메뉴 건너뛰기




Volumn 87, Issue 3-4 SPEC. ISS., 2005, Pages 315-320

Functional imaging of pericellular proteolysis in cancer cell invasion

Author keywords

Collagen fragments; Collagen type I; Collagenases; Protease activity; Quenched and dequenched FITC

Indexed keywords

FLUORESCEIN ISOTHIOCYANATE; LAMININ; MATRIX METALLOPROTEINASE;

EID: 15244351837     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biochi.2004.10.016     Document Type: Article
Times cited : (52)

References (30)
  • 1
    • 0030136756 scopus 로고    scopus 로고
    • Dynamics of matrix turnover during pathologic remodeling of the extracellular matrix
    • W.G. Stetler-Stevenson, M.L. Corcoran, and D.E. Kleiner Jr. Dynamics of matrix turnover during pathologic remodeling of the extracellular matrix Am. J. Pathol. 148 1996 1345 1350
    • (1996) Am. J. Pathol. , vol.148 , pp. 1345-1350
    • Stetler-Stevenson, W.G.1    Corcoran, M.L.2    Kleiner Jr., D.E.3
  • 2
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • M.D. Sternlicht, and Z. Werb How matrix metalloproteinases regulate cell behavior Annu. Rev. Cell Dev. Biol. 17 2001 463 516
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 3
    • 0031985228 scopus 로고    scopus 로고
    • The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study
    • G.S. Butler, M.J. Butler, S.J. Atkinson, H. Will, T. Tamura, and S.S. Van:Westrum The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study J. Biol. Chem. 273 1998 871 880
    • (1998) J. Biol. Chem. , vol.273 , pp. 871-880
    • Butler, G.S.1    Butler, M.J.2    Atkinson, S.J.3    Will, H.4    Tamura, T.5    Van6    Westrum, S.S.7
  • 4
    • 0034697144 scopus 로고    scopus 로고
    • Binding of active (57:kDa) membrane type 1-matrix metalloproteinase (MT1-MMP) to tissue inhibitor of metalloproteinase (TIMP)-2 regulates MT1-MMP processing and pro-MMP-2 activation
    • S. Hernandez-Barrantes, M. Toth, M.M. Bernardo, M. Yurkova, D.C. Gervasi, and Y. Raz Binding of active (57:kDa) membrane type 1-matrix metalloproteinase (MT1-MMP) to tissue inhibitor of metalloproteinase (TIMP)-2 regulates MT1-MMP processing and pro-MMP-2 activation J. Biol. Chem. 275 2000 12080 12089
    • (2000) J. Biol. Chem. , vol.275 , pp. 12080-12089
    • Hernandez-Barrantes, S.1    Toth, M.2    Bernardo, M.M.3    Yurkova, M.4    Gervasi, D.C.5    Raz, Y.6
  • 5
    • 0034671857 scopus 로고    scopus 로고
    • Domain interactions in the gelatinase A.TIMP-2.MT1-MMP activation complex. The ectodomain of the 44-kDa form of membrane type-1 matrix metalloproteinase does not modulate gelatinase a activation
    • C.M. Overall, E. Tam, G.A. McQuibban, C. Morrison, U.M. Wallon, and H.F. Bigg Domain interactions in the gelatinase A.TIMP-2.MT1-MMP activation complex. The ectodomain of the 44-kDa form of membrane type-1 matrix metalloproteinase does not modulate gelatinase A activation J. Biol. Chem. 275 2000 39497 39506
    • (2000) J. Biol. Chem. , vol.275 , pp. 39497-39506
    • Overall, C.M.1    Tam, E.2    McQuibban, G.A.3    Morrison, C.4    Wallon, U.M.5    Bigg, H.F.6
  • 6
    • 0028907318 scopus 로고
    • Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease
    • A.Y. Strongin, I. Collier, G. Bannikov, B.L. Marmer, G.A. Grant, and G.I. Goldberg Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease J. Biol. Chem. 270 1995 5331 5338
    • (1995) J. Biol. Chem. , vol.270 , pp. 5331-5338
    • Strongin, A.Y.1    Collier, I.2    Bannikov, G.3    Marmer, B.L.4    Grant, G.A.5    Goldberg, G.I.6
  • 7
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: Trials and tribulations
    • L.M. Coussens, B. Fingleton, and L.M. Matrisian Matrix metalloproteinase inhibitors and cancer: trials and tribulations Science 295 2002 2387 2392
    • (2002) Science , vol.295 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 8
    • 0032834211 scopus 로고    scopus 로고
    • Functional hierarchy of simultaneously expressed adhesion receptors: Integrin alpha2beta1 but not CD44 mediates MV3 melanoma cell migration and matrix reorganization within three-dimensional hyaluronan-containing collagen matrices
    • K. Maaser, K. Wolf, C.E. Klein, B. Niggemann, K.S. Zanker, and E.B. Brocker Functional hierarchy of simultaneously expressed adhesion receptors: integrin alpha2beta1 but not CD44 mediates MV3 melanoma cell migration and matrix reorganization within three-dimensional hyaluronan-containing collagen matrices Mol. Biol. Cell 10 1999 3067 3079
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3067-3079
    • Maaser, K.1    Wolf, K.2    Klein, C.E.3    Niggemann, B.4    Zanker, K.S.5    Brocker, E.B.6
  • 9
    • 0030913972 scopus 로고    scopus 로고
    • Migration of highly aggressive MV3 melanoma cells in 3-dimensional collagen lattices results in local matrix reorganization and shedding of alpha2 and beta1 integrins and CD44
    • P. Friedl, K. Maaser, C.E. Klein, B. Niggemann, G. Krohne, and K.S. Zanker Migration of highly aggressive MV3 melanoma cells in 3-dimensional collagen lattices results in local matrix reorganization and shedding of alpha2 and beta1 integrins and CD44 Cancer Res. 57 1997 2061 2070
    • (1997) Cancer Res. , vol.57 , pp. 2061-2070
    • Friedl, P.1    Maaser, K.2    Klein, C.E.3    Niggemann, B.4    Krohne, G.5    Zanker, K.S.6
  • 10
    • 0037064041 scopus 로고    scopus 로고
    • Collagen binding properties of the membrane type-1 matrix metalloproteinase (MT1-MMP) hemopexin C domain. The ectodomain of the 44-kDa autocatalytic product of MT1-MMP inhibits cell invasion by disrupting native type I collagen cleavage
    • E.M. Tam, Y.I. Wu, G.S. Butler, M.S. Stack, and C.M. Overall Collagen binding properties of the membrane type-1 matrix metalloproteinase (MT1-MMP) hemopexin C domain. The ectodomain of the 44-kDa autocatalytic product of MT1-MMP inhibits cell invasion by disrupting native type I collagen cleavage J. Biol. Chem. 277 2002 39005 39014
    • (2002) J. Biol. Chem. , vol.277 , pp. 39005-39014
    • Tam, E.M.1    Wu, Y.I.2    Butler, G.S.3    Stack, M.S.4    Overall, C.M.5
  • 11
    • 0030827411 scopus 로고    scopus 로고
    • Tumor cell invasion through matrigel is regulated by activated matrix metalloproteinase-2
    • E.I. Deryugina, G.X. Luo, R.A. Reisfeld, M.A. Bourdon, and A. Strongin Tumor cell invasion through matrigel is regulated by activated matrix metalloproteinase-2 Anticancer Res. 17 1997 3201 3210
    • (1997) Anticancer Res. , vol.17 , pp. 3201-3210
    • Deryugina, E.I.1    Luo, G.X.2    Reisfeld, R.A.3    Bourdon, M.A.4    Strongin, A.5
  • 12
    • 0001125655 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 activation modulates glioma cell migration. Enhanced cleavage of type II collagen by collagenases in osteoarthritic articular cartilage
    • E.I. Deryugina, M.A. Bourdon, G.X. Luo, R.A. Reisfeld, A. Strongin, and R.C. Billinghurst Matrix metalloproteinase-2 activation modulates glioma cell migration. Enhanced cleavage of type II collagen by collagenases in osteoarthritic articular cartilage J. Cell Sci. 110 Pt 19 1997 2473 2482
    • (1997) J. Cell Sci. , vol.110 , Issue.19 PART , pp. 2473-2482
    • Deryugina, E.I.1    Bourdon, M.A.2    Luo, G.X.3    Reisfeld, R.A.4    Strongin, A.5    Billinghurst, R.C.6
  • 15
    • 0142245603 scopus 로고    scopus 로고
    • Amoeboid shape change and contact guidance: T-lymphocyte crawling through fibrillar collagen is independent of matrix remodeling by MMPs and other proteases
    • K. Wolf, R. Muller, S. Borgmann, E.B. Brocker, and P. Friedl Amoeboid shape change and contact guidance: T-lymphocyte crawling through fibrillar collagen is independent of matrix remodeling by MMPs and other proteases Blood 102 2003 3262 3269
    • (2003) Blood , vol.102 , pp. 3262-3269
    • Wolf, K.1    Muller, R.2    Borgmann, S.3    Brocker, E.B.4    Friedl, P.5
  • 17
    • 0036262509 scopus 로고    scopus 로고
    • Identification of activated matrix metalloproteinase-2 (MMP-2) as the main gelatinolytic enzyme in malignant melanoma by in situ zymography
    • P. Kurschat, C. Wickenhauser, W. Groth, T. Krieg, and C. Mauch Identification of activated matrix metalloproteinase-2 (MMP-2) as the main gelatinolytic enzyme in malignant melanoma by in situ zymography J. Pathol 197 2002 179 187
    • (2002) J. Pathol , vol.197 , pp. 179-187
    • Kurschat, P.1    Wickenhauser, C.2    Groth, W.3    Krieg, T.4    Mauch, C.5
  • 19
    • 1842856332 scopus 로고    scopus 로고
    • Following matrix metalloproteinases activity near the cell boundary by infrared micro-spectroscopy
    • S. Federman, L.M. Miller, and I. Sagi Following matrix metalloproteinases activity near the cell boundary by infrared micro-spectroscopy Matrix Biol. 21 2002 567 577
    • (2002) Matrix Biol. , vol.21 , pp. 567-577
    • Federman, S.1    Miller, L.M.2    Sagi, I.3
  • 20
    • 2442505682 scopus 로고    scopus 로고
    • Pericellular proteolysis by leukocytes and tumor cells on substrates: Focal activation and the role of urokinase-type plasminogen activator, Histochem
    • A.L. Kindzelskii, I. Amhad, D. Keller, M.J. Zhou, R.P. Haugland, B.A. Garni-Wagner, M.R. Gyetko, R.F. Todd III, and H.R. Petty Pericellular proteolysis by leukocytes and tumor cells on substrates: focal activation and the role of urokinase-type plasminogen activator, Histochem Cell Biol. 121 2004 299 310
    • (2004) Cell Biol. , vol.121 , pp. 299-310
    • Kindzelskii, A.L.1    Amhad, I.2    Keller, D.3    Zhou, M.J.4    Haugland, R.P.5    Garni-Wagner, B.A.6    Gyetko, M.R.7    Todd III, R.F.8    Petty, H.R.9
  • 21
    • 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
  • 22
    • 0032951071 scopus 로고    scopus 로고
    • In vivo imaging of tumors with protease-activated near-infrared fluorescent probes
    • R. Weissleder, C.H. Tung, U. Mahmood, and A. Bogdanov Jr. In vivo imaging of tumors with protease-activated near-infrared fluorescent probes Nat. Biotechnol. 17 1999 375 378
    • (1999) Nat. Biotechnol. , vol.17 , pp. 375-378
    • Weissleder, R.1    Tung, C.H.2    Mahmood, U.3    Bogdanov Jr., A.4
  • 23
    • 0344874727 scopus 로고    scopus 로고
    • Molecular imaging of proteolytic activity in cancer
    • J.O. McIntyre, and L.M. Matrisian Molecular imaging of proteolytic activity in cancer J. Cell Biochem. 90 2003 1087 1097
    • (2003) J. Cell Biochem. , vol.90 , pp. 1087-1097
    • McIntyre, J.O.1    Matrisian, L.M.2
  • 24
    • 0037675000 scopus 로고    scopus 로고
    • In situ localization of gelatinolytic activity in the extracellular matrix of metastases of colon cancer in rat liver using quenched fluorogenic DQ-gelatin
    • O.R. Mook, C. Van:Overbeek, E.G. Ackema, F. Van:Maldegem, and W.M. Frederiks In situ localization of gelatinolytic activity in the extracellular matrix of metastases of colon cancer in rat liver using quenched fluorogenic DQ-gelatin J. Histochem. Cytochem. 51 2003 821 829
    • (2003) J. Histochem. Cytochem. , vol.51 , pp. 821-829
    • Mook, O.R.1    Van2    Overbeek, C.3    Ackema, E.G.4    Van5    Maldegem, F.6    Frederiks, W.M.7
  • 25
    • 0038049137 scopus 로고    scopus 로고
    • Tumour-cell invasion and migration: Diversity and escape mechanisms
    • P. Friedl, and K. Wolf Tumour-cell invasion and migration: diversity and escape mechanisms Nat. Rev. Cancer 3 2003 362 374
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 362-374
    • Friedl, P.1    Wolf, K.2
  • 27
    • 15844420283 scopus 로고    scopus 로고
    • Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3
    • P.C. Brooks, S. Stromblad, L.C. Sanders, T.L. Von:Schalscha, R.T. Aimes, and W.G. Stetler-Stevenson Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3 Cell 85 1996 683 693
    • (1996) Cell , vol.85 , pp. 683-693
    • Brooks, P.C.1    Stromblad, S.2    Sanders, L.C.3    Von4    Schalscha, T.L.5    Aimes, R.T.6    Stetler-Stevenson, W.G.7
  • 28
    • 0037064589 scopus 로고    scopus 로고
    • ECM regulates MT1-MMP localization with beta1 or alpha v beta3 integrins at distinct cell compartments modulating its internalization and activity on human endothelial cells
    • B.G. Galvez, S. Matias-Roman, M. Yanez-Mo, F. Sanchez-Madrid, and A.G. Arroyo ECM regulates MT1-MMP localization with beta1 or alpha v beta3 integrins at distinct cell compartments modulating its internalization and activity on human endothelial cells J. Cell Biol. 159 2002 509 521
    • (2002) J. Cell Biol. , vol.159 , pp. 509-521
    • Galvez, B.G.1    Matias-Roman, S.2    Yanez-Mo, M.3    Sanchez-Madrid, F.4    Arroyo, A.G.5
  • 30
    • 0032895321 scopus 로고    scopus 로고
    • U.K. Saarialho-Kere, Expression of collagenases-1 and -3 and their inhibitors TIMP-1 and -3 correlates with the level of invasion in malignant melanomas
    • K. Airola, T. Karonen, M. Vaalamo, K. Lehti, J. Lohi, and A.L. Kariniemi U.K. Saarialho-Kere, Expression of collagenases-1 and -3 and their inhibitors TIMP-1 and -3 correlates with the level of invasion in malignant melanomas Br. J. Cancer 80 1999 733 743
    • (1999) Br. J. Cancer , vol.80 , pp. 733-743
    • Airola, K.1    Karonen, T.2    Vaalamo, M.3    Lehti, K.4    Lohi, J.5    Kariniemi, A.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.