898 scopus 로고    scopus 로고
    • Critical appraisal of the use of matrix metalloproteinase inhibitors in cancer treatment
    • DOI 10.1038/sj.onc.1204097
    • S. Zucker, J. Cao, and W.T. Chen Critical appraisal of the use of matrix metalloproteinase inhibitors in cancer treatment Oncogene 19 2000 6642 6650 (Pubitemid 32197703)
    • (2000) Oncogene , vol.19 , Issue.56 , pp. 6642-6650
    • Zucker, S.1    Cao, J.2    Chen, W.-T.3
  • 12
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: Trials and tribulations
    • DOI 10.1126/science.1067100
    • L.M. Coussens, B. Fingleton, and L.M. Matrisian Matrix metalloproteinase inhibitors and cancer: trials and tribulations Science 295 2002 2387 2392 (Pubitemid 34270240)
    • (2002) Science , vol.295 , Issue.5564 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 13
    • 75749157368 scopus 로고    scopus 로고
    • Selective matrix metalloproteinase (MMP) inhibitors in cancer therapy: Ready for prime time?
    • S. Zucker, and J. Cao Selective matrix metalloproteinase (MMP) inhibitors in cancer therapy: ready for prime time? Cancer Biol. Ther. 8 2009 2371 2373
    • (2009) Cancer Biol. Ther. , vol.8 , pp. 2371-2373
    • Zucker, S.1    Cao, J.2
  • 14
    • 33644545381 scopus 로고    scopus 로고
    • Validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy
    • DOI 10.1038/nrc1821, PII N1821
    • C.M. Overall, and O. Kleifeld Tumour microenvironment - opinion: validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy Nat. Rev. Cancer 6 2006 227 239 (Pubitemid 43292566)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.3 , pp. 227-239
    • Overall, C.M.1    Kleifeld, O.2
  • 15
    • 8844228268 scopus 로고    scopus 로고
    • Location, location, location: Trafficking and function of secreted proteases of toxoplasma and plasmodium
    • DOI 10.1111/j.1600-0854.2004.00244.x
    • E.M. Binder, and K. Kim Location, location, location: trafficking and function of secreted proteases of Toxoplasma and Plasmodium Traffic 5 2004 914 924 (Pubitemid 39534484)
    • (2004) Traffic , vol.5 , Issue.12 , pp. 914-924
    • Binder, E.M.1    Kim, K.2
  • 16
    • 12744262976 scopus 로고    scopus 로고
    • Cysteine proteases of malaria parasites
    • P.J. Rosenthal Cysteine proteases of malaria parasites Int. J. Parasitol. 34 2004 1489 1499
    • (2004) Int. J. Parasitol. , vol.34 , pp. 1489-1499
    • Rosenthal, P.J.1
  • 18
    • 33749017931 scopus 로고    scopus 로고
    • Cysteine cathepsins: Multifunctional enzymes in cancer
    • DOI 10.1038/nrc1949, PII NRC1949
    • M.M. Mohamed, and B.F. Sloane Cysteine cathepsins: multifunctional enzymes in cancer Nat. Rev. Cancer 6 2006 764 775 (Pubitemid 44450465)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.10 , pp. 764-775
    • Mohamed, M.M.1    Sloane, B.F.2
  • 19
    • 0034486945 scopus 로고    scopus 로고
    • Imaging proteolysis by living human breast cancer cells
    • M. Sameni, K. Moin, and B.F. Sloane Imaging proteolysis by living human breast cancer cells Neoplasia 2 2000 496 504 (Pubitemid 32098684)
    • (2000) Neoplasia , vol.2 , Issue.6 , pp. 496-504
    • Sameni, M.1    Moin, K.2    Sloane, B.F.3
  • 21
    • 60349083291 scopus 로고    scopus 로고
    • Endo180 expression with cofunctional partners MT1-MMP and uPAR-uPA is correlated with prostate cancer progression
    • G. Kogianni, M.M. Walker, J. Waxman, and J. Sturge Endo180 expression with cofunctional partners MT1-MMP and uPAR-uPA is correlated with prostate cancer progression Eur. J. Cancer 45 2009 685 693
    • (2009) Eur. J. Cancer , vol.45 , pp. 685-693
    • Kogianni, G.1    Walker, M.M.2    Waxman, J.3    Sturge, J.4
  • 22
    • 79959823579 scopus 로고    scopus 로고
    • Downregulation of uPARAP mediates cytoskeletal rearrangements and decreases invasion and migration properties in glioma cells
    • S. Takahashi, H. Yamada-Okabe, K. Hamada, S. Ohta, T. Kawase, K. Yoshida, and M. Toda Downregulation of uPARAP mediates cytoskeletal rearrangements and decreases invasion and migration properties in glioma cells J. Neurooncol. 103 2011 267 276
    • (2011) J. Neurooncol. , vol.103 , pp. 267-276
    • Takahashi, S.1    Yamada-Okabe, H.2    Hamada, K.3    Ohta, S.4    Kawase, T.5    Yoshida, K.6    Toda, M.7
  • 23
    • 70849100053 scopus 로고    scopus 로고
    • Membrane type-1 matrix metalloproteinase activity is regulated by the endocytic collagen receptor Endo180
    • G. Messaritou, L. East, C. Roghi, C.M. Isacke, and H. Yarwood Membrane type-1 matrix metalloproteinase activity is regulated by the endocytic collagen receptor Endo180 J. Cell Sci. 122 2009 4042 4048
    • (2009) J. Cell Sci. , vol.122 , pp. 4042-4048
    • Messaritou, G.1    East, L.2    Roghi, C.3    Isacke, C.M.4    Yarwood, H.5
  • 24
    • 12344326777 scopus 로고
    • The histological distribution of proteinase and peptidase activity in solid tumor transplants; A histochemical study on the enzymic characteristics of the different tumor cell types
    • B. Sylven, and H. Malmgren The histological distribution of proteinase and peptidase activity in solid tumor transplants; a histochemical study on the enzymic characteristics of the different tumor cell types Acta Radiol. Suppl. 1957 1 124
    • (1957) Acta Radiol. Suppl. , pp. 1-124
    • Sylven, B.1    Malmgren, H.2
  • 25
    • 0016314296 scopus 로고
    • Immunofluorescent studies on the occurrence of cathepsin B1 at tumor cell surfaces
    • B. Sylven, O. Snellman, and P. Strauli Immunofluorescent studies on the occurrence of cathepsin B1 at tumor cell surfaces Virchows Arch. B Cell Pathol. 17 1974 97 112
    • (1974) Virchows Arch. B Cell Pathol. , vol.17 , pp. 97-112
    • Sylven, B.1    Snellman, O.2    Strauli, P.3
  • 26
    • 0017822028 scopus 로고
    • Differences in secretion of the proteinase cathepsin B at the edges of human breast carcinomas and fibroadenomas
    • A.R. Poole, K.J. Tiltman, A.D. Recklies, and T.A. Stoker Differences in secretion of the proteinase cathepsin B at the edges of human breast carcinomas and fibroadenomas Nature 273 1978 545 547 (Pubitemid 8346587)
    • (1978) Nature , vol.273 , Issue.5663 , pp. 545-547
    • Poole, A.R.1    Tiltman, K.J.2    Recklies, A.D.3    Stoker, T.A.M.4
  • 27
    • 0018841721 scopus 로고
    • Secretion of proteinases from malignant and nonmalignant human breast tissue
    • A.D. Recklies, K.J. Tiltman, T.A. Stoker, and A.R. Poole Secretion of proteinases from malignant and nonmalignant human breast tissue Cancer Res. 40 1980 550 556 (Pubitemid 10174866)
    • (1980) Cancer Research , vol.40 , Issue.3 , pp. 550-556
    • Recklies, A.D.1    Tiltman, K.J.2    Stoker, T.A.M.3    Poole, A.R.4
  • 28
    • 0023032007 scopus 로고
    • The major excreted protein of transformed fibroblasts is an activable acid-protease
    • S. Gal, and M.M. Gottesman The major excreted protein of transformed fibroblasts is an activable acid-protease J. Biol. Chem. 261 1986 1760 1765 (Pubitemid 17205010)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.4 , pp. 1760-1765
    • Gal, S.1    Gottesman, M.M.2
  • 30
    • 0023575526 scopus 로고
    • Properties of a plasma membrane-associated cathepsin B-like cysteine proteinase in metastatic B16 melanoma variants
    • J. Rozhin, D. Robinson, M.A. Stevens, T.T. Lah, K.V. Honn, R.E. Ryan, and B.F. Sloane Properties of a plasma membrane-associated cathepsin B-like cysteine proteinase in metastatic B16 melanoma variants Cancer Res. 47 1987 6620 6628 (Pubitemid 18019666)
    • (1987) Cancer Research , vol.47 , Issue.24 , pp. 6620-6628
    • Rozhin, J.1    Robinson, D.2    Stevens, M.A.3    Lah, T.T.4    Honn, K.V.5    Ryan, R.E.6    Sloane, B.F.7
  • 31
    • 0034725119 scopus 로고    scopus 로고
    • Human procathepsin B interacts with the annexin II tetramer on the surface of tumor cells
    • DOI 10.1074/jbc.275.17.12806
    • J. Mai, R.L. Finley Jr., D.M. Waisman, and B.F. Sloane Human procathepsin B interacts with the annexin II tetramer on the surface of tumor cells J. Biol. Chem. 275 2000 12806 12812 (Pubitemid 30241435)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.17 , pp. 12806-12812
    • Mai, J.1    Finley Jr., R.L.2    Waisman, D.M.3    Sloane, B.F.4
  • 32
    • 63049095880 scopus 로고    scopus 로고
    • Live-cell imaging demonstrates extracellular matrix degradation in association with active cathepsin B in caveolae of endothelial cells during tube formation
    • D. Cavallo-Medved, D. Rudy, G. Blum, M. Bogyo, D. Caglic, and B.F. Sloane Live-cell imaging demonstrates extracellular matrix degradation in association with active cathepsin B in caveolae of endothelial cells during tube formation Exp. Cell Res. 315 2009 1234 1246
    • (2009) Exp. Cell Res. , vol.315 , pp. 1234-1246
    • Cavallo-Medved, D.1    Rudy, D.2    Blum, G.3    Bogyo, M.4    Caglic, D.5    Sloane, B.F.6
  • 33
    • 17844362479 scopus 로고    scopus 로고
    • Caveolin-1 mediates the expression and localization of cathepsin B, pro-urokinase plasminogen activator and their cell-surface receptors in human colorectal carcinoma cells
    • DOI 10.1242/jcs.02278
    • D. Cavallo-Medved, J. Mai, J. Dosescu, M. Sameni, and B.F. Sloane Caveolin-1 mediates the expression and localization of cathepsin B, pro-urokinase plasminogen activator and their cell-surface receptors in human colorectal carcinoma cells J. Cell Sci. 118 2005 1493 1503 (Pubitemid 40585129)
    • (2005) Journal of Cell Science , vol.118 , Issue.7 , pp. 1493-1503
    • Cavallo-Medved, D.1    Mai, J.2    Dosescu, J.3    Sameni, M.4    Sloane, B.F.5
  • 34
    • 81155127516 scopus 로고    scopus 로고
    • Inhibition of cathepsin B activity attenuates extracellular matrix degradation and inflammatory breast cancer invasion
    • in press
    • B.C. Victor, A. Anbalagan, M.M. Mohamed, B.F. Sloane, D. Cavallo-Medved, in press. Inhibition of cathepsin B activity attenuates extracellular matrix degradation and inflammatory breast cancer invasion, Breast Cancer Res.
    • Breast Cancer Res.
    • Victor, B.C.1    Anbalagan, A.2    Mohamed, M.M.3    Sloane, B.F.4    Cavallo-Medved, D.5
  • 35
    • 35848947186 scopus 로고    scopus 로고
    • Cysteine cathepsin non-inhibitory binding partners: Modulating intracellular trafficking and function
    • DOI 10.1515/BC.2007.150
    • B.C. Victor, and B.F. Sloane Cysteine cathepsin non-inhibitory binding partners: modulating intracellular trafficking and function Biol. Chem. 388 2007 1131 1140 (Pubitemid 350059626)
    • (2007) Biological Chemistry , vol.388 , Issue.11 , pp. 1131-1140
    • Victor, B.C.1    Sloane, B.F.2
  • 37
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • M. Egeblad, and Z. Werb New functions for the matrix metalloproteinases in cancer progression Nat. Rev. Cancer 2 2002 161 174 (Pubitemid 37328786)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.3 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 38
    • 0037320124 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors - An emphasis on gastrointestinal malignancies
    • DOI 10.1016/S1040-8428(02)00015-X, PII S104084280200015X
    • I. Chau, A. Rigg, and D. Cunningham Matrix metalloproteinase inhibitors - an emphasis on gastrointestinal malignancies Crit. Rev. Oncol. Hematol. 45 2003 151 176 (Pubitemid 36216311)
    • (2003) Critical Reviews in Oncology/Hematology , vol.45 , Issue.2 , pp. 151-176
    • Chau, I.1    Rigg, A.2    Cunningham, D.3
  • 39
    • 0344874727 scopus 로고    scopus 로고
    • Molecular Imaging of Proteolytic Activity in Cancer
    • DOI 10.1002/jcb.10713
    • J.O. McIntyre, and L.M. Matrisian Molecular imaging of proteolytic activity in cancer J. Cell. Biochem. 90 2003 1087 1097 (Pubitemid 37485047)
    • (2003) Journal of Cellular Biochemistry , vol.90 , Issue.6 , pp. 1087-1097
    • McIntyre, J.O.1    Matrisian, L.M.2
  • 40
    • 0142074839 scopus 로고    scopus 로고
    • Imaging matrix metalloproteinase expression in tumors
    • W.P. Li, and C.J. Anderson Imaging matrix metalloproteinase expression in tumors Q. J. Nucl. Med. 47 2003 201 208 (Pubitemid 37279156)
    • (2003) Quarterly Journal of Nuclear Medicine , vol.47 , Issue.3 , pp. 201-208
    • Li, W.P.1    Anderson, C.J.2
  • 41
    • 0043238937 scopus 로고    scopus 로고
    • Activity of biphenyl matrix metalloproteinase inhibitor BAY 12-9566 in a human breast cancer orthotopic model
    • DOI 10.1023/A:1025473709656
    • S. Nozaki, S. Sissons, D.S. Chien, and G.W. Sledge Jr. Activity of biphenyl matrix metalloproteinase inhibitor BAY 12-9566 in a human breast cancer orthotopic model Clin. Exp. Metastasis 20 2003 407 412 (Pubitemid 37108426)
    • (2003) Clinical and Experimental Metastasis , vol.20 , Issue.5 , pp. 407-412
    • Nozaki, S.1    Sissons, S.2    Chien, D.-S.3    Sledge Jr., G.W.4
  • 43
    • 0030918546 scopus 로고    scopus 로고
    • Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors
    • B. Turk, V. Turk, and D. Turk Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors Biol. Chem. 378 1997 141 150 (Pubitemid 27230596)
    • (1997) Biological Chemistry , vol.378 , Issue.3-4 , pp. 141-150
    • Turk, B.1    Turk, V.2    Turk, D.3
  • 46
    • 36148994693 scopus 로고    scopus 로고
    • The other side of MMPs: Protective roles in tumor progression
    • DOI 10.1007/s10555-007-9089-4, Forty Years of Metastasis Research: A Tribute to Dr. Isaiah J. Fidler
    • M.D. Martin, and L.M. Matrisian The other side of MMPs: protective roles in tumor progression Cancer Metastasis Rev. 26 2007 717 724 (Pubitemid 350115119)
    • (2007) Cancer and Metastasis Reviews , vol.26 , Issue.3-4 , pp. 717-724
    • Martin, M.D.1    Matrisian, L.M.2
  • 47
    • 34648815810 scopus 로고    scopus 로고
    • Emerging roles of proteases in tumour suppression
    • DOI 10.1038/nrc2228, PII NRC2228
    • C. Lopez-Otin, and L.M. Matrisian Emerging roles of proteases in tumour suppression Nat. Rev. Cancer 7 2007 800 808 (Pubitemid 47463671)
    • (2007) Nature Reviews Cancer , vol.7 , Issue.10 , pp. 800-808
    • Lopez-Otin, C.1    Matrisian, L.M.2
  • 48
    • 77249129690 scopus 로고    scopus 로고
    • Avoiding spam in the proteolytic internet: Future strategies for anti-metastatic MMP inhibition
    • A. Kruger, R.E. Kates, and D.R. Edwards Avoiding spam in the proteolytic internet: future strategies for anti-metastatic MMP inhibition Biochim. Biophys. Acta 1803 2010 95 102
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 95-102
    • Kruger, A.1    Kates, R.E.2    Edwards, D.R.3
  • 51
    • 45849098735 scopus 로고    scopus 로고
    • The role of tissue inhibitors of metalloproteinases in tumorigenesis and metastasis
    • DOI 10.1080/10408360801973244, PII 793265826
    • W. Cruz-Munoz, and R. Khokha The role of tissue inhibitors of metalloproteinases in tumorigenesis and metastasis Crit. Rev. Clin. Lab. Sci. 45 2008 291 338 (Pubitemid 351883130)
    • (2008) Critical Reviews in Clinical Laboratory Sciences , vol.45 , Issue.3 , pp. 291-338
    • Cruz-Munoz, W.1    Khokha, R.2
  • 52
    • 77149164774 scopus 로고    scopus 로고
    • Matrix metalloproteinases: What do they not do? New substrates and biological roles identified by murine models and proteomics
    • D. Rodriguez, C.J. Morrison, and C.M. Overall Matrix metalloproteinases: what do they not do? New substrates and biological roles identified by murine models and proteomics Biochim. Biophys. Acta 1803 2010 39 54
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 39-54
    • Rodriguez, D.1    Morrison, C.J.2    Overall, C.M.3
  • 56
    • 79953163995 scopus 로고    scopus 로고
    • Proteolytic networks in cancer
    • S.D. Mason, and J.A. Joyce Proteolytic networks in cancer Trends Cell Biol. 21 2011 228 237
    • (2011) Trends Cell Biol. , vol.21 , pp. 228-237
    • Mason, S.D.1    Joyce, J.A.2
  • 57
    • 69249227502 scopus 로고    scopus 로고
    • Lysosome biogenesis and lysosomal membrane proteins: Trafficking meets function
    • P. Saftig, and J. Klumperman Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function Nat. Rev. Mol. Cell Biol. 10 2009 623 635
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 623-635
    • Saftig, P.1    Klumperman, J.2
  • 59
    • 50849119416 scopus 로고    scopus 로고
    • The caspase-1 inflammasome: A pilot of innate immune responses
    • H.B. Yu, and B.B. Finlay The caspase-1 inflammasome: a pilot of innate immune responses Cell Host Microbe 4 2008 198 208
    • (2008) Cell Host Microbe , vol.4 , pp. 198-208
    • Yu, H.B.1    Finlay, B.B.2
  • 60
    • 0038215389 scopus 로고    scopus 로고
    • Pericellular cathepsin B and malignant progression
    • DOI 10.1023/A:1023007717757
    • S. Roshy, B.F. Sloane, and K. Moin Pericellular cathepsin B and malignant progression Cancer Metastasis Rev. 22 2003 271 286 (Pubitemid 36561062)
    • (2003) Cancer and Metastasis Reviews , vol.22 , Issue.2-3 , pp. 271-286
    • Roshy, S.1    Sloane, B.F.2    Moin, K.3
  • 61
    • 70350094711 scopus 로고    scopus 로고
    • Urokinase-receptor-mediated phenotypic changes in vascular smooth muscle cells require the involvement of membrane rafts
    • J. Kiyan, G. Smith, H. Haller, and I. Dumler Urokinase-receptor-mediated phenotypic changes in vascular smooth muscle cells require the involvement of membrane rafts Biochem. J. 423 2009 343 351
    • (2009) Biochem. J. , vol.423 , pp. 343-351
    • Kiyan, J.1    Smith, G.2    Haller, H.3    Dumler, I.4
  • 62
    • 44249097734 scopus 로고    scopus 로고
    • Invadopodia: At the cutting edge of tumour invasion
    • S.S. Stylli, A.H. Kaye, and P. Lock Invadopodia: at the cutting edge of tumour invasion J. Clin. Neurosci. 15 2008 725 737
    • (2008) J. Clin. Neurosci. , vol.15 , pp. 725-737
    • Stylli, S.S.1    Kaye, A.H.2    Lock, P.3
  • 63
    • 72249116890 scopus 로고    scopus 로고
    • Lipid rafts and caveolin-1 are required for invadopodia formation and extracellular matrix degradation by human breast cancer cells
    • H. Yamaguchi, Y. Takeo, S. Yoshida, Z. Kouchi, Y. Nakamura, and K. Fukami Lipid rafts and caveolin-1 are required for invadopodia formation and extracellular matrix degradation by human breast cancer cells Cancer Res. 69 2009 8594 8602
    • (2009) Cancer Res. , vol.69 , pp. 8594-8602
    • Yamaguchi, H.1    Takeo, Y.2    Yoshida, S.3    Kouchi, Z.4    Nakamura, Y.5    Fukami, K.6
  • 67
    • 1342288875 scopus 로고    scopus 로고
    • Increased expression of caveolin-1 and microvessel density correlates with metastasis and poor prognosis in clear cell renal cell carcinoma
    • DOI 10.1111/j.1464-410X.2004.04604.x
    • H.J. Joo, D.K. Oh, Y.S. Kim, K.B. Lee, and S.J. Kim Increased expression of caveolin-1 and microvessel density correlates with metastasis and poor prognosis in clear cell renal cell carcinoma BJU Int. 93 2004 291 296 (Pubitemid 38253572)
    • (2004) BJU International , vol.93 , Issue.3 , pp. 291-296
    • Joo, H.J.1    Oh, D.K.2    Kim, Y.S.3    Lee, K.B.4    Kim, S.J.5
  • 68
    • 0036841790 scopus 로고    scopus 로고
    • Up-regulated caveolin-1 accentuates the metastasis capability of lung adenocarcinoma by inducing filopodia formation
    • C.C. Ho, P.H. Huang, H.Y. Huang, Y.H. Chen, P.C. Yang, and S.M. Hsu Up-regulated caveolin-1 accentuates the metastasis capability of lung adenocarcinoma by inducing filopodia formation Am. J. Pathol. 161 2002 1647 1656
    • (2002) Am. J. Pathol. , vol.161 , pp. 1647-1656
    • Ho, C.C.1    Huang, P.H.2    Huang, H.Y.3    Chen, Y.H.4    Yang, P.C.5    Hsu, S.M.6
  • 69
    • 0037083622 scopus 로고    scopus 로고
    • Overexpression of caveolin-1 in esophageal squamous cell carcinoma correlates with lymph node metastasis and pathologic stage
    • DOI 10.1002/cncr.10329
    • K. Kato, Y. Hida, M. Miyamoto, H. Hashida, T. Shinohara, T. Itoh, S. Okushiba, S. Kondo, and H. Katoh Overexpression of caveolin-1 in esophageal squamous cell carcinoma correlates with lymph node metastasis and pathologic stage Cancer 94 2002 929 933 (Pubitemid 34150846)
    • (2002) Cancer , vol.94 , Issue.4 , pp. 929-933
    • Kato, K.1    Hida, Y.2    Miyamoto, M.3    Hashida, H.4    Shinohara, T.5    Itoh, T.6    Okushiba, S.7    Kondo, S.8    Katoh, H.9
  • 70
    • 0035153475 scopus 로고    scopus 로고
    • Elevated expression of caveolin-1 in adenocarcinoma of the colon
    • DOI 10.1309/YL54-CCU7-4V0P-FDUT
    • S.W. Fine, M.P. Lisanti, F. Galbiati, and M. Li Elevated expression of caveolin-1 in adenocarcinoma of the colon Am. J. Clin. Pathol. 115 2001 719 724 (Pubitemid 33051539)
    • (2001) American Journal of Clinical Pathology , vol.115 , Issue.5 , pp. 719-724
    • Fine, S.W.1    Lisanti, M.P.2    Galbiati, F.3    Li, M.4
  • 71
    • 0347683401 scopus 로고    scopus 로고
    • Mutant K-ras Regulates Cathepsin B Localization on the Surface of Human Colorectal Carcinoma Cells
    • D. Cavallo-Medved, J. Dosescu, B.E. Linebaugh, M. Sameni, D. Rudy, and B.F. Sloane Mutant K-ras regulates cathepsin B localization on the surface of human colorectal carcinoma cells Neoplasia 5 2003 507 519 (Pubitemid 38045088)
    • (2003) Neoplasia , vol.5 , Issue.6 , pp. 507-519
    • Cavallo-Medved, D.1    Dosescu, J.2    Linebaugh, B.E.3    Sameni, M.4    Rudy, D.5    Sloane, B.F.6
  • 72
    • 10044296956 scopus 로고    scopus 로고
    • Overexpression of caveolin-1 in experimental colon adenocarcinomas and human colon cancer cell lines
    • J.M. Patlolla, M.V. Swamy, J. Raju, and C.V. Rao Overexpression of caveolin-1 in experimental colon adenocarcinomas and human colon cancer cell lines Oncol. Rep. 11 2004 957 963
    • (2004) Oncol. Rep. , vol.11 , pp. 957-963
    • Patlolla, J.M.1    Swamy, M.V.2    Raju, J.3    Rao, C.V.4
  • 76
  • 77
    • 79551588858 scopus 로고    scopus 로고
    • Distinct roles of endothelial and adipocyte caveolin-1 in macrophage infiltration and adipose tissue metabolic activity
    • N. Briand, S. Le Lay, W.C. Sessa, P. Ferre, and I. Dugail Distinct roles of endothelial and adipocyte caveolin-1 in macrophage infiltration and adipose tissue metabolic activity Diabetes 60 2011 448 453
    • (2011) Diabetes , vol.60 , pp. 448-453
    • Briand, N.1    Le Lay, S.2    Sessa, W.C.3    Ferre, P.4    Dugail, I.5
  • 78
    • 17444366177 scopus 로고    scopus 로고
    • S100A10, annexin A2, and annexin A2 heterotetramer as candidate plasminogen receptors
    • M. Kwon, T.J. MacLeod, Y. Zhang, and D.M. Waisman S100A10, annexin A2, and annexin a2 heterotetramer as candidate plasminogen receptors Front. Biosci. 10 2005 300 325 (Pubitemid 40543035)
    • (2005) Frontiers in Bioscience , vol.10 , Issue.1 , pp. 300-325
    • Kwon, M.1    MacLeod, T.J.2    Zhang, Y.3    Waisman, D.M.4
  • 79
    • 0036479735 scopus 로고    scopus 로고
    • Annexin II: A plasminogen-plasminogen activator co-receptor
    • J. Kim, and K.A. Hajjar Annexin II: a plasminogen-plasminogen activator co-receptor Front. Biosci. 7 2002 d341 d348
    • (2002) Front. Biosci. , vol.7
    • Kim, J.1    Hajjar, K.A.2
  • 81
    • 77951883821 scopus 로고    scopus 로고
    • The urokinase receptor: Focused cell surface proteolysis, cell adhesion and signaling
    • F. Blasi, and N. Sidenius The urokinase receptor: focused cell surface proteolysis, cell adhesion and signaling FEBS Lett. 584 2010 1923 1930
    • (2010) FEBS Lett. , vol.584 , pp. 1923-1930
    • Blasi, F.1    Sidenius, N.2
  • 83
    • 0027179188 scopus 로고
    • Effects of membrane-associated cathepsin B on the activtion of receptor-bound prourokinase and subsequent invasion of reconstituted basement membranes
    • DOI 10.1016/0167-4889(93)90109-3
    • H. Kobayashi, N. Moniwa, M. Sugimura, H. Shinohara, H. Ohi, and T. Terao Effects of membrane-associated cathepsin B on the activation of receptor-bound prourokinase and subsequent invasion of reconstituted basement membranes Biochim. Biophys. Acta 1178 1993 55 62 (Pubitemid 23236096)
    • (1993) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1178 , Issue.1 , pp. 55-62
    • Kobayashi, H.1    Moniwa, N.2    Sugimura, M.3    Shinohara, H.4    Ohi, H.5    Terao, T.6
  • 84
    • 0037177886 scopus 로고    scopus 로고
    • Phorbol ester activation of a proteolytic cascade capable of activating latent transforming growth factor-β. A process initiated by the exocytosis of cathepsin B
    • DOI 10.1074/jbc.M108180200
    • M. Guo, P.A. Mathieu, B. Linebaugh, B.F. Sloane, and J.J. Reiners Jr. Phorbol ester activation of a proteolytic cascade capable of activating latent transforming growth factor-betaL a process initiated by the exocytosis of cathepsin B J. Biol. Chem. 277 2002 14829 14837 (Pubitemid 34952555)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.17 , pp. 14829-14837
    • Guo, M.1    Mathieu, P.A.2    Linebaugh, B.3    Sloane, B.F.4    Reiners Jr., J.J.5
  • 85
    • 3543114271 scopus 로고    scopus 로고
    • Foot and mouth: Podosomes, invadopodia and circular dorsal ruffles
    • DOI 10.1038/nrm1436
    • R. Buccione, J.D. Orth, and M.A. McNiven Foot and mouth: podosomes, invadopodia and circular dorsal ruffles Nat. Rev. Mol. Cell Biol. 5 2004 647 657 (Pubitemid 39025065)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.8 , pp. 647-657
    • Buccione, R.1    Orth, J.D.2    McNiven, M.A.3
  • 88
    • 79957521262 scopus 로고    scopus 로고
    • Membrane lipids in invadopodia and podosomes: Key structures for cancer invasion and metastasis
    • H. Yamaguchi, and T. Oikawa Membrane lipids in invadopodia and podosomes: key structures for cancer invasion and metastasis Oncotarget 1 2010 320 328
    • (2010) Oncotarget , vol.1 , pp. 320-328
    • Yamaguchi, H.1    Oikawa, T.2
  • 89
    • 75449112263 scopus 로고    scopus 로고
    • Aiming for invadopodia: Organizing polarized delivery at sites of invasion
    • G. Caldieri, and R. Buccione Aiming for invadopodia: organizing polarized delivery at sites of invasion Trends Cell Biol. 20 2010 64 70
    • (2010) Trends Cell Biol. , vol.20 , pp. 64-70
    • Caldieri, G.1    Buccione, R.2
  • 90
    • 0028152543 scopus 로고
    • A potential marker protease of invasiveness, seprase, is localized on invadopodia of human malignant melanoma cells
    • W.L. Monsky, C.Y. Lin, A. Aoyama, T. Kelly, S.K. Akiyama, S.C. Mueller, and W.T. Chen A potential marker protease of invasiveness, seprase, is localized on invadopodia of human malignant melanoma cells Cancer Res. 54 1994 5702 5710 (Pubitemid 24346270)
    • (1994) Cancer Research , vol.54 , Issue.21 , pp. 5702-5710
    • Monsky, W.L.1    Lin, C.-Y.2    Aoyama, A.3    Kelly, T.4    Akiyama, S.K.5    Mueller, S.C.6    Chen, W.-T.7
  • 91
    • 53149100519 scopus 로고    scopus 로고
    • Seprase: An overview of an important matrix serine protease
    • P. O'Brien, and B.F. O'Connor Seprase: an overview of an important matrix serine protease Biochim. Biophys. Acta 1784 2008 1130 1145
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1130-1145
    • O'Brien, P.1    O'Connor, B.F.2
  • 93
    • 79151475365 scopus 로고    scopus 로고
    • Dynamic membrane remodeling at invadopodia differentiates invadopodia from podosomes
    • V.V. Artym, K. Matsumoto, S.C. Mueller, and K.M. Yamada Dynamic membrane remodeling at invadopodia differentiates invadopodia from podosomes Eur. J. Cell Biol. 90 2011 172 180
    • (2011) Eur. J. Cell Biol. , vol.90 , pp. 172-180
    • Artym, V.V.1    Matsumoto, K.2    Mueller, S.C.3    Yamada, K.M.4
  • 94
    • 76249088362 scopus 로고    scopus 로고
    • Matrix architecture dictates three-dimensional migration modes of human macrophages: Differential involvement of proteases and podosome-like structures
    • E. Van Goethem, R. Poincloux, F. Gauffre, I. Maridonneau-Parini, and V. Le Cabec Matrix architecture dictates three-dimensional migration modes of human macrophages: differential involvement of proteases and podosome-like structures J. Immunol. 184 2010 1049 1061
    • (2010) J. Immunol. , vol.184 , pp. 1049-1061
    • Van Goethem, E.1    Poincloux, R.2    Gauffre, F.3    Maridonneau-Parini, I.4    Le Cabec, V.5
  • 95
    • 65249155429 scopus 로고    scopus 로고
    • Protease-dependent versus -independent cancer cell invasion programs: Three-dimensional amoeboid movement revisited
    • F. Sabeh, R. Shimizu-Hirota, and S.J. Weiss Protease-dependent versus -independent cancer cell invasion programs: three-dimensional amoeboid movement revisited J. Cell Biol. 185 2009 11 19
    • (2009) J. Cell Biol. , vol.185 , pp. 11-19
    • Sabeh, F.1    Shimizu-Hirota, R.2    Weiss, S.J.3
  • 96
    • 56449113201 scopus 로고    scopus 로고
    • Lysosomal cathepsin B participates in the podosome-mediated extracellular matrix degradation and invasion via secreted lysosomes in v-Src fibroblasts
    • C. Tu, C.F. Ortega-Cava, G. Chen, N.D. Fernandes, D. Cavallo-Medved, B.F. Sloane, V. Band, and H. Band Lysosomal cathepsin B participates in the podosome-mediated extracellular matrix degradation and invasion via secreted lysosomes in v-Src fibroblasts Cancer Res. 68 2008 9147 9156
    • (2008) Cancer Res. , vol.68 , pp. 9147-9156
    • Tu, C.1    Ortega-Cava, C.F.2    Chen, G.3    Fernandes, N.D.4    Cavallo-Medved, D.5    Sloane, B.F.6    Band, V.7    Band, H.8
  • 97
    • 49049118735 scopus 로고    scopus 로고
    • Actin cytoskeletal organisation in osteoclasts: A model to decipher transmigration and matrix degradation
    • F. Saltel, A. Chabadel, E. Bonnelye, and P. Jurdic Actin cytoskeletal organisation in osteoclasts: a model to decipher transmigration and matrix degradation Eur. J. Cell Biol. 87 2008 459 468
    • (2008) Eur. J. Cell Biol. , vol.87 , pp. 459-468
    • Saltel, F.1    Chabadel, A.2    Bonnelye, E.3    Jurdic, P.4
  • 99
    • 0036423664 scopus 로고    scopus 로고
    • Formation and function of the ruffled border in osteoclasts
    • DOI 10.1016/S1084952102000587
    • G. Stenbeck Formation and function of the ruffled border in osteoclasts Semin. Cell Dev. Biol. 13 2002 285 292 (Pubitemid 35304514)
    • (2002) Seminars in Cell and Developmental Biology , vol.13 , Issue.4 , pp. 285-292
    • Stenbeck, G.1
  • 100
    • 0027373117 scopus 로고
    • Vacuolar-type H(+)-ATPases are functionally expressed in plasma membranes of human tumor cells
    • R. Martinez-Zaguilan, R.M. Lynch, G.M. Martinez, and R.J. Gillies Vacuolar-type H(+)-ATPases are functionally expressed in plasma membranes of human tumor cells Am. J. Physiol. 265 1993 C1015 C1029
    • (1993) Am. J. Physiol. , vol.265
    • Martinez-Zaguilan, R.1    Lynch, R.M.2    Martinez, G.M.3    Gillies, R.J.4
  • 102
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • D. Hanahan, and R.A. Weinberg The hallmarks of cancer Cell 100 2000 57 70 (Pubitemid 30046295)
    • (2000) Cell , vol.100 , Issue.1 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 103
    • 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
  • 105
    • 0021732164 scopus 로고
    • The relevance of tumour pH to the treatment of malignant disease
    • J.L. Wike-Hooley, J. Haveman, and H.S. Reinhold The relevance of tumour pH to the treatment of malignant disease Radiother. Oncol. 2 1984 343 366 (Pubitemid 15166545)
    • (1984) Radiotherapy and Oncology , vol.2 , Issue.4 , pp. 343-366
    • Wike-Hooley, J.L.1    Haveman, J.2    Reinhold, H.S.3
  • 109
    • 0037348402 scopus 로고    scopus 로고
    • + diffusion to the acidic pH of tumors
    • P.A. Schornack, and R.J. Gillies Contributions of cell metabolism and H + diffusion to the acidic pH of tumors Neoplasia 5 2003 135 145 (Pubitemid 36369009)
    • (2003) Neoplasia , vol.5 , Issue.2 , pp. 135-145
    • Schomack, P.A.1    Gillies, R.J.2
  • 111
    • 0028618307 scopus 로고
    • Pericellular pH affects distribution and secretion of cathepsin B in malignant cells
    • J. Rozhin, M. Sameni, G. Ziegler, and B.F. Sloane Pericellular pH affects distribution and secretion of cathepsin B in malignant cells Cancer Res. 54 1994 6517 6525
    • (1994) Cancer Res. , vol.54 , pp. 6517-6525
    • Rozhin, J.1    Sameni, M.2    Ziegler, G.3    Sloane, B.F.4
  • 112
    • 0029970607 scopus 로고    scopus 로고
    • Implications of acidic tumor microenvironment for neoplastic growth and cancer treatment: A computer analysis
    • M. Kraus, and B. Wolf Implications of acidic tumor microenvironment for neoplastic growth and cancer treatment: a computer analysis Tumour Biol. 17 1996 133 154 (Pubitemid 26150508)
    • (1996) Tumor Biology , vol.17 , Issue.3 , pp. 133-154
    • Kraus, M.1    Wolf, B.2
  • 113
    • 0030614893 scopus 로고    scopus 로고
    • 2 gradients in solid tumors in vivo: High-resolution measurements reveal a lack of correlation
    • DOI 10.1038/nm0297-177
    • G. Helmlinger, F. Yuan, M. Dellian, and R.K. Jain Interstitial pH and pO2 gradients in solid tumors in vivo: high-resolution measurements reveal a lack of correlation Nat. Med. 3 1997 177 182 (Pubitemid 27064702)
    • (1997) Nature Medicine , vol.3 , Issue.2 , pp. 177-182
    • Helmlinger, G.1    Yuan, F.2    Dellian, M.3    Jain, R.K.4
  • 114
    • 0035071662 scopus 로고    scopus 로고
    • The effects of extracellular pH on immune function
    • A. Lardner The effects of extracellular pH on immune function J. Leukoc. Biol. 69 2001 522 530 (Pubitemid 32294836)
    • (2001) Journal of Leukocyte Biology , vol.69 , Issue.4 , pp. 522-530
    • Lardner, A.1
  • 115
    • 0034662635 scopus 로고    scopus 로고
    • Acidic pH-induced elevation in interleukin 8 expression by human ovarian carcinoma cells
    • L. Xu, and I.J. Fidler Acidic pH-induced elevation in interleukin 8 expression by human ovarian carcinoma cells Cancer Res. 60 2000 4610 4616 (Pubitemid 32103647)
    • (2000) Cancer Research , vol.60 , Issue.16 , pp. 4610-4616
    • Xu, L.1    Fidler, I.J.2
  • 116
    • 0037192802 scopus 로고    scopus 로고
    • Acidic extracellular pH induces vascular endothelial growth factor (VEGF) in human glioblastoma cells via ERK1/2 MAPK signaling pathway. Mechanism of low pH-induced VEGF
    • DOI 10.1074/jbc.M108347200
    • L. Xu, D. Fukumura, and R.K. Jain Acidic extracellular pH induces vascular endothelial growth factor (VEGF) in human glioblastoma cells via ERK1/2 MAPK signaling pathway: mechanism of low pH-induced VEGF J. Biol. Chem. 277 2002 11368 11374 (Pubitemid 34952903)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.13 , pp. 11368-11374
    • Xu, L.1    Fukumura, D.2    Jain, R.K.3
  • 117
    • 0035927544 scopus 로고    scopus 로고
    • Regulation of vascular endothelial growth factor expression by acidosis in human cancer cells
    • DOI 10.1038/sj.onc.1204500
    • Q. Shi, X. Le, B. Wang, J.L. Abbruzzese, Q. Xiong, Y. He, and K. Xie Regulation of vascular endothelial growth factor expression by acidosis in human cancer cells Oncogene 20 2001 3751 3756 (Pubitemid 32624967)
    • (2001) Oncogene , vol.20 , Issue.28 , pp. 3751-3756
    • Shi, Q.1    Le, X.2    Wang, B.3    Abbruzzese, J.L.4    Xiong, Q.5    He, Y.6    Xie, K.7
  • 120
  • 121
    • 33746149756 scopus 로고    scopus 로고
    • Acidic extracellular pH promotes experimental metastasis of human melanoma cells in athymic nude mice
    • DOI 10.1158/0008-5472.CAN-06-0983
    • E.K. Rofstad, B. Mathiesen, K. Kindem, and K. Galappathi Acidic extracellular pH promotes experimental metastasis of human melanoma cells in athymic nude mice Cancer Res. 66 2006 6699 6707 (Pubitemid 44085627)
    • (2006) Cancer Research , vol.66 , Issue.13 , pp. 6699-6707
    • Rofstad, E.K.1    Mathiesen, B.2    Kindem, K.3    Galappathi, K.4
  • 122
    • 0025771024 scopus 로고
    • Glucose starvation and acidosis: Effect on experimental metastatic potential, DNA content and MTX resistance of murine tumour cells
    • O.K. Schlappack, A. Zimmermann, and R.P. Hill Glucose starvation and acidosis: effect on experimental metastatic potential, DNA content and MTX resistance of murine tumour cells Br. J. Cancer 64 1991 663 670
    • (1991) Br. J. Cancer , vol.64 , pp. 663-670
    • Schlappack, O.K.1    Zimmermann, A.2    Hill, R.P.3
  • 124
    • 0038486779 scopus 로고    scopus 로고
    • Molecular regulation of human cathepsin B: Implication in pathologies
    • DOI 10.1515/BC.2003.095
    • S. Yan, and B.F. Sloane Molecular regulation of human cathepsin B: implication in pathologies Biol. Chem. 384 2003 845 854 (Pubitemid 36874498)
    • (2003) Biological Chemistry , vol.384 , Issue.6 , pp. 845-854
    • Yan, S.1    Sloane, B.F.2
  • 125
    • 0642339104 scopus 로고    scopus 로고
    • Cell-surface cathepsin B: Understanding its functional significance
    • PII S0070215303540133
    • D. Cavallo-Medved, and B.F. Sloane Cell-surface cathepsin B: understanding its functional significance Curr. Top. Dev. Biol. 54 2003 313 341 (Pubitemid 137639473)
    • (2003) Current Topics in Developmental Biology , vol.54 , pp. 313-341
    • Cavallo-Medved, D.1    Sloane, B.F.2
  • 126
    • 1542495341 scopus 로고    scopus 로고
    • Cathepsin B and its role(s) in cancer progression
    • I. Podgorski, and B.F. Sloane Cathepsin B and its role(s) in cancer progression Biochem. Soc. Symp. 2003 263 276 (Pubitemid 38497232)
    • (2003) Biochemical Society Symposium , Issue.70 , pp. 263-276
    • Podgorski, I.1    Sloane, B.F.2
  • 127
    • 57549090060 scopus 로고    scopus 로고
    • Visualizing protease activity in living cells: From two dimensions to four dimensions
    • 20.21-15
    • C. Jedeszko, M. Sameni, M.B. Olive, K. Moin, and B.F. Sloane Visualizing protease activity in living cells: from two dimensions to four dimensions Curr. Protoc. Cell Biol. 39 2008 20.21-15
    • (2008) Curr. Protoc. Cell Biol. , vol.39
    • Jedeszko, C.1    Sameni, M.2    Olive, M.B.3    Moin, K.4    Sloane, B.F.5
  • 128
    • 0034930565 scopus 로고    scopus 로고
    • Imaging proteolysis by living human glioma cells
    • DOI 10.1515/BC.2001.094
    • M. Sameni, J. Dosescu, and B.F. Sloane Imaging proteolysis by living human glioma cells Biol. Chem. 382 2001 785 788 (Pubitemid 32631715)
    • (2001) Biological Chemistry , vol.382 , Issue.5 , pp. 785-788
    • Sameni, M.1    Dosescu, J.2    Sloane, B.F.3
  • 129
    • 0242577116 scopus 로고    scopus 로고
    • Functional imaging of proteolysis: Stromal and inflammatory cells increase tumor proteolysis
    • M. Sameni, J. Dosescu, K. Moin, and B.F. Sloane Functional imaging of proteolysis: stromal and inflammatory cells increase tumor proteolysis Mol. Imaging 2 2003 159 175
    • (2003) Mol. Imaging , vol.2 , pp. 159-175
    • Sameni, M.1    Dosescu, J.2    Moin, K.3    Sloane, B.F.4
  • 131
    • 0035902141 scopus 로고    scopus 로고
    • The microenvironment of the tumour-host interface
    • L.A. Liotta, and E.C. Kohn The microenvironment of the tumour-host interface Nature 411 2001 375 379
    • (2001) Nature , vol.411 , pp. 375-379
    • Liotta, L.A.1    Kohn, E.C.2
  • 132
    • 0034123653 scopus 로고    scopus 로고
    • Interactions between tumour cells and stromal cells and proteolytic modification of the extracellular matrix by metalloproteinases in cancer
    • Y.A. DeClerck Interactions between tumour cells and stromal cells and proteolytic modification of the extracellular matrix by metalloproteinases in cancer Eur. J. Cancer 36 2000 1258 1268
    • (2000) Eur. J. Cancer , vol.36 , pp. 1258-1268
    • Declerck, Y.A.1
  • 133
    • 0031719897 scopus 로고    scopus 로고
    • Cancer invasion and tissue remodeling: Common themes in proteolytic matrix degradation
    • DOI 10.1016/S0955-0674(98)80044-6
    • M. Johnsen, L.R. Lund, J. Romer, K. Almholt, and K. Dano Cancer invasion and tissue remodeling: common themes in proteolytic matrix degradation Curr. Opin. Cell Biol. 10 1998 667 671 (Pubitemid 28477027)
    • (1998) Current Opinion in Cell Biology , vol.10 , Issue.5 , pp. 667-671
    • Johnsen, M.1    Lund, L.R.2    Romer, J.3    Almholt, K.4    Dano, K.5
  • 134
    • 0037180757 scopus 로고    scopus 로고
    • Inflammation and cancer
    • DOI 10.1038/nature01322
    • L.M. Coussens, and Z. Werb Inflammation and cancer Nature 420 2002 860 867 (Pubitemid 36019639)
    • (2002) Nature , vol.420 , Issue.6917 , pp. 860-867
    • Coussens, L.M.1    Werb, Z.2
  • 135
    • 0242456170 scopus 로고    scopus 로고
    • Axis of evil: Molecular mechanisms of cancer metastasis
    • T. Bogenrieder, and M. Herlyn Axis of evil: molecular mechanisms of cancer metastasis Oncogene 22 2003 6524 6536 (Pubitemid 37372332)
    • (2003) Oncogene , vol.22 , Issue.43 , pp. 6524-6536
    • Bogenrieder, T.1    Herlyn, M.2
  • 136
    • 0036781709 scopus 로고    scopus 로고
    • MMP9 potentiates pulmonary metastasis formation
    • DOI 10.1016/S1535-6108(02)00157-5
    • L.C. van Kempen, and L.M. Coussens MMP9 potentiates pulmonary metastasis formation Cancer Cell 2 2002 251 252 (Pubitemid 41043957)
    • (2002) Cancer Cell , vol.2 , Issue.4 , pp. 251-252
    • Van Kempen, L.C.L.1    Coussens, L.M.2
  • 140
    • 0035911221 scopus 로고    scopus 로고
    • Colony-stimulating factor 1 promotes progression of mammary tumors to malignancy
    • E.Y. Lin, A.V. Nguyen, R.G. Russell, and J.W. Pollard Colony-stimulating factor 1 promotes progression of mammary tumors to malignancy J. Exp. Med. 193 2001 727 740
    • (2001) J. Exp. Med. , vol.193 , pp. 727-740
    • Lin, E.Y.1    Nguyen, A.V.2    Russell, R.G.3    Pollard, J.W.4
  • 141
    • 0036038593 scopus 로고    scopus 로고
    • Requirement of macrophages and eosinophils and their cytokines/chemokines for mammary gland development
    • DOI 10.1186/bcr441
    • V. Gouon-Evans, E.Y. Lin, and J.W. Pollard Requirement of macrophages and eosinophils and their cytokines/chemokines for mammary gland development Breast Cancer Res. 4 2002 155 164 (Pubitemid 35012324)
    • (2002) Breast Cancer Research , vol.4 , Issue.4 , pp. 155-164
    • Gouon-Evans, V.1    Lin, E.Y.2    Pollard, J.W.3
  • 142
    • 0036082948 scopus 로고    scopus 로고
    • Colony stimulating factor-1 is required to recruit macrophages into the mammary gland to facilitate mammary ductal outgrowth
    • DOI 10.1006/dbio.2002.0669
    • A. Van Nguyen, and J.W. Pollard Colony stimulating factor-1 is required to recruit macrophages into the mammary gland to facilitate mammary ductal outgrowth Dev. Biol. 247 2002 11 25 (Pubitemid 34681162)
    • (2002) Developmental Biology , vol.247 , Issue.1 , pp. 11-25
    • Van Nguyen, A.1    Pollard, J.W.2
  • 143
    • 1042292614 scopus 로고    scopus 로고
    • Regulation of mammary gland branching morphogenesis by the extracellular matrix and its remodeling enzymes
    • J.E. Fata, Z. Werb, and M.J. Bissell Regulation of mammary gland branching morphogenesis by the extracellular matrix and its remodeling enzymes Breast Cancer Res. 6 2004 1 11 (Pubitemid 38195555)
    • (2004) Breast Cancer Research , vol.6 , Issue.1 , pp. 1-11
    • Fata, J.E.1    Werb, Z.2    Bissell, M.J.3
  • 144
    • 0037484174 scopus 로고    scopus 로고
    • Modelling tissue-specific signaling and organ function in three dimensions
    • DOI 10.1242/jcs.00503
    • K.L. Schmeichel, and M.J. Bissell Modeling tissue-specific signaling and organ function in three dimensions J. Cell Sci. 116 2003 2377 2388 (Pubitemid 36790120)
    • (2003) Journal of Cell Science , vol.116 , Issue.12 , pp. 2377-2388
    • Schmeichel, K.L.1    Bissell, M.J.2
  • 145
    • 0037603113 scopus 로고    scopus 로고
    • Morphogenesis and oncogenesis of MCF-10A mammary epithelial acini grown in three-dimensional basement membrane cultures
    • DOI 10.1016/S1046-2023(03)00032-X
    • J. Debnath, S.K. Muthuswamy, and J.S. Brugge Morphogenesis and oncogenesis of MCF-10A mammary epithelial acini grown in three-dimensional basement membrane cultures Methods 30 2003 256 268 (Pubitemid 36677560)
    • (2003) Methods , vol.30 , Issue.3 , pp. 256-268
    • Debnath, J.1    Muthuswamy, S.K.2    Brugge, J.S.3
  • 146
    • 25444443688 scopus 로고    scopus 로고
    • Modelling glandular epithelial cancers in three-dimensional cultures
    • DOI 10.1038/nrc1695, PII N1695
    • J. Debnath, and J.S. Brugge Modelling glandular epithelial cancers in three-dimensional cultures Nat. Rev. Cancer 5 2005 675 688 (Pubitemid 41486361)
    • (2005) Nature Reviews Cancer , vol.5 , Issue.9 , pp. 675-688
    • Debnath, J.1    Brugge, J.S.2
  • 149
    • 0030044330 scopus 로고    scopus 로고
    • MCF10AT: A model for the evolution of cancer from proliferative breast disease
    • P.J. Dawson, S.R. Wolman, L. Tait, G.H. Heppner, and F.R. Miller MCF10AT: a model for the evolution of cancer from proliferative breast disease Am. J. Pathol. 148 1996 313 319
    • (1996) Am. J. Pathol. , vol.148 , pp. 313-319
    • Dawson, P.J.1    Wolman, S.R.2    Tait, L.3    Heppner, G.H.4    Miller, F.R.5
  • 150
    • 0034686626 scopus 로고    scopus 로고
    • MCF10DCIS.com xenograft model of human comedo ductal carcinoma in situ
    • F.R. Miller, S.J. Santner, L. Tait, and P.J. Dawson MCF10DCIS.com xenograft model of human comedo ductal carcinoma in situ J. Natl. Cancer Inst. 92 2000 1185 1186
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 1185-1186
    • Miller, F.R.1    Santner, S.J.2    Tait, L.3    Dawson, P.J.4
  • 151
    • 0034458577 scopus 로고    scopus 로고
    • Xenograft models of premalignant breast disease
    • DOI 10.1023/A:1009577811584
    • F.R. Miller Xenograft models of premalignant breast disease J. Mammary Gland Biol. Neoplasia 5 2000 379 391 (Pubitemid 32236769)
    • (2000) Journal of Mammary Gland Biology and Neoplasia , vol.5 , Issue.4 , pp. 379-391
    • Miller, F.R.1
  • 153
    • 0037020196 scopus 로고    scopus 로고
    • The role of apoptosis in creating and maintaining luminal space within normal and oncogene-expressing mammary acini
    • J. Debnath, K.R. Mills, N.L. Collins, M.J. Reginato, S.K. Muthuswamy, and J.S. Brugge The role of apoptosis in creating and maintaining luminal space within normal and oncogene-expressing mammary acini Cell 111 2002 29 40
    • (2002) Cell , vol.111 , pp. 29-40
    • Debnath, J.1    Mills, K.R.2    Collins, N.L.3    Reginato, M.J.4    Muthuswamy, S.K.5    Brugge, J.S.6
  • 154
    • 41649085584 scopus 로고    scopus 로고
    • P21-Activated kinase 1 coordinates aberrant cell survival and pericellular proteolysis in a three-dimensional culture model for premalignant progression of human breast cancer
    • Q. Li, S.R. Mullins, B.F. Sloane, and R.R. Mattingly p21-Activated kinase 1 coordinates aberrant cell survival and pericellular proteolysis in a three-dimensional culture model for premalignant progression of human breast cancer Neoplasia 10 2008 314 329
    • (2008) Neoplasia , vol.10 , pp. 314-329
    • Li, Q.1    Mullins, S.R.2    Sloane, B.F.3    Mattingly, R.R.4
  • 155
    • 0035835829 scopus 로고    scopus 로고
    • Heterotypic signaling between epithelial tumor cells and fibroblasts in carcinoma formation
    • DOI 10.1006/excr.2000.5133
    • B. Elenbaas, and R.A. Weinberg Heterotypic signaling between epithelial tumor cells and fibroblasts in carcinoma formation Exp. Cell Res. 264 2001 169 184 (Pubitemid 32989090)
    • (2001) Experimental Cell Research , vol.264 , Issue.1 , pp. 169-184
    • Elenbaas, B.1    Weinberg, R.A.2
  • 156
    • 0035999132 scopus 로고    scopus 로고
    • The dominance of the microenvironment in breast and ovarian cancer
    • DOI 10.1006/scbi.2001.0417
    • C.D. Roskelley, and M.J. Bissell The dominance of the microenvironment in breast and ovarian cancer Semin. Cancer Biol. 12 2002 97 104 (Pubitemid 34680738)
    • (2002) Seminars in Cancer Biology , vol.12 , Issue.2 , pp. 97-104
    • Roskelley, C.D.1    Bissell, M.J.2
  • 157
    • 0037052448 scopus 로고    scopus 로고
    • Development: Stromal effects on mammary gland development and breast cancer
    • DOI 10.1126/science.1067431
    • B.S. Wiseman, and Z. Werb Stromal effects on mammary gland development and breast cancer Science 296 2002 1046 1049 (Pubitemid 34517108)
    • (2002) Science , vol.296 , Issue.5570 , pp. 1046-1049
    • Wiseman, B.S.1    Werb, Z.2
  • 158
    • 0037312899 scopus 로고    scopus 로고
    • The not-so innocent bystander: The microenvironment as a therapeutic target in cancer
    • DOI 10.1517/14728222.7.1.71
    • A.C. Erickson, and M.H. Barcellos-Hoff The not-so innocent bystander: the microenvironment as a therapeutic target in cancer Expert Opin. Ther. Targets 7 2003 71 88 (Pubitemid 36204590)
    • (2003) Expert Opinion on Therapeutic Targets , vol.7 , Issue.1 , pp. 71-88
    • Erickson, A.C.1    Barcellos-Hoff, M.H.2
  • 159
    • 0038066574 scopus 로고    scopus 로고
    • Host microenvironment in breast cancer development. Inflammatory cells, cytokines and chemokines in breast cancer progression: Reciprocal tumor-microenvironment interactions
    • DOI 10.1186/bcr554
    • A. Ben-Baruch Host microenvironment in breast cancer development: inflammatory cells, cytokines and chemokines in breast cancer progression: reciprocal tumor-microenvironment interactions Breast Cancer Res. 5 2003 31 36 (Pubitemid 36553576)
    • (2003) Breast Cancer Research , vol.5 , Issue.1 , pp. 31-36
    • Ben-Baruch, A.1
  • 160
    • 0037277319 scopus 로고    scopus 로고
    • Breast cancer-induced angiogenesis: Multiple mechanisms and the role of the microenvironment
    • DOI 10.1186/bcr589
    • N. Boudreau, and C. Myers Breast cancer-induced angiogenesis: multiple mechanisms and the role of the microenvironment Breast Cancer Res. 5 2003 140 146 (Pubitemid 36519407)
    • (2003) Breast Cancer Research , vol.5 , Issue.3 , pp. 140-146
    • Boudreau, N.1    Myers, C.2
  • 161
    • 33747095513 scopus 로고    scopus 로고
    • Do myoepithelial cells hold the key for breast tumor progression?
    • K. Polyak, and M. Hu Do myoepithelial cells hold the key for breast tumor progression? J. Mammary Gland Biol. Neoplasia 10 2005 231 247
    • (2005) J. Mammary Gland Biol. Neoplasia , vol.10 , pp. 231-247
    • Polyak, K.1    Hu, M.2
  • 162
    • 31044433663 scopus 로고    scopus 로고
    • Macrophages: Obligate partners for tumor cell migration, invasion, and metastasis
    • DOI 10.1016/j.cell.2006.01.007, PII S0092867406000559
    • J. Condeelis, and J.W. Pollard Macrophages: obligate partners for tumor cell migration, invasion, and metastasis Cell 124 2006 263 266 (Pubitemid 43121975)
    • (2006) Cell , vol.124 , Issue.2 , pp. 263-266
    • Condeelis, J.1    Pollard, J.W.2
  • 163
    • 31544441610 scopus 로고    scopus 로고
    • Distinct role of macrophages in different tumor microenvironments
    • DOI 10.1158/0008-5472.CAN-05-4005
    • C.E. Lewis, and J.W. Pollard Distinct role of macrophages in different tumor microenvironments Cancer Res. 66 2006 605 612 (Pubitemid 43165918)
    • (2006) Cancer Research , vol.66 , Issue.2 , pp. 605-612
    • Lewis, C.E.1    Pollard, J.W.2
  • 164
    • 23744515305 scopus 로고    scopus 로고
    • Modeling dynamic reciprocity: Engineering three-dimensional culture models of breast architecture, function, and neoplastic transformation
    • DOI 10.1016/j.semcancer.2005.05.001, PII S1044579X05000283
    • C.M. Nelson, and M.J. Bissell Modeling dynamic reciprocity: engineering three-dimensional culture models of breast architecture, function, and neoplastic transformation Semin. Cancer Biol. 15 2005 342 352 (Pubitemid 41140304)
    • (2005) Seminars in Cancer Biology , vol.15 , Issue.5 SPEC. ISS. , pp. 342-352
    • Nelson, C.M.1    Bissell, M.J.2
  • 165
    • 1542375858 scopus 로고    scopus 로고
    • Multistep tumorigenesis and the microenvironment
    • P. Schedin, and A. Elias Multistep tumorigenesis and the microenvironment Breast Cancer Res. 6 2004 93 101
    • (2004) Breast Cancer Res. , vol.6 , pp. 93-101
    • Schedin, P.1    Elias, A.2
  • 166
    • 0037276432 scopus 로고    scopus 로고
    • Extracellular matrix-stromal cell contribution to neoplastic phenotype of epithelial cells in the breast
    • DOI 10.1186/bcr580
    • M.P. Shekhar, R. Pauley, and G. Heppner Host microenvironment in breast cancer development: extracellular matrix-stromal cell contribution to neoplastic phenotype of epithelial cells in the breast Breast Cancer Res. 5 2003 130 135 (Pubitemid 36519405)
    • (2003) Breast Cancer Research , vol.5 , Issue.3 , pp. 130-135
    • Shekhar, M.P.V.1    Pauley, R.2    Heppner, G.3
  • 167
    • 0038700554 scopus 로고    scopus 로고
    • Epithelia-mesenchymal transition in breast cancer development
    • DOI 10.1186/bcr578
    • A. Vincent-Salomon, and J.P. Thiery Host microenvironment in breast cancer development: epithelial-mesenchymal transition in breast cancer development Breast Cancer Res. 5 2003 101 106 (Pubitemid 36348104)
    • (2003) Breast Cancer Research , vol.5 , Issue.2 , pp. 101-106
    • Vincent-Salomon, A.1    Thiery, J.P.2
  • 168
    • 0037686184 scopus 로고    scopus 로고
    • Inflammatory and immune cells in tumour angiogenesis and arteriogenesis
    • DOI 10.1186/bcr573
    • J.L. Yu, and J.W. Rak Host microenvironment in breast cancer development: inflammatory and immune cells in tumour angiogenesis and arteriogenesis Breast Cancer Res. 5 2003 83 88 (Pubitemid 36348101)
    • (2003) Breast Cancer Research , vol.5 , Issue.2 , pp. 83-88
    • Yu, J.L.1    Rak, J.W.2
  • 169
    • 27144506171 scopus 로고    scopus 로고
    • Ets2-dependent microenvironmental support of mouse mammary tumors
    • DOI 10.1038/sj.onc.1208856, PII 1208856
    • J.A. Tynan, F. Wen, W.J. Muller, and R.G. Oshima Ets2-dependent microenvironmental support of mouse mammary tumors Oncogene 24 2005 6870 6876 (Pubitemid 41509410)
    • (2005) Oncogene , vol.24 , Issue.46 , pp. 6870-6876
    • Tynan, J.A.1    Wen, F.2    Muller, W.J.3    Oshima, R.G.4
  • 172
    • 0842320021 scopus 로고    scopus 로고
    • Cell fusion: A hidden enemy?
    • DOI 10.1016/S1535-6108(03)00114-4, PII S1535610803001144
    • D. Duelli, and Y. Lazebnik Cell fusion: a hidden enemy? Cancer Cell 3 2003 445 448 (Pubitemid 38340291)
    • (2003) Cancer Cell , vol.3 , Issue.5 , pp. 445-448
    • Duelli, D.1    Lazebnik, Y.2
  • 174
    • 34147191467 scopus 로고    scopus 로고
    • Stromal cells associated with early invasive foci in human mammary ductal carcinoma in situ coexpress urokinase and urokinase receptor
    • DOI 10.1002/ijc.22340
    • B.S. Nielsen, F. Rank, M. Illemann, L.R. Lund, and K. Dano Stromal cells associated with early invasive foci in human mammary ductal carcinoma in situ coexpress urokinase and urokinase receptor Int. J. Cancer 120 2007 2086 2095 (Pubitemid 46555845)
    • (2007) International Journal of Cancer , vol.120 , Issue.10 , pp. 2086-2095
    • Nielsen, B.S.1    Rank, F.2    Illemann, M.3    Lund, L.R.4    Dano, K.5
  • 175
    • 71549136169 scopus 로고    scopus 로고
    • Fibroblast hepatocyte growth factor promotes invasion of human mammary ductal carcinoma in situ
    • C. Jedeszko, B.C. Victor, I. Podgorski, and B.F. Sloane Fibroblast hepatocyte growth factor promotes invasion of human mammary ductal carcinoma in situ Cancer Res. 69 2009 9148 9155
    • (2009) Cancer Res. , vol.69 , pp. 9148-9155
    • Jedeszko, C.1    Victor, B.C.2    Podgorski, I.3    Sloane, B.F.4
  • 176
    • 3042692979 scopus 로고    scopus 로고
    • + exchanger (NHE1) creates acidic microenvironments leading to hyaluronidase-2 and cathepsin B activation and breast tumor cell invasion
    • DOI 10.1074/jbc.M311838200
    • L.Y. Bourguignon, P.A. Singleton, F. Diedrich, R. Stern, and E. Gilad CD44 interaction with Na + - H + exchanger (NHE1) creates acidic microenvironments leading to hyaluronidase-2 and cathepsin B activation and breast tumor cell invasion J. Biol. Chem. 279 2004 26991 27007 (Pubitemid 38812535)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.26 , pp. 26991-27007
    • Bourguignon, L.Y.W.1    Singleton, P.A.2    Diedrich, F.3    Stern, R.4    Gilad, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.