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Volumn 117, Issue 4, 2004, Pages 571-581

Murine tenascin-W: A novel mammalian tenascin expressed in kidney and at sites of bone and smooth muscle development

Author keywords

Adhesion; Development; Expression; Extracellular matrix; Hexabrachion; Tenascin

Indexed keywords

ACTIN; ALPHA INTEGRIN; ARGINYLGLYCYLASPARTIC ACID; BONE MORPHOGENETIC PROTEIN 2; RECOMBINANT PROTEIN; SCLEROPROTEIN; TENASCIN; TENASCIN W; UNCLASSIFIED DRUG;

EID: 1242284590     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00867     Document Type: Article
Times cited : (76)

References (40)
  • 1
    • 0035939662 scopus 로고    scopus 로고
    • Identification and characterization of a novel extracellular matrix protein nephronectin that is associated with integrin alpha8beta1 in the embryonic kidney
    • Brandenberger, R., Schmidt, A., Linton, J., Wang, D., Backus, C., Denda, S., Muller, U. and Reichardt, L. F. (2001). Identification and characterization of a novel extracellular matrix protein nephronectin that is associated with integrin alpha8beta1 in the embryonic kidney. J. Cell Biol. 154, 447-458.
    • (2001) J. Cell Biol. , vol.154 , pp. 447-458
    • Brandenberger, R.1    Schmidt, A.2    Linton, J.3    Wang, D.4    Backus, C.5    Denda, S.6    Muller, U.7    Reichardt, I.F.8
  • 2
    • 0028859440 scopus 로고
    • Tenascins, a growing family of extracellular matrix proteins
    • Chiquet-Ehrismann, R. (1995). Tenascins, a growing family of extracellular matrix proteins. Experientia 51, 853-862.
    • (1995) Experientia , vol.51 , pp. 853-862
    • Chiquet-Ehrismann, R.1
  • 4
    • 0038236713 scopus 로고    scopus 로고
    • Tenascins: Regulation and putative functions during pathological stress
    • Chiquet-Ehrismann, R. and Chiquet, M. (2003). Tenascins: regulation and putative functions during pathological stress. J. Pathol. 4, 488-499.
    • (2003) J. Pathol. , vol.4 , pp. 488-499
    • Chiquet-Ehrismann, R.1    Chiquet, M.2
  • 6
    • 0031813775 scopus 로고    scopus 로고
    • Identification of osteopontin as a novel ligand for the integrin alpha8 beta1 and potential roles for this integrin-ligand interaction in kidney morphogenesis
    • Denda, S., Reichardt, L. F. and Muller, U. (1998). Identification of osteopontin as a novel ligand for the integrin alpha8 beta1 and potential roles for this integrin-ligand interaction in kidney morphogenesis. Mol. Biol. Cell 9, 1425-1435.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1425-1435
    • Denda, S.1    Reichardt, L.F.2    Muller, U.3
  • 7
    • 0033179677 scopus 로고    scopus 로고
    • Cell adhesion to tenascin-X mapping of adhesion sites and identification of integrin receptors
    • Elefteriou, F., Exposito, J. Y., Garrone, R. and Lethias, C. (1999). Cell adhesion to tenascin-X mapping of adhesion sites and identification of integrin receptors. Eur. J. Biochem. 263, 840-848.
    • (1999) Eur. J. Biochem. , vol.263 , pp. 840-848
    • Elefteriou, F.1    Exposito, J.Y.2    Garrone, R.3    Lethias, C.4
  • 8
    • 0030297699 scopus 로고    scopus 로고
    • Domain organizations of modular extracellular matrix proteins and their evolution
    • Engel, J. (1996). Domain organizations of modular extracellular matrix proteins and their evolution. Matrix Biol. 15, 295-299.
    • (1996) Matrix Biol. , vol.15 , pp. 295-299
    • Engel, J.1
  • 9
    • 0027685702 scopus 로고
    • Tenascin-C, tenascin-R and tenascin-X: A family of talented proteins in search of functions
    • Erickson, H. P. (1993). Tenascin-C, tenascin-R and tenascin-X: a family of talented proteins in search of functions. Curr. Opin. Cell Biol. 5, 869-876.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 869-876
    • Erickson, H.P.1
  • 10
    • 0021166341 scopus 로고
    • A six-armed oligomer isolated from cell surface fibronectin preparations
    • Erickson, H. P. and Inglesias, J. L. (1984). A six-armed oligomer isolated from cell surface fibronectin preparations. Nature 311, 267-269.
    • (1984) Nature , vol.311 , pp. 267-269
    • Erickson, H.P.1    Inglesias, J.L.2
  • 11
    • 0028813381 scopus 로고
    • A single heparin binding region within the fibrinogen-like domain is functional in chick tenascin-C
    • Fischer, D., Chiquet-Ehrismann, R., Bernasconi, C. and Chiquet, M. (1995). A single heparin binding region within the fibrinogen-like domain is functional in chick tenascin-C. J. Biol. Chem. 270, 3378-3384.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3378-3384
    • Fischer, D.1    Chiquet-Ehrismann, R.2    Bernasconi, C.3    Chiquet, M.4
  • 12
    • 0030851834 scopus 로고    scopus 로고
    • Cell-adhesive responses to tenascin-C splice variants involve formation of fascin microspikes
    • Fischer, D., Tucker, R. P., Chiquet-Ehrismann, R. and Adams, J. C. (1997). Cell-adhesive responses to tenascin-C splice variants involve formation of fascin microspikes. Mol. Biol. Cell 8, 2055-2075.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2055-2075
    • Fischer, D.1    Tucker, R.P.2    Chiquet-Ehrismann, R.3    Adams, J.C.4
  • 13
    • 0029822205 scopus 로고    scopus 로고
    • Tenascin-Y: A protein of novel domain structure is secreted by differentiated fibroblasts of muscle connective tissue
    • Hagios, C., Koch, M., Spring, J., Chiquet, M. and Chiquet-Ehrismann, R. (1996). Tenascin-Y: a protein of novel domain structure is secreted by differentiated fibroblasts of muscle connective tissue. J. Cell Biol. 134, 1499-1512.
    • (1996) J. Cell Biol. , vol.134 , pp. 1499-1512
    • Hagios, C.1    Koch, M.2    Spring, J.3    Chiquet, M.4    Chiquet-Ehrismann, R.5
  • 14
    • 0035576810 scopus 로고    scopus 로고
    • Interference of tenascin-C with syndecan-4 binding to fibronectin blocks cell adhesion and stimulates tumor cell proliferation
    • Huang, W., Chiquet-Ehrismann, R., Moyano, J. V., Garcia-Pardo, A. and Orend, G. (2001). Interference of tenascin-C with syndecan-4 binding to fibronectin blocks cell adhesion and stimulates tumor cell proliferation. Cancer Res. 61, 8586-8594.
    • (2001) Cancer Res. , vol.61 , pp. 8586-8594
    • Huang, W.1    Chiquet-Ehrismann, R.2    Moyano, J.V.3    Garcia-Pardo, A.4    Orend, G.5
  • 15
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes, R. O. (2002). Integrins: bidirectional, allosteric signaling machines. Cell 110, 673-687
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 16
    • 0032517136 scopus 로고    scopus 로고
    • Structural analysis of mouse tenascin-X: Evolutionary aspects of reduplication of FNIII repeats in the tenascin gene family
    • Ikuta, T., Sogawa, N., Ariga, H., Ikemura, T. and Matsumoto, K. (1998). Structural analysis of mouse tenascin-X: evolutionary aspects of reduplication of FNIII repeats in the tenascin gene family. Gene 217, 1-13.
    • (1998) Gene , vol.217 , pp. 1-13
    • Ikuta, T.1    Sogawa, N.2    Ariga, H.3    Ikemura, T.4    Matsumoto, K.5
  • 17
    • 0034117025 scopus 로고    scopus 로고
    • The tenascin family of ECM glycoproteins: Structure, function, and regulation during embryonic development and tissue remodeling
    • Jones, F. S. and Jones, P. L. (2000a). The tenascin family of ECM glycoproteins: structure, function, and regulation during embryonic development and tissue remodeling. Dev. Dyn. 218, 235-259.
    • (2000) Dev. Dyn. , vol.218 , pp. 235-259
    • Jones, F.S.1    Jones, P.L.2
  • 18
    • 0033731472 scopus 로고    scopus 로고
    • Tenascin-C in development and disease: Gene regulation and cell function
    • Jones, F. S. and Jones, P. L. (2000b). Tenascin-C in development and disease: gene regulation and cell function. Matrix Biol. 19, 581-596.
    • (2000) Matrix Biol. , vol.19 , pp. 581-596
    • Jones, F.S.1    Jones, P.L.2
  • 19
    • 0032562663 scopus 로고    scopus 로고
    • Tenascin-C hexabrachion assembly is a sequential two-step process initiated by coiled-coil alpha-helices
    • Kammerer, R. A., Schulthess, T., Landwehr, R., Lustig, A., Fischer, D. and Engel, J. (1998). Tenascin-C hexabrachion assembly is a sequential two-step process initiated by coiled-coil alpha-helices. J. Biol. Chem. 273, 10602-10608.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10602-10608
    • Kammerer, R.A.1    Schulthess, T.2    Landwehr, R.3    Lustig, A.4    Fischer, D.5    Engel, J.6
  • 22
    • 0033491886 scopus 로고    scopus 로고
    • The tenascin-C knockout revisited
    • Mackie, E. J., and Tucker, R. P. (1999). The tenascin-C knockout revisited. J. Cell Sci. 112, 3847-3853.
    • (1999) J. Cell Sci. , vol.112 , pp. 3847-3853
    • Mackie, E.J.1    Tucker, R.P.2
  • 23
    • 0036544872 scopus 로고    scopus 로고
    • Tenascin-X deficiency mimics Ehlers-Danlos syndrome in mice through alteration of collagen deposition
    • Mao, J. R., Taylor, G., Dean, W. B., Wagner, D. R., Afzal, V., Lotz, J. C., Rubin, E. M. and Bristow, J. (2002). Tenascin-X deficiency mimics Ehlers-Danlos syndrome in mice through alteration of collagen deposition. Nat. Genet. 30, 421-425.
    • (2002) Nat. Genet. , vol.30 , pp. 421-425
    • Mao, J.R.1    Taylor, G.2    Dean, W.B.3    Wagner, D.R.4    Afzal, V.5    Lotz, J.C.6    Rubin, E.M.7    Bristow, J.8
  • 24
    • 0028353447 scopus 로고
    • The distribution of tenascin-X is distinct and often reciprocal to that of tenascin-C
    • Matsumoto, K., Saga, Y., Ikemura, T., Sakakura, T. and Chiquet-Ehrismann, R. (1994). The distribution of tenascin-X is distinct and often reciprocal to that of tenascin-C. J. Cell Biol. 125, 483-493.
    • (1994) J. Cell Biol. , vol.125 , pp. 483-493
    • Matsumoto, K.1    Saga, Y.2    Ikemura, T.3    Sakakura, T.4    Chiquet-Ehrismann, R.5
  • 25
    • 0030663082 scopus 로고    scopus 로고
    • Long and short splice variants of human tenascin differentially regulate neurite outgrowth
    • Meiners, S. and Geller, H. M. (1997). Long and short splice variants of human tenascin differentially regulate neurite outgrowth. Mol. Cell. Neurosci. 10, 100-116.
    • (1997) Mol. Cell. Neurosci. , vol.10 , pp. 100-116
    • Meiners, S.1    Geller, H.M.2
  • 26
    • 0035939656 scopus 로고    scopus 로고
    • Mystery solved: Discovery of a novel integrin ligand in the developing kidney
    • Miner, J. H. (2001). Mystery solved: discovery of a novel integrin ligand in the developing kidney. J. Cell Biol. 154, 447-458.
    • (2001) J. Cell Biol. , vol.154 , pp. 447-458
    • Miner, J.H.1
  • 27
    • 0028989653 scopus 로고
    • Integrin alpha 8 beta 1 promotes attachment, cell spreading, and neurite outgrowth on fibronectin
    • Muller, U., Bossy, B., Venstrom, K. and Reichardt, L. E. (1995). Integrin alpha 8 beta 1 promotes attachment, cell spreading, and neurite outgrowth on fibronectin. Mol. Biol. Cell 6, 433-448.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 433-448
    • Muller, U.1    Bossy, B.2    Venstrom, K.3    Reichardt, L.E.4
  • 28
    • 0030614865 scopus 로고    scopus 로고
    • Integrin alpha8beta1 is critically important for epithelial-mesenchymal interactions during kidney morphogenesis
    • Muller, U., Wang, D., Denda, S., Meness, J. J., Pedersen, R. A. and Reichardt, L. F. (1997). Integrin alpha8beta1 is critically important for epithelial-mesenchymal interactions during kidney morphogenesis. Cell 88, 603-613.
    • (1997) Cell , vol.88 , pp. 603-613
    • Muller, U.1    Wang, D.2    Denda, S.3    Meness, J.J.4    Pedersen, R.A.5    Reichardt, L.F.6
  • 29
    • 0026633247 scopus 로고
    • The chicken neural extracellular matrix molecule restrictin: Similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs
    • Norenberg, U., Wille, H., Wolff, J. M., Frank, R. and Rathjen, F. G. (1992). The chicken neural extracellular matrix molecule restrictin: similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs. Neuron 8, 849-863.
    • (1992) Neuron. , vol.8 , pp. 849-863
    • Norenberg, U.1    Wille, H.2    Wolff, J.M.3    Frank, R.4    Rathjen, F.G.5
  • 30
    • 0025744729 scopus 로고
    • Restrictin: A chick neural extracellular matrix protein involved in cell attachment co-purifies with the cell recognition molecule F11
    • Rathjen, F. G., Wolff, J. M. and Chiquet-Ehrismann, R. (1991). Restrictin: a chick neural extracellular matrix protein involved in cell attachment co-purifies with the cell recognition molecule F11. Development 113, 151-164.
    • (1991) Development , vol.113 , pp. 151-164
    • Rathjen, F.G.1    Wolff, J.M.2    Chiquet-Ehrismann, R.3
  • 32
    • 0028981367 scopus 로고
    • The human integrin alpha 8 beta 1 functions as a receptor for tenascin, fibronectin, and vitronectin
    • Schnapp, L. M., Hatch, N., Ramos, D. M., Klimanskaya, I. V., Sheppard, D. and Pytela, R. (1995a). The human integrin alpha 8 beta 1 functions as a receptor for tenascin, fibronectin, and vitronectin. J. Biol. Chem. 270, 23196-23202.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23196-23202
    • Schnapp, L.M.1    Hatch, N.2    Ramos, D.M.3    Klimanskaya, I.V.4    Sheppard, D.5    Pytela, R.6
  • 33
    • 0028939758 scopus 로고
    • Sequence and tissue distribution of the human integrin alpha 8 subunit: A beta 1-associated alpha subunit expressed in smooth muscle cells
    • Schnapp, L. M., Breuss, J. M., Ramos, D. M., Sheppard, D. and Pytela, R. (1995b). Sequence and tissue distribution of the human integrin alpha 8 subunit: a beta 1-associated alpha subunit expressed in smooth muscle cells. J. Cell Sci. 108, 537-544.
    • (1995) J. Cell Sci. , vol.108 , pp. 537-544
    • Schnapp, L.M.1    Breuss, J.M.2    Ramos, D.M.3    Sheppard, D.4    Pytela, R.5
  • 34
    • 0035160092 scopus 로고    scopus 로고
    • Teneurin-2 is expressed in tissues that regulate limb and somite pattern formation and is induced in vitro and in situ by FGF8
    • Tucker, R. P., Chiquet-Ehrismann, R., Chevron, M. P., Martin, D., Hall, R. J. and Rubin, B. P. (2001a). Teneurin-2 is expressed in tissues that regulate limb and somite pattern formation and is induced in vitro and in situ by FGF8. Dev. Dyn. 220, 27-39.
    • (2001) Dev. Dyn. , vol.220 , pp. 27-39
    • Tucker, R.P.1    Chiquet-Ehrismann, R.2    Chevron, M.P.3    Martin, D.4    Hall, R.J.5    Rubin, B.P.6
  • 35
    • 0035499672 scopus 로고    scopus 로고
    • Tenascin-Y is concentrated in adult nerve roots and has barrier properties in vitro
    • Tucker, R. P., Hagios, C., Santiago, A. and Chiquet-Ehrismann, R. (2001b). Tenascin-Y is concentrated in adult nerve roots and has barrier properties in vitro. J. Neurosci. Res. 66, 439-447.
    • (2001) J. Neurosci. Res. , vol.66 , pp. 439-447
    • Tucker, R.P.1    Hagios, C.2    Santiago, A.3    Chiquet-Ehrismann, R.4
  • 36
    • 0031970896 scopus 로고    scopus 로고
    • Zebrafish tenascin-W, a new member of the tenascin family
    • Weber, P., Montag, D., Schachner, M. and Bernhardt, R. R. (1998). Zebrafish tenascin-W, a new member of the tenascin family. J. Neurobiol. 35, 1-16.
    • (1998) J. Neurobiol. , vol.35 , pp. 1-16
    • Weber, P.1    Montag, D.2    Schachner, M.3    Bernhardt, R.R.4
  • 38
    • 0027445532 scopus 로고
    • Detection of messenger RNA by in situ hybridization to tissue sections and whole mounts
    • Wilkinson, D. G. and Nieto, M. A. (1993). Detection of messenger RNA by in situ hybridization to tissue sections and whole mounts. Methods Enzymol. 225, 361-373.
    • (1993) Methods Enzymol. , vol.225 , pp. 361-373
    • Wilkinson, D.G.1    Nieto, M.A.2
  • 39
    • 0028171068 scopus 로고
    • The integrin alpha 9 beta 1 mediates cell attachment to a non-RGD site in the third fibronectin type III repeat of tenascin
    • Yokosaki, Y., Palmer, E. L., Prieto, A. L., Crossin, K. L., Bourdon, M. A., Pytela, R. and Sheppard, D. (1994). The integrin alpha 9 beta 1 mediates cell attachment to a non-RGD site in the third fibronectin type III repeat of tenascin. J. Biol. Chem. 269, 26691-26696.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26691-26696
    • Yokosaki, Y.1    Palmer, E.L.2    Prieto, A.L.3    Crossin, K.L.4    Bourdon, M.A.5    Pytela, R.6    Sheppard, D.7
  • 40
    • 0032496223 scopus 로고    scopus 로고
    • Identification of the ligand binding site for the integrin alpha9 beta1 in the third fibronectin type III repeat of tenascin-C
    • Yokosaki, Y., Matsuura, N., Higashiyama, S., Murakami, I., Obara, M., Yamakido, M., Shigeto, N., Chen, J. and Sheppard, D. (1998). Identification of the ligand binding site for the integrin alpha9 beta1 in the third fibronectin type III repeat of tenascin-C. J. Biol. Chem. 273, 11423-11428.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11423-11428
    • Yokosaki, Y.1    Matsuura, N.2    Higashiyama, S.3    Murakami, I.4    Obara, M.5    Yamakido, M.6    Shigeto, N.7    Chen, J.8    Sheppard, D.9


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