메뉴 건너뛰기




Volumn 117, Issue 12, 2004, Pages 2611-2622

Inhibition of basement membrane formation by a nidogen-binding laminin γ1-chain fragment in human skin-organotypic cocultures

Author keywords

Basement membrane; Humanskin organotypic coculture; Nidogen

Indexed keywords

ALPHA6BETA4 INTEGRIN; BIOLOGICAL MARKER; COLLAGEN TYPE 4; ENTACTIN; ISOPROTEIN; KALININ; KERATIN; LAMININ 1; PERLECAN; RECOMBINANT PROTEIN;

EID: 3042733154     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.01127     Document Type: Article
Times cited : (47)

References (73)
  • 1
    • 0030454231 scopus 로고    scopus 로고
    • Rescue of mammary epithelial cell apoptosis and entactin degradation by a tissue inhibitor of metalloproteinases-1 transgene
    • Alexander, C. M., Howard, E. W., Bissell, M. J. and Werb, Z. (1996). Rescue of mammary epithelial cell apoptosis and entactin degradation by a tissue inhibitor of metalloproteinases-1 transgene. J. Cell Biol. 135, 1669-1677.
    • (1996) J. Cell Biol. , vol.135 , pp. 1669-1677
    • Alexander, C.M.1    Howard, E.W.2    Bissell, M.J.3    Werb, Z.4
  • 2
    • 0021926418 scopus 로고
    • Epidermal morphogenesis and induction of the 67 kd polypeptide by culture of human keratinocytes at the liquid-air interface
    • Asselineau, D., Bernhard, B., Bailly, C. and Darmon, M. (1985). Epidermal morphogenesis and induction of the 67 kd polypeptide by culture of human keratinocytes at the liquid-air interface. Exp. Cell Res. 159, 536-539.
    • (1985) Exp. Cell Res. , vol.159 , pp. 536-539
    • Asselineau, D.1    Bernhard, B.2    Bailly, C.3    Darmon, M.4
  • 3
    • 0028579734 scopus 로고
    • Perlecan, basal lamina proteoglycan, promotes basic fibroblast growth factor-receptor binding, mitogenesis, and angiogenesis
    • Aviezer, D., Hecht, D., Safran, M., Eisinger, M., David, G. and Yayon, A. (1994). Perlecan, basal lamina proteoglycan, promotes basic fibroblast growth factor-receptor binding, mitogenesis, and angiogenesis. Cell 79, 1005-1013.
    • (1994) Cell , vol.79 , pp. 1005-1013
    • Aviezer, D.1    Hecht, D.2    Safran, M.3    Eisinger, M.4    David, G.5    Yayon, A.6
  • 4
    • 0024460533 scopus 로고
    • Binding of nidogen and the laminin-nidogen complex to basement membrane collagen type IV
    • Aumailley, M., Wiedemann, H., Mann, K. and Timpl, R. (1989). Binding of nidogen and the laminin-nidogen complex to basement membrane collagen type IV. Eur. J. Biochem. 184, 241-248.
    • (1989) Eur. J. Biochem. , vol.184 , pp. 241-248
    • Aumailley, M.1    Wiedemann, H.2    Mann, K.3    Timpl, R.4
  • 5
    • 0033752213 scopus 로고    scopus 로고
    • Membrane-type metalloproteinase-mediated progelatinase a activation in non-tumorigenic and tumorigenic human keratinocytes
    • Baumann, P., Zigrino, P., Mauch, C., Breitkreutz, D. and Nischt, R. (2000). Membrane-type metalloproteinase-mediated progelatinase a activation in non-tumorigenic and tumorigenic human keratinocytes. Br. J. Cancer 83, 1387-1393.
    • (2000) Br. J. Cancer , vol.83 , pp. 1387-1393
    • Baumann, P.1    Zigrino, P.2    Mauch, C.3    Breitkreutz, D.4    Nischt, R.5
  • 6
    • 0032908323 scopus 로고    scopus 로고
    • Structure and function of hemidesmosomes: More than simple adhesion complexes
    • Borradori, L. and Sonnenberg, A. (1999). Structure and function of hemidesmosomes: more than simple adhesion complexes. J. Invest. Dermatol. 112, 411-418.
    • (1999) J. Invest. Dermatol. , vol.112 , pp. 411-418
    • Borradori, L.1    Sonnenberg, A.2
  • 7
    • 0026494418 scopus 로고
    • Influence of dermal equivalent maturation on the development of a cultured skin equivalent
    • Bouvard, V., Germain, L., Rompré, P., Roy, B. and Auger, F. A. (1992). Influence of dermal equivalent maturation on the development of a cultured skin equivalent. Biochem. Cell Biol. 70, 34-42.
    • (1992) Biochem. Cell Biol. , vol.70 , pp. 34-42
    • Bouvard, V.1    Germain, L.2    Rompré, P.3    Roy, B.4    Auger, F.A.5
  • 8
    • 84985765947 scopus 로고
    • Differentiation specific functions in cultured and transplanted mouse keratinocytes: Environmental influence on ultrastructure and keratin expression
    • Breitkreutz, D., Bohnert, A., Herzmann, E., Bowden, P. E., Boukamp, P. and Fusenig, N. E. (1984). Differentiation specific functions in cultured and transplanted mouse keratinocytes: environmental influence on ultrastructure and keratin expression. Differentiation 26, 154-169.
    • (1984) Differentiation , vol.26 , pp. 154-169
    • Breitkreutz, D.1    Bohnert, A.2    Herzmann, E.3    Bowden, P.E.4    Boukamp, P.5    Fusenig, N.E.6
  • 9
    • 0031047074 scopus 로고    scopus 로고
    • Integrin and basement membrane normalization in mouse grafts of human keratinocytes - Implications for epidermal homeostasis
    • Breitkreutz, D., Stark, H. J., Mirancea, N., Tomakidi, P., Steinbauer, H. and Fusenig, N. E. (1997). Integrin and basement membrane normalization in mouse grafts of human keratinocytes - implications for epidermal homeostasis. Differentiation 61, 195-209.
    • (1997) Differentiation , vol.61 , pp. 195-209
    • Breitkreutz, D.1    Stark, H.J.2    Mirancea, N.3    Tomakidi, P.4    Steinbauer, H.5    Fusenig, N.E.6
  • 10
    • 0031945960 scopus 로고    scopus 로고
    • Epidermal differentiation and basement membrane formation by HaCaT cells in surface transplants
    • Breitkreutz, D., Schoop, V. M., Mirancea, N., Baur, M., Stark, H. J. and Fusenig, N. E. (1998). Epidermal differentiation and basement membrane formation by HaCaT cells in surface transplants. Eur. J. Cell Biol. 75, 273-286.
    • (1998) Eur. J. Cell Biol. , vol.75 , pp. 273-286
    • Breitkreutz, D.1    Schoop, V.M.2    Mirancea, N.3    Baur, M.4    Stark, H.J.5    Fusenig, N.E.6
  • 11
    • 0025679064 scopus 로고
    • Distinct functions for integrins α3β1 in focal adhesions and α6β4/bullous pemphigoid antigen in a new stable anchoring contact (SAC) of keatinocytes: Relation to hemidesmosomes
    • Carter, W. G., Kaur, P., Gil, S. G., Gahr, P. J. and Wayner, E. A. (1990). Distinct functions for integrins α3β1 in focal adhesions and α6β4/bullous pemphigoid antigen in a new stable anchoring contact (SAC) of keatinocytes: relation to hemidesmosomes. J. Cell Biol. 111, 3141-3154.
    • (1990) J. Cell Biol. , vol.111 , pp. 3141-3154
    • Carter, W.G.1    Kaur, P.2    Gil, S.G.3    Gahr, P.J.4    Wayner, E.A.5
  • 12
    • 0029864911 scopus 로고    scopus 로고
    • Human amnion contains a novel laminin variant, laminin-7, which like laminin 6, covalently associates with laminin 5 to promote epithelial-stromal attachment
    • Champliaud, M. F., Lunstrum, G. P., Rousselle, P., Nishiyama, T., Keane, D. R. and Burgeson, R. E. (1996). Human amnion contains a novel laminin variant, laminin-7, which like laminin 6, covalently associates with laminin 5 to promote epithelial-stromal attachment. J. Cell Biol. 132, 1189-1198.
    • (1996) J. Cell Biol. , vol.132 , pp. 1189-1198
    • Champliaud, M.F.1    Lunstrum, G.P.2    Rousselle, P.3    Nishiyama, T.4    Keane, D.R.5    Burgeson, R.E.6
  • 13
    • 0034075654 scopus 로고    scopus 로고
    • Form and function: The laminin family of heterotrimers
    • Colognato, H. and Yurchenco, P. (2000). Form and function: the laminin family of heterotrimers. Dev. Dyn. 218, 213-234.
    • (2000) Dev. Dyn. , vol.218 , pp. 213-234
    • Colognato, H.1    Yurchenco, P.2
  • 14
    • 0027507150 scopus 로고
    • Culturing keratinocytes and fibroblasts in a three-dimensional mesh results in epidermal differentiation and formation of a basal lamina-anchoring zone
    • Contard, P., Bartel, R. L., Jacobs, L. II, Perlish, J. S., MacDonald, D. II, Handler, L., Cone, D. and Fleischmajer, R. (1993). Culturing keratinocytes and fibroblasts in a three-dimensional mesh results in epidermal differentiation and formation of a basal lamina-anchoring zone. J. Invest. Dermatol. 100, 35-39.
    • (1993) J. Invest. Dermatol. , vol.100 , pp. 35-39
    • Contard, P.1    Bartel, R.L.2    Jacobs II, L.3    Perlish, J.S.4    MacDonald II, D.5    Handler, L.6    Cone, D.7    Fleischmajer, R.8
  • 15
    • 0026725843 scopus 로고
    • The receptor for basement membrane glycoprotein entactin is the integrin alpha3/beta1
    • Dedhar, S., Jewell, K., Rojiani, M. and Gray, V. (1992). The receptor for basement membrane glycoprotein entactin is the integrin alpha3/beta1. J. Biol. Chem. 267, 18908-18914.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18908-18914
    • Dedhar, S.1    Jewell, K.2    Rojiani, M.3    Gray, V.4
  • 18
    • 0035800766 scopus 로고    scopus 로고
    • Pro-collagenase-1 (matrix metalloproteinase-1) binds the α2β1 integrin upon release from keratinocytes migrating on type I collagen
    • Dumin, J. A., Dickeson, S. K., Stricker, T. P., Bhattacharyya-Pakrasi, M., Roby, J. D., Santoro, S. A. and Parks, W. C. (2001). Pro-collagenase-1 (matrix metalloproteinase-1) binds the α 2β1 integrin upon release from keratinocytes migrating on type I collagen. J. Biol. Chem. 276, 129368-129374.
    • (2001) J. Biol. Chem. , vol.276 , pp. 129368-129374
    • Dumin, J.A.1    Dickeson, S.K.2    Stricker, T.P.3    Bhattacharyya-Pakrasi, M.4    Roby, J.D.5    Santoro, S.A.6    Parks, W.C.7
  • 20
    • 0018579727 scopus 로고
    • Dithiothreitol separation of newborn rodent dermis and epidermis
    • Epstein, E. H., Munderloh, N. H. and Fukuyama, K. (1979). Dithiothreitol separation of newborn rodent dermis and epidermis. J. Invest. Dermatol. 73, 207-210.
    • (1979) J. Invest. Dermatol. , vol.73 , pp. 207-210
    • Epstein, E.H.1    Munderloh, N.H.2    Fukuyama, K.3
  • 21
    • 0023876483 scopus 로고
    • Monoclonal antibody to human carcinoma-associated protein complex: Quantitation in normal and tumor tissue
    • Falcioni, R., Sacchi, A., Resau, J. and Kennel, S. J. (1988). Monoclonal antibody to human carcinoma-associated protein complex: quantitation in normal and tumor tissue. Cancer Res. 48, 816-821.
    • (1988) Cancer Res. , vol.48 , pp. 816-821
    • Falcioni, R.1    Sacchi, A.2    Resau, J.3    Kennel, S.J.4
  • 24
    • 0018848803 scopus 로고
    • Immunofluorescent localization of type IV collagen and laminin during endochondral bone differentiation and regulation by pituitary growth hormone
    • Foidart, J. M. and Reddi, A. H. (1980). Immunofluorescent localization of type IV collagen and laminin during endochondral bone differentiation and regulation by pituitary growth hormone. Dev. Biol. 75, 130-136.
    • (1980) Dev. Biol. , vol.75 , pp. 130-136
    • Foidart, J.M.1    Reddi, A.H.2
  • 26
    • 0035858887 scopus 로고    scopus 로고
    • The short arm of the laminin γ2 chain plays a pivotal role in the incorporation of laminin 5 into the extracellular matrix and in cell adhesion
    • Gagnoux-Palacios, L., Allegra, M., Spirito, F., Pommeret, O., Romero, C., Ortonne, J. P. and Meneguzzi, G. (2001). The short arm of the laminin γ2 chain plays a pivotal role in the incorporation of laminin 5 into the extracellular matrix and in cell adhesion. J. Cell Biol. 153, 835-849.
    • (2001) J. Cell Biol. , vol.153 , pp. 835-849
    • Gagnoux-Palacios, L.1    Allegra, M.2    Spirito, F.3    Pommeret, O.4    Romero, C.5    Ortonne, J.P.6    Meneguzzi, G.7
  • 27
    • 0030006606 scopus 로고    scopus 로고
    • Desmosomes and hemidesmosomes: Structure and function of molecular components
    • Green, K. J. and Jones, J. C. R. (1996). Desmosomes and hemidesmosomes: structure and function of molecular components. FASEB J. 10, 871-881.
    • (1996) FASEB J. , vol.10 , pp. 871-881
    • Green, K.J.1    Jones, J.C.R.2
  • 28
    • 0025728732 scopus 로고
    • Integrin expression during human epidermal development in vitro and in vivo
    • Hertle, M. D., Adams, J. C. and Watt, F. M. (1991). Integrin expression during human epidermal development in vitro and in vivo. Development 112, 193-206.
    • (1991) Development , vol.112 , pp. 193-206
    • Hertle, M.D.1    Adams, J.C.2    Watt, F.M.3
  • 29
    • 0025811645 scopus 로고
    • Characterization of human loricrin, structure and function of a new class of epidermal cell envelope proteins
    • Hohl, D., Mehrel, T., Lichti, U., Truner, M. L., Roop, D. R. and Steinert, P. M. (1991). Characterization of human loricrin, structure and function of a new class of epidermal cell envelope proteins. J. Biol. Chem. 266, 6626-6636.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6626-6636
    • Hohl, D.1    Mehrel, T.2    Lichti, U.3    Truner, M.L.4    Roop, D.R.5    Steinert, P.M.6
  • 30
    • 0037192771 scopus 로고    scopus 로고
    • Integrin α2-deficient mice develop normally, are fertile, but display partially defective platelet interaction with collagen
    • Holtkötter, O., Nieswandt, B., Smyth, N., Müller, W., Hafner, M., Schulte, V., Krieg, T. and Eckes, B. (2002). Integrin α2-deficient mice develop normally, are fertile, but display partially defective platelet interaction with collagen. J. Biol. Chem. 277, 10789-10794.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10789-10794
    • Holtkötter, O.1    Nieswandt, B.2    Smyth, N.3    Müller, W.4    Hafner, M.5    Schulte, V.6    Krieg, T.7    Eckes, B.8
  • 31
    • 0031059074 scopus 로고    scopus 로고
    • Importance of nidogen binding to laminin γ1 for branching epithelial morphogenesis of the submandibular gland
    • Kadoya, Y., Salmivirta, K., Talts, J. F., Kadoya, K., Mayer. U., Timpl, R. and Ekblom, P. (1997). Importance of nidogen binding to laminin γ1 for branching epithelial morphogenesis of the submandibular gland. Development 124, 683-691.
    • (1997) Development , vol.124 , pp. 683-691
    • Kadoya, Y.1    Salmivirta, K.2    Talts, J.F.3    Kadoya, K.4    Mayer, U.5    Timpl, R.6    Ekblom, P.7
  • 32
    • 0025880917 scopus 로고
    • Integrin α2β1 is upregulated in fibroblasts and highly aggressive melanoma cells in three-dimensional collagen lattices and mediates the reorganization of collagen I fibrils
    • Klein, C. E., Dressel, D., Steinmayer, T., Mauch, C., Eckes, B., Krieg, T., Bankert, R. B. and Weber, L. (1991). Integrin α 2β1 is upregulated in fibroblasts and highly aggressive melanoma cells in three-dimensional collagen lattices and mediates the reorganization of collagen I fibrils. J. Cell Biol. 115, 1427-1436.
    • (1991) J. Cell Biol. , vol.115 , pp. 1427-1436
    • Klein, C.E.1    Dressel, D.2    Steinmayer, T.3    Mauch, C.4    Eckes, B.5    Krieg, T.6    Bankert, R.B.7    Weber, L.8
  • 33
    • 0032508461 scopus 로고    scopus 로고
    • Nidogen-2: A new basement membrane protein with diverse binding properties
    • Kohfeldt, E., Sasaki, T., Göhring, W. and Timpl, R. (1998). Nidogen-2: a new basement membrane protein with diverse binding properties. J. Mol. Biol. 282, 99-109.
    • (1998) J. Mol. Biol. , vol.282 , pp. 99-109
    • Kohfeldt, E.1    Sasaki, T.2    Göhring, W.3    Timpl, R.4
  • 34
    • 0024328320 scopus 로고
    • The use of retinoic acid to probe the relation between hyperproliferation-associated keratins and cell proliferation in normal and malignant epidermal cells
    • Kopan, R. and Fuchs, E. (1989). The use of retinoic acid to probe the relation between hyperproliferation-associated keratins and cell proliferation in normal and malignant epidermal cells. J. Cell Biol. 109, 295-307.
    • (1989) J. Cell Biol. , vol.109 , pp. 295-307
    • Kopan, R.1    Fuchs, E.2
  • 35
    • 0027217908 scopus 로고
    • Expression of integrins and basement membrane components by wound keratinocytes
    • Larjava, H., Salo, T., Kramer, R. H. and Heino, J. (1993). Expression of integrins and basement membrane components by wound keratinocytes. J. Clin. Invest. 92, 1425-1435.
    • (1993) J. Clin. Invest. , vol.92 , pp. 1425-1435
    • Larjava, H.1    Salo, T.2    Kramer, R.H.3    Heino, J.4
  • 37
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • Lorand, L. and Graham, R. M. (2003). Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat. Rev. Mol. Cell Biol. 4, 140-156.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 38
    • 0027454382 scopus 로고
    • Cellular origin of the dermal-epidermal basement membrane
    • Marinkovich, P., Keene, D. R., Rimberg, C. S. and Burgeson, R. (1993). Cellular origin of the dermal-epidermal basement membrane. Dev. Dyn. 197, 255-267.
    • (1993) Dev. Dyn. , vol.197 , pp. 255-267
    • Marinkovich, P.1    Keene, D.R.2    Rimberg, C.S.3    Burgeson, R.4
  • 39
    • 0027286695 scopus 로고
    • A single EGF-like motif of laminin is responsible for high affinity nidogen binding
    • Mayer, U., Nischt, R., Pöschl, E., Mann, K., Fukuda, K., Gerl, M., Yamada, Y. and Timpl, R. (1993). A single EGF-like motif of laminin is responsible for high affinity nidogen binding. EMBO J. 12, 1879-1885.
    • (1993) EMBO J. , vol.12 , pp. 1879-1885
    • Mayer, U.1    Nischt, R.2    Pöschl, E.3    Mann, K.4    Fukuda, K.5    Gerl, M.6    Yamada, Y.7    Timpl, R.8
  • 41
    • 0141619176 scopus 로고    scopus 로고
    • Ultrastructural orientation of laminin 5 in the epidermal basement membrane: An updated model for basement membrane organization
    • McMillan, J. R., Akiyama, M. and Shimizu, H. (2003). Ultrastructural orientation of laminin 5 in the epidermal basement membrane: an updated model for basement membrane organization. J. Histochem. Cytochem. 51, 1299-1306.
    • (2003) J. Histochem. Cytochem. , vol.51 , pp. 1299-1306
    • McMillan, J.R.1    Akiyama, M.2    Shimizu, H.3
  • 42
    • 0030919488 scopus 로고    scopus 로고
    • The laminin α chains: Expression, developmental transitions, and chromosomal locations of α1-5, and cloning of a novel α3 isoform
    • Miner, J. H., Patton, B. L., Lentz, S. I., Gilbert, D. J., Snider, W. D., Jenkins, N. A., Copeland, N. G. and Sanes, J. R. (1997). The laminin α chains: expression, developmental transitions, and chromosomal locations of α1-5, and cloning of a novel α3 isoform. J. Cell Biol. 137, 685-701.
    • (1997) J. Cell Biol. , vol.137 , pp. 685-701
    • Miner, J.H.1    Patton, B.L.2    Lentz, S.I.3    Gilbert, D.J.4    Snider, W.D.5    Jenkins, N.A.6    Copeland, N.G.7    Sanes, J.R.8
  • 43
    • 0036860601 scopus 로고    scopus 로고
    • Evidence of nidogen-2 compensation for nidogen-1 deficiency in transgenic mice
    • Miosge, N., Sasaki, T. and Timpl, R. (2002). Evidence of nidogen-2 compensation for nidogen-1 deficiency in transgenic mice. Matrix Biol. 21, 611-621.
    • (2002) Matrix Biol. , vol.21 , pp. 611-621
    • Miosge, N.1    Sasaki, T.2    Timpl, R.3
  • 44
    • 0036222549 scopus 로고    scopus 로고
    • Sensing the environment: A historical perspective on integrin signal transduction
    • Miranti, C. K. and Brugge, J. S. (2002). Sensing the environment: a historical perspective on integrin signal transduction. Nat. Cell Biol. 4, 83-90.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 83-90
    • Miranti, C.K.1    Brugge, J.S.2
  • 47
    • 0023377705 scopus 로고
    • Laminin-nidogen complex: Extraction with chelating agents and structural characterisation
    • Paulsson, M., Aumailley, M., Deutzmann, R., Timpl, R., Beck, K. and Engel, J. (1987). Laminin-nidogen complex: extraction with chelating agents and structural characterisation. Eur. J. Biochem. 166, 11-19.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 11-19
    • Paulsson, M.1    Aumailley, M.2    Deutzmann, R.3    Timpl, R.4    Beck, K.5    Engel, J.6
  • 48
    • 0030867922 scopus 로고    scopus 로고
    • The formation of competent barrier lipids in reconstructed human epidermis requires the presence of vitamin C
    • Ponec, M., Weerheim, A., Kempenaar, J., Mulder, A., Gooris, G., Bouwstra, J. and Mommaas, A. M. (1997). The formation of competent barrier lipids in reconstructed human epidermis requires the presence of vitamin C. J. Invest. Dermatol. 109, 348-355.
    • (1997) J. Invest. Dermatol. , vol.109 , pp. 348-355
    • Ponec, M.1    Weerheim, A.2    Kempenaar, J.3    Mulder, A.4    Gooris, G.5    Bouwstra, J.6    Mommaas, A.M.7
  • 49
    • 0028074247 scopus 로고
    • Two non-contiguous regions contribute to nidogen binding to a single EGF-like motif of the laminin gamma 1 chain
    • Pöschl, E., Fox, J. W., Block, D., Mayer, U. and Timpl, R. (1994). Two non-contiguous regions contribute to nidogen binding to a single EGF-like motif of the laminin gamma 1 chain. EMBO J. 13, 3741-3747.
    • (1994) EMBO J. , vol.13 , pp. 3741-3747
    • Pöschl, E.1    Fox, J.W.2    Block, D.3    Mayer, U.4    Timpl, R.5
  • 50
    • 0029790892 scopus 로고    scopus 로고
    • Site-directed mutagenesis and structural interpretation of the nidogen binding site of the laminin gamma 1 chain
    • Pöschl, E., Mayer, U., Stetefeld, J., Baumgartner, R., Holak, T. A., Huber, R. and Timpl, R. (1996). Site-directed mutagenesis and structural interpretation of the nidogen binding site of the laminin gamma 1 chain. EMBO J. 15, 5154-5159.
    • (1996) EMBO J. , vol.15 , pp. 5154-5159
    • Pöschl, E.1    Mayer, U.2    Stetefeld, J.3    Baumgartner, R.4    Holak, T.A.5    Huber, R.6    Timpl, R.7
  • 51
    • 0034108469 scopus 로고    scopus 로고
    • Nidogen-1 regulates laminin-1 dependent mammary specific gene expression
    • Pujuguet, P., Simian, M., Liaw, J., Timpl, R., Werb, Z. and Bissell, M. J. (2000). Nidogen-1 regulates laminin-1 dependent mammary specific gene expression. J. Cell Sci. 113, 849-858.
    • (2000) J. Cell Sci. , vol.113 , pp. 849-858
    • Pujuguet, P.1    Simian, M.2    Liaw, J.3    Timpl, R.4    Werb, Z.5    Bissell, M.J.6
  • 52
    • 0032962217 scopus 로고    scopus 로고
    • Mutation analysis and molecular genetics of epidermolysis bullosa
    • Pulkkinen, L. and Uitto, J. (1999). Mutation analysis and molecular genetics of epidermolysis bullosa. Matrix Biol. 18, 29-42.
    • (1999) Matrix Biol. , vol.18 , pp. 29-42
    • Pulkkinen, L.1    Uitto, J.2
  • 53
    • 0032489678 scopus 로고    scopus 로고
    • Linking α6β4-based cell adhesion to the intermediate filament cytoskeleton: Direct interaction between the β4 subunit and plectin at multiple sites
    • Rezniczek, G. A., de Pereda, J. M., Reipert, S. and Wiche, G. (1998). Linking α6β4-based cell adhesion to the intermediate filament cytoskeleton: direct interaction between the β4 subunit and plectin at multiple sites. J. Cell Biol. 141, 209-225.
    • (1998) J. Cell Biol. , vol.141 , pp. 209-225
    • Rezniczek, G.A.1    de Pereda, J.M.2    Reipert, S.3    Wiche, G.4
  • 54
    • 0025879967 scopus 로고
    • Kalinin: An epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments
    • Rousselle, P., Lunstrum, G. P., Keene, D. R. and Burgeson, R. E. (1991). Kalinin: an epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments. J. Cell Biol. 114, 567-576.
    • (1991) J. Cell Biol. , vol.114 , pp. 567-576
    • Rousselle, P.1    Lunstrum, G.P.2    Keene, D.R.3    Burgeson, R.E.4
  • 55
    • 0036405396 scopus 로고    scopus 로고
    • Binding of mouse nidogen-2 to basement membrane components and cells and its expression in embryonic and adult tissues suggest complementary functions of the two nidogens
    • Salmivirta, K., Talts, J. F., Olsson, M., Sasaki, T., Timpl, R. and Ekblom, P. (2002). Binding of mouse nidogen-2 to basement membrane components and cells and its expression in embryonic and adult tissues suggest complementary functions of the two nidogens. Exp. Cell Res. 279, 188-201.
    • (2002) Exp. Cell Res. , vol.279 , pp. 188-201
    • Salmivirta, K.1    Talts, J.F.2    Olsson, M.3    Sasaki, T.4    Timpl, R.5    Ekblom, P.6
  • 57
    • 0036785584 scopus 로고    scopus 로고
    • Gene structure and functional analysis of the mouse nidogen-2 gene: Nidogen-2 is not essential for basement membrane formation in mice
    • Schymeinsky, J. Nedbal, S., Miosge, N., Pöschl, E., Rao, C., Beier, D. R., Skarnes, W. C., Timpl, R. and Bader, B. (2002). Gene structure and functional analysis of the mouse nidogen-2 gene: nidogen-2 is not essential for basement membrane formation in mice. Mol. Cell. Biol. 22, 6820-6830.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6820-6830
    • Schymeinsky, J.1    Nedbal, S.2    Miosge, N.3    Pöschl, E.4    Rao, C.5    Beier, D.R.6    Skarnes, W.C.7    Timpl, R.8    Bader, B.9
  • 58
    • 0028019250 scopus 로고
    • Organotypic and epidermal-dermal cocultures of normal human keratinocytes and dermal cells: Regulation of transforming growth factor α, β1 and β2 mRNA levels
    • Smola, H., Thiekötter, G., Baur, M., Stark, H.-J., Breitkreutz, D. and Fusenig, N. E. (1994). Organotypic and epidermal-dermal cocultures of normal human keratinocytes and dermal cells: regulation of transforming growth factor α, β1 and β2 mRNA levels. Toxicology in vitro 8, 641-650.
    • (1994) Toxicology in Vitro , vol.8 , pp. 641-650
    • Smola, H.1    Thiekötter, G.2    Baur, M.3    Stark, H.-J.4    Breitkreutz, D.5    Fusenig, N.E.6
  • 59
    • 0031845096 scopus 로고    scopus 로고
    • Dynamics of basement membrane formation by keratinocyte-fibroblast interactions in organotypic skin culture
    • Smola, H., Stark, H. J., Thiekötter, G., Mirancea, N., Krieg, T. and Fusenig, N. E. (1998). Dynamics of basement membrane formation by keratinocyte-fibroblast interactions in organotypic skin culture. Exp. Cell Res. 239, 399-410.
    • (1998) Exp. Cell Res. , vol.239 , pp. 399-410
    • Smola, H.1    Stark, H.J.2    Thiekötter, G.3    Mirancea, N.4    Krieg, T.5    Fusenig, N.E.6
  • 61
    • 0024272151 scopus 로고
    • Isolation of complementary DNA for bullous pemphigoid antigen by use of patients' antibodies
    • Stanley, J. R., Tanaka, T., Mueller, S., Klaus-Kovtun, V. and Roop, D. R. (1988). Isolation of complementary DNA for bullous pemphigoid antigen by use of patients' antibodies. J. Clin. Invest. 82, 1864-1870.
    • (1988) J. Clin. Invest. , vol.82 , pp. 1864-1870
    • Stanley, J.R.1    Tanaka, T.2    Mueller, S.3    Klaus-Kovtun, V.4    Roop, D.R.5
  • 62
    • 0032896837 scopus 로고    scopus 로고
    • Organotypic keratinocyte cocultures in defined medium with regular epidermal morphogenesis and differentiation
    • Stark, H. J., Baur, M., Breitkreutz, D., Mirancea, N. and Fusenig, N. E. (1999). Organotypic keratinocyte cocultures in defined medium with regular epidermal morphogenesis and differentiation. J. Invest. Dermatol. 112, 681-691.
    • (1999) J. Invest. Dermatol. , vol.112 , pp. 681-691
    • Stark, H.J.1    Baur, M.2    Breitkreutz, D.3    Mirancea, N.4    Fusenig, N.E.5
  • 64
    • 0030271572 scopus 로고    scopus 로고
    • Macromolecular organization of basement membranes
    • Timpl, R. (1996). Macromolecular organization of basement membranes. Curr. Opin. Cell Biol. 8, 618-624.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 618-624
    • Timpl, R.1
  • 65
    • 0033047394 scopus 로고    scopus 로고
    • Defects of basement membrane and hemidesmosome structure correlate with malignant phenotype and stromal interactions in HaCaT-ras xenografts
    • Tomakidi, P., Mirancea, N., Fusenig, N. E., Herold-Mende, C., Bosch, F. X. and Breitkreutz, D. (1999). Defects of basement membrane and hemidesmosome structure correlate with malignant phenotype and stromal interactions in HaCaT-ras xenografts. Differentiation 64, 263-275.
    • (1999) Differentiation , vol.64 , pp. 263-275
    • Tomakidi, P.1    Mirancea, N.2    Fusenig, N.E.3    Herold-Mende, C.4    Bosch, F.X.5    Breitkreutz, D.6
  • 66
    • 0032440684 scopus 로고    scopus 로고
    • Laminin 5 can promote assembly of the lamina densa in the skin equivalent model
    • Tsunenaga, M., Adachi, E., Amano, S., Burgeson, R. E. and Nishiyama, T. (1998). Laminin 5 can promote assembly of the lamina densa in the skin equivalent model. Matrix Biol. 17, 603-613.
    • (1998) Matrix Biol. , vol.17 , pp. 603-613
    • Tsunenaga, M.1    Adachi, E.2    Amano, S.3    Burgeson, R.E.4    Nishiyama, T.5
  • 67
    • 0037351011 scopus 로고    scopus 로고
    • Expression of the nidogen-binding site of the laminin γ1 chain disturbs basement membrane formation and maintenance in F9 embryoid bodies
    • Tunggal, J., Wartenberg, M., Paulsson, M. and Smyth, N. (2003). Expression of the nidogen-binding site of the laminin γ1 chain disturbs basement membrane formation and maintenance in F9 embryoid bodies. J. Cell Sci. 116, 803-812.
    • (2003) J. Cell Sci. , vol.116 , pp. 803-812
    • Tunggal, J.1    Wartenberg, M.2    Paulsson, M.3    Smyth, N.4
  • 69
    • 0036683057 scopus 로고    scopus 로고
    • Role of integrins in regulating epidermal adhesion, growth and differentiation
    • Watt, F. M. (2002). Role of integrins in regulating epidermal adhesion, growth and differentiation. EMBO J. 21, 3919-3926.
    • (2002) EMBO J. , vol.21 , pp. 3919-3926
    • Watt, F.M.1
  • 70
    • 0036333442 scopus 로고    scopus 로고
    • Specific ablation of the nidogen-binding site in the laminin γ1 chain interferes with kidney and lung development
    • Willem, M., Miosge, N., Halfter, W., Smyth, N., Jannetti, I., Burghart, E., Timpl, R. and Mayer, U. (2002). Specific ablation of the nidogen-binding site in the laminin γ1 chain interferes with kidney and lung development. Development 129, 2711-2722.
    • (2002) Development , vol.129 , pp. 2711-2722
    • Willem, M.1    Miosge, N.2    Halfter, W.3    Smyth, N.4    Jannetti, I.5    Burghart, E.6    Timpl, R.7    Mayer, U.8
  • 71
    • 0036229695 scopus 로고    scopus 로고
    • Integrin regulation of growth factor receptors
    • Yamada, K. M. and Even-Ram, S. (2002). Integrin regulation of growth factor receptors. Nat. Cell Biol. 4, 75-76.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 75-76
    • Yamada, K.M.1    Even-Ram, S.2
  • 72
    • 0026639532 scopus 로고
    • Laminins form an independent network in basement membranes
    • Yurchenco, P. D., Cheng, Y. S. and Colognato, H. (1992). Laminins form an independent network in basement membranes. J. Cell Biol. 117, 1119-1133.
    • (1992) J. Cell Biol. , vol.117 , pp. 1119-1133
    • Yurchenco, P.D.1    Cheng, Y.S.2    Colognato, H.3
  • 73
    • 0028987192 scopus 로고
    • Transforming growth factor-β1 modulates β1 and β5 integrin receptors and induces the de novo expression of the αvβ6 heterodimer in normal human keratinocytes: Implications for wound healing
    • Zambruno, G., Marchisio, P. C., Marconi, A., Vashierei, C., Melchiori, A., Gianetti, A. and DeLuca, M. (1995). Transforming growth factor-β1 modulates β1 and β5 integrin receptors and induces the de novo expression of the αvβ6 heterodimer in normal human keratinocytes: implications for wound healing. J. Cell Biol. 129, 853-865.
    • (1995) J. Cell Biol. , vol.129 , pp. 853-865
    • Zambruno, G.1    Marchisio, P.C.2    Marconi, A.3    Vashierei, C.4    Melchiori, A.5    Gianetti, A.6    DeLuca, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.