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Volumn 27, Issue 7, 2008, Pages 640-647

Fluorescently tagged laminin subunits facilitate analyses of the properties, assembly and processing of laminins in live and fixed lung epithelial cells and keratinocytes

Author keywords

Epithelial cell; Laminin; Live cell imaging; Matrix

Indexed keywords

ADENOVIRUS VECTOR; LAMININ;

EID: 54249164014     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.matbio.2008.06.003     Document Type: Article
Times cited : (6)

References (42)
  • 3
    • 0030753712 scopus 로고    scopus 로고
    • Laminin-5 and modulation of keratin cytoskeleton arrangement in FG pancreatic carcinoma cells: involvement of IFAP300 and evidence that laminin-5/cell interactions correlate with a dephosphorylation of alpha 6A integrin
    • Baker S.E., Skalli O., Goldman R.D., and Jones J.C. Laminin-5 and modulation of keratin cytoskeleton arrangement in FG pancreatic carcinoma cells: involvement of IFAP300 and evidence that laminin-5/cell interactions correlate with a dephosphorylation of alpha 6A integrin. Cell Motil. Cytoskel. 37 (1997) 271-286
    • (1997) Cell Motil. Cytoskel. , vol.37 , pp. 271-286
    • Baker, S.E.1    Skalli, O.2    Goldman, R.D.3    Jones, J.C.4
  • 4
    • 0030272476 scopus 로고    scopus 로고
    • Hemidesmosomes: role in adhesion, signaling and human diseases
    • Borradori L., and Sonnenberg A. Hemidesmosomes: role in adhesion, signaling and human diseases. Curr. Opin. Cell Biol. 8 (1996) 647-656
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 647-656
    • Borradori, L.1    Sonnenberg, A.2
  • 5
    • 0033519279 scopus 로고    scopus 로고
    • Laminin polymerization induces a receptor-cytoskeleton network
    • Colognato H., Winkelmann D.A., and Yurchenco P.D. Laminin polymerization induces a receptor-cytoskeleton network. J. Cell Biol. 145 (1999) 619-631
    • (1999) J. Cell Biol. , vol.145 , pp. 619-631
    • Colognato, H.1    Winkelmann, D.A.2    Yurchenco, P.D.3
  • 8
    • 0034329439 scopus 로고    scopus 로고
    • Adenovirus-mediated transfer of an Na/K-ATPase beta1 subunit gene improves alveolar fluid clearance and survival in hyperoxic rats
    • Factor P., Dumasius V., Saldias F., Brown L.A.S., and Sznajder J.I. Adenovirus-mediated transfer of an Na/K-ATPase beta1 subunit gene improves alveolar fluid clearance and survival in hyperoxic rats. Hum. Gene Ther. 11 (2000) 2231-2242
    • (2000) Hum. Gene Ther. , vol.11 , pp. 2231-2242
    • Factor, P.1    Dumasius, V.2    Saldias, F.3    Brown, L.A.S.4    Sznajder, J.I.5
  • 9
    • 0032489876 scopus 로고    scopus 로고
    • Processing of laminin-5 and its functional consequences: role of plasmin and tissue-type plasminogen activator
    • Goldfinger L.E., Stack M.S., and Jones J.C.R. Processing of laminin-5 and its functional consequences: role of plasmin and tissue-type plasminogen activator. J. Cell Biol. 141 (1998) 255-265
    • (1998) J. Cell Biol. , vol.141 , pp. 255-265
    • Goldfinger, L.E.1    Stack, M.S.2    Jones, J.C.R.3
  • 10
    • 0032841440 scopus 로고    scopus 로고
    • The α3 laminin subunit, α6β4 and α3β1 integrin coordinately regulate wound healing in cultured epithelial cells and in the skin
    • Goldfinger L.E., Hopkinson S.B., deHart G.W., Collawn S., Couchman J.R., and Jones J.C.R. The α3 laminin subunit, α6β4 and α3β1 integrin coordinately regulate wound healing in cultured epithelial cells and in the skin. J. Cell Sci. 112 (1999) 2615-2629
    • (1999) J. Cell Sci. , vol.112 , pp. 2615-2629
    • Goldfinger, L.E.1    Hopkinson, S.B.2    deHart, G.W.3    Collawn, S.4    Couchman, J.R.5    Jones, J.C.R.6
  • 11
    • 0032893678 scopus 로고    scopus 로고
    • A cell signal pathway involving laminin-5, α3β1 integrin, and mitogen-activated protein kinase can regulate epithelial cell proliferation
    • Gonzales M., Haan K., Baker S.E., Fitchmun M.I., Todorov I., Weitzman S., and Jones J.C.R. A cell signal pathway involving laminin-5, α3β1 integrin, and mitogen-activated protein kinase can regulate epithelial cell proliferation. Mol. Biol. Cell 10 (1999) 259-270
    • (1999) Mol. Biol. Cell , vol.10 , pp. 259-270
    • Gonzales, M.1    Haan, K.2    Baker, S.E.3    Fitchmun, M.I.4    Todorov, I.5    Weitzman, S.6    Jones, J.C.R.7
  • 12
    • 0000747456 scopus 로고
    • Preparation of extracellular matrices produced by cultured bovine corneal endothelial cells and PF-HR-9 endodermal cells: their use in cell culture
    • Alan R. (Ed), Alan R. Liss. Inc., New York
    • Gospodarowicz D.I.E. Preparation of extracellular matrices produced by cultured bovine corneal endothelial cells and PF-HR-9 endodermal cells: their use in cell culture. In: Alan R. (Ed). Methods for Preparation of Media, Supplements, and Substrata for Serum-free Animal Cell Culture (1984), Alan R. Liss. Inc., New York 275-293
    • (1984) Methods for Preparation of Media, Supplements, and Substrata for Serum-free Animal Cell Culture , pp. 275-293
    • Gospodarowicz, D.I.E.1
  • 13
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • Harlow E., and Lane D. Antibodies: A Laboratory Manual (1988), Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 485-510
    • (1988) Antibodies: A Laboratory Manual , pp. 485-510
    • Harlow, E.1    Lane, D.2
  • 14
    • 0034698047 scopus 로고    scopus 로고
    • Structural requirement of carboxyl-terminal globular domains of laminin α3 chain for promotion of rapid cell adhesion and migration by laminin-5
    • Hirosaki T., Mizushima H., Tsubota Y., Moriyama K., and Miyazaki K. Structural requirement of carboxyl-terminal globular domains of laminin α3 chain for promotion of rapid cell adhesion and migration by laminin-5. J. Biol. Chem. 275 (2000) 22495-22502
    • (2000) J. Biol. Chem. , vol.275 , pp. 22495-22502
    • Hirosaki, T.1    Mizushima, H.2    Tsubota, Y.3    Moriyama, K.4    Miyazaki, K.5
  • 15
    • 0348014936 scopus 로고    scopus 로고
    • Quantitative assessment of collagen assembly by live cells
    • Johnson C., and Galis Z.S. Quantitative assessment of collagen assembly by live cells. J. Biomed. Mat. Res. 67A (2003) 775-784
    • (2003) J. Biomed. Mat. Res. , vol.67 A , pp. 775-784
    • Johnson, C.1    Galis, Z.S.2
  • 17
    • 21644486912 scopus 로고    scopus 로고
    • Laminin-6 assembles into multimolecular fibrillar complexes with perlecan and participates in mechano-signal transduction via a dystroglycan-dependent, integrin-independent, mechanism
    • Jones J.C.R., Lane K., Hopkinson S.B., Lecuona E., Geiger R.C., Dean D.A., Correa-Meyer E., Gonzales M., Campbell K., Sznajder J.I., and Budinger S. Laminin-6 assembles into multimolecular fibrillar complexes with perlecan and participates in mechano-signal transduction via a dystroglycan-dependent, integrin-independent, mechanism. J. Cell Sci. 118 (2005) 2557-2565
    • (2005) J. Cell Sci. , vol.118 , pp. 2557-2565
    • Jones, J.C.R.1    Lane, K.2    Hopkinson, S.B.3    Lecuona, E.4    Geiger, R.C.5    Dean, D.A.6    Correa-Meyer, E.7    Gonzales, M.8    Campbell, K.9    Sznajder, J.I.10    Budinger, S.11
  • 18
    • 0024814987 scopus 로고
    • Immunochemical characterization of three components of the hemidesmosome and their expression in cultured epithelial cells
    • Klatte D.H., Kurpakus M.A., Grelling K.A., and Jones J.C.R. Immunochemical characterization of three components of the hemidesmosome and their expression in cultured epithelial cells. J. Cell Biol. 109 (1989) 3377-3390
    • (1989) J. Cell Biol. , vol.109 , pp. 3377-3390
    • Klatte, D.H.1    Kurpakus, M.A.2    Grelling, K.A.3    Jones, J.C.R.4
  • 19
    • 36148996844 scopus 로고    scopus 로고
    • The Slingshot family of phosphatases mediates Rac1 regulation of cofilin phosphorylation, laminin-332 organization and motility behavior of keratinocytes
    • Kligys K., Claiborne J.N., DeBiase P., Hopkinson S.B., Mizuno K., and Jones J.C.R. The Slingshot family of phosphatases mediates Rac1 regulation of cofilin phosphorylation, laminin-332 organization and motility behavior of keratinocytes. J. Biol. Chem. 282 (2007) 32520-32528
    • (2007) J. Biol. Chem. , vol.282 , pp. 32520-32528
    • Kligys, K.1    Claiborne, J.N.2    DeBiase, P.3    Hopkinson, S.B.4    Mizuno, K.5    Jones, J.C.R.6
  • 21
    • 33644665921 scopus 로고    scopus 로고
    • Fluorescently labeled collagen binding proteins allow specific visualization of collagen in tissues and live cell cultures
    • Krahn K.N., Bouten C.V.C., van Tuijl S., Zandvoort M.A.M.J., and Merkx M. Fluorescently labeled collagen binding proteins allow specific visualization of collagen in tissues and live cell cultures. Anal. Biochem. 350 (2006) 177-185
    • (2006) Anal. Biochem. , vol.350 , pp. 177-185
    • Krahn, K.N.1    Bouten, C.V.C.2    van Tuijl, S.3    Zandvoort, M.A.M.J.4    Merkx, M.5
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 277 (1970) 680-685
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0027242415 scopus 로고
    • The matrix secreted by 804G cells contains laminin-related components that participate in hemidesmosome assembly in vitro
    • Langhofer M., Hopkinson S.B., and Jones J.C.R. The matrix secreted by 804G cells contains laminin-related components that participate in hemidesmosome assembly in vitro. J. Cell Sci. 105 (1993) 753-764
    • (1993) J. Cell Sci. , vol.105 , pp. 753-764
    • Langhofer, M.1    Hopkinson, S.B.2    Jones, J.C.R.3
  • 24
    • 33748797944 scopus 로고    scopus 로고
    • Cell and fibronectin dynamics during branching morphogenesis
    • Larsen M., Wei C., and Yamada K.M. Cell and fibronectin dynamics during branching morphogenesis. J. Cell Sci. 119 (2006) 3376-3384
    • (2006) J. Cell Sci. , vol.119 , pp. 3376-3384
    • Larsen, M.1    Wei, C.2    Yamada, K.M.3
  • 25
    • 0022357460 scopus 로고
    • A serum-free method for culturing normal human bronchial epithelial cells at clonal density
    • Lechner J.F., and LaVeck M.A. A serum-free method for culturing normal human bronchial epithelial cells at clonal density. J. Tissue Culture Methods 9 (1985) 43-48
    • (1985) J. Tissue Culture Methods , vol.9 , pp. 43-48
    • Lechner, J.F.1    LaVeck, M.A.2
  • 26
    • 0037166935 scopus 로고    scopus 로고
    • Matrix assembly, regulation, and survival functions of laminin and its receptors in embryonic stem cell differentiation
    • Li S., Harrison D., Carbonetto S., Fässler R., Smyth N., Edgar D., and Yurchenco P.D. Matrix assembly, regulation, and survival functions of laminin and its receptors in embryonic stem cell differentiation. J. Cell Biol. 157 (2002) 1279-1290
    • (2002) J. Cell Biol. , vol.157 , pp. 1279-1290
    • Li, S.1    Harrison, D.2    Carbonetto, S.3    Fässler, R.4    Smyth, N.5    Edgar, D.6    Yurchenco, P.D.7
  • 27
    • 0026640262 scopus 로고
    • The anchoring filament protein kalinin is synthesized and secreted as a high molecular weight precursor
    • Marinkovich M.P., Lunstrum G.P., and Burgeson R.E. The anchoring filament protein kalinin is synthesized and secreted as a high molecular weight precursor. J. Biol. Chem. 267 (1992) 17900-17906
    • (1992) J. Biol. Chem. , vol.267 , pp. 17900-17906
    • Marinkovich, M.P.1    Lunstrum, G.P.2    Burgeson, R.E.3
  • 30
    • 0030930419 scopus 로고    scopus 로고
    • Identification of integrin-dependent and -independent cell adhesion domains in COOH-terminal globular region of laminin-5 α3 chain
    • Mizushima H., Takamura H., Miyagi Y., Kikkawa Y., Yamanaka N., Yasumitsu H., Misugi K., and Miyazaki K. Identification of integrin-dependent and -independent cell adhesion domains in COOH-terminal globular region of laminin-5 α3 chain. Cell Growth Differ. 8 (1997) 979-987
    • (1997) Cell Growth Differ. , vol.8 , pp. 979-987
    • Mizushima, H.1    Takamura, H.2    Miyagi, Y.3    Kikkawa, Y.4    Yamanaka, N.5    Yasumitsu, H.6    Misugi, K.7    Miyazaki, K.8
  • 31
    • 0035941357 scopus 로고    scopus 로고
    • Ligation of integrin α3β1 by laminin 5 at the wound edge activates Rho-dependent adhesion of leading keratinocytes on collagen
    • Nguyen B.P., Ren X.-D., Schwartz M.A., and Carter W.G. Ligation of integrin α3β1 by laminin 5 at the wound edge activates Rho-dependent adhesion of leading keratinocytes on collagen. J. Biol. Chem. 276 (2000) 43860-43870
    • (2000) J. Biol. Chem. , vol.276 , pp. 43860-43870
    • Nguyen, B.P.1    Ren, X.-D.2    Schwartz, M.A.3    Carter, W.G.4
  • 32
    • 0037087773 scopus 로고    scopus 로고
    • Dual labeling of the fibronectin matrix and actin cytoskeleton with green fluorescent protein variants
    • Ohashi T., Kiehart D.P., and Erickson H.P. Dual labeling of the fibronectin matrix and actin cytoskeleton with green fluorescent protein variants. J. Cell Sci. 115 (2002) 1221-1229
    • (2002) J. Cell Sci. , vol.115 , pp. 1221-1229
    • Ohashi, T.1    Kiehart, D.P.2    Erickson, H.P.3
  • 35
    • 33646817397 scopus 로고    scopus 로고
    • New insights into extracellular matrix assembly and reorganization from dynamic imaging of extracellular matrix proteins in living osteoblasts
    • Sivakumar P., Czirok A., Rongsih B.J., Divakara V.P., Wang Y., and Dallas S.L. New insights into extracellular matrix assembly and reorganization from dynamic imaging of extracellular matrix proteins in living osteoblasts. J. Cell. Sci. 119 (2005) 1350-1360
    • (2005) J. Cell. Sci. , vol.119 , pp. 1350-1360
    • Sivakumar, P.1    Czirok, A.2    Rongsih, B.J.3    Divakara, V.P.4    Wang, Y.5    Dallas, S.L.6
  • 37
    • 17644420066 scopus 로고    scopus 로고
    • Regulation of biological activity and matrix assembly of laminin-5 by COOH-terminal, LG4-5 domain of α3 chain
    • Tsubota Y., Yasuda C., Kariya Y., Ogawa T., Hirosaki T., Mizushima H., and Miyazaki K. Regulation of biological activity and matrix assembly of laminin-5 by COOH-terminal, LG4-5 domain of α3 chain. J. Biol. Chem. 280 (2005) 14370-14377
    • (2005) J. Biol. Chem. , vol.280 , pp. 14370-14377
    • Tsubota, Y.1    Yasuda, C.2    Kariya, Y.3    Ogawa, T.4    Hirosaki, T.5    Mizushima, H.6    Miyazaki, K.7
  • 38
    • 0038713422 scopus 로고    scopus 로고
    • Membrane type-1-matrix metalloproteinase expressed by prostate carcinoma cells cleaves human laminin-5 beta3 chain and induces cell migration
    • Udayakumar T.S., Chen M.L., Bair E.L., Von Bredow D.C., Cress A.E., Nagle R.B., and Bowden G.T. Membrane type-1-matrix metalloproteinase expressed by prostate carcinoma cells cleaves human laminin-5 beta3 chain and induces cell migration. Cancer Res. 63 (2003) 2292-2299
    • (2003) Cancer Res. , vol.63 , pp. 2292-2299
    • Udayakumar, T.S.1    Chen, M.L.2    Bair, E.L.3    Von Bredow, D.C.4    Cress, A.E.5    Nagle, R.B.6    Bowden, G.T.7
  • 39
    • 0035800814 scopus 로고    scopus 로고
    • A unique sequence of the laminin alpha 3 G domain binds to heparin and promotes cell adhesion through syndecan-2 and -4
    • Utani A., Nomizu M., Matsuura H., Kato K., Kobayashi T., Takeda U., Aota S., Nielsen P.K., and Shinkai H. A unique sequence of the laminin alpha 3 G domain binds to heparin and promotes cell adhesion through syndecan-2 and -4. J. Biol. Chem. 276 (2001) 28779-28788
    • (2001) J. Biol. Chem. , vol.276 , pp. 28779-28788
    • Utani, A.1    Nomizu, M.2    Matsuura, H.3    Kato, K.4    Kobayashi, T.5    Takeda, U.6    Aota, S.7    Nielsen, P.K.8    Shinkai, H.9
  • 40
    • 0042887252 scopus 로고    scopus 로고
    • The ins and outs of fibronectin matrix assembly
    • Wierzbicka-Patynowski I., and Schwarzbauer J. The ins and outs of fibronectin matrix assembly. J. Cell Sci. 116 (2003) 3269-3276
    • (2003) J. Cell Sci. , vol.116 , pp. 3269-3276
    • Wierzbicka-Patynowski, I.1    Schwarzbauer, J.2
  • 41
    • 0025943405 scopus 로고
    • Immortalization of normal human bronchial epithelial cells by human papillomaviruses 16 or 18
    • Willey J.C., Broussoud A., Sleemi A., Bennett W.P., Cerutti P., and Harris C.C. Immortalization of normal human bronchial epithelial cells by human papillomaviruses 16 or 18. Cancer Res. 51 (1991) 5370-5377
    • (1991) Cancer Res. , vol.51 , pp. 5370-5377
    • Willey, J.C.1    Broussoud, A.2    Sleemi, A.3    Bennett, W.P.4    Cerutti, P.5    Harris, C.C.6
  • 42
    • 0030046992 scopus 로고    scopus 로고
    • Anchorage mediated by integrin α6β4 to laminin 5 (epiligrin) regulates tyrosine phosphorylation of a membrane associated 80-kD protein
    • Xia Y., Gill S.G., and Carter W.G. Anchorage mediated by integrin α6β4 to laminin 5 (epiligrin) regulates tyrosine phosphorylation of a membrane associated 80-kD protein. J. Cell Biol. 132 (1996) 727-740
    • (1996) J. Cell Biol. , vol.132 , pp. 727-740
    • Xia, Y.1    Gill, S.G.2    Carter, W.G.3


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