메뉴 건너뛰기




Volumn 253, Issue 2, 1999, Pages 607-617

Tenascin-Y, a component of distinctive connective tissues, supports muscle cell growth

Author keywords

Cell adhesion; Differentiation; Expression pattern; Integrin; Tissue distribution

Indexed keywords

TENASCIN;

EID: 0033572767     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1999.4658     Document Type: Article
Times cited : (19)

References (36)
  • 2
    • 0028170207 scopus 로고
    • The regulation of alpha 5 beta 1 integrin expression in human muscle cells
    • Blaschuk K. L., Holland P. C. The regulation of alpha 5 beta 1 integrin expression in human muscle cells. Dev. Biol. 164:1994;475-483.
    • (1994) Dev. Biol. , vol.164 , pp. 475-483
    • Blaschuk, K.L.1    Holland, P.C.2
  • 4
    • 0027231385 scopus 로고
    • Tenascin-X: A novel extracellular matrix protein encoded by the human XB gene overlapping P450c21B
    • Bristow J., Tee M. K., Gitelman S. E., Mellon S. H., Miller W. L. Tenascin-X: A novel extracellular matrix protein encoded by the human XB gene overlapping P450c21B. J. Cell Biol. 122:1993;265-278.
    • (1993) J. Cell Biol. , vol.122 , pp. 265-278
    • Bristow, J.1    Tee, M.K.2    Gitelman, S.E.3    Mellon, S.H.4    Miller, W.L.5
  • 5
    • 0029142882 scopus 로고
    • Embryonic expression of tenascin-X suggests a role in limb, muscle, and heart development
    • Burch G. H., Bedolli M. A., McDonough S., Rosenthal S. M., Bristow J. Embryonic expression of tenascin-X suggests a role in limb, muscle, and heart development. Dev. Dynam. 203:1995;491-504.
    • (1995) Dev. Dynam. , vol.203 , pp. 491-504
    • Burch, G.H.1    Bedolli, M.A.2    McDonough, S.3    Rosenthal, S.M.4    Bristow, J.5
  • 7
    • 0018800306 scopus 로고
    • Developmental regulation of creatine kinase isoenzymes in myogenic cell cultures from chicken: Biosynthesis of creatine kinase subunits M and B
    • Caravatti M., Perriard J. C., Eppenberger H. M. Developmental regulation of creatine kinase isoenzymes in myogenic cell cultures from chicken: Biosynthesis of creatine kinase subunits M and B. J. Biol. Chem. 254:1979;1388-1394.
    • (1979) J. Biol. Chem. , vol.254 , pp. 1388-1394
    • Caravatti, M.1    Perriard, J.C.2    Eppenberger, H.M.3
  • 8
    • 0018419829 scopus 로고
    • Fibronectin mediates attachment of chicken myoblasts to a gelatin-coated substratum
    • Chiquet M., Puri E. C., Turner D. C. Fibronectin mediates attachment of chicken myoblasts to a gelatin-coated substratum. J. Biol. Chem. 254:1979;5475-5482.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5475-5482
    • Chiquet, M.1    Puri, E.C.2    Turner, D.C.3
  • 9
    • 0021270360 scopus 로고
    • Chick myotendinous antigen. I. A monoclonal antibody as a marker for tendon and muscle morphogenesis
    • Chiquet M., Fambrough D. M. Chick myotendinous antigen. I. A monoclonal antibody as a marker for tendon and muscle morphogenesis. J. Cell. Biol. 98:1984;1926-1936.
    • (1984) J. Cell. Biol. , vol.98 , pp. 1926-1936
    • Chiquet, M.1    Fambrough, D.M.2
  • 10
    • 0025736963 scopus 로고
    • Isolation of chick tenascin variants and fragments: A C-terminal heparin-binding fragment produced by cleavage of the extra domain from the largest subunit splicing variant
    • Chiquet M., Vrucinic-Filipi N., Schenk S., Beck K., Chiquet-Ehrismann R. Isolation of chick tenascin variants and fragments: A C-terminal heparin-binding fragment produced by cleavage of the extra domain from the largest subunit splicing variant. Eur. J. Biochem. 199:1991;379-388.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 379-388
    • Chiquet, M.1    Vrucinic-Filipi, N.2    Schenk, S.3    Beck, K.4    Chiquet-Ehrismann, R.5
  • 11
    • 0028859440 scopus 로고
    • Tenascins, a growing family of extracellular matrix proteins
    • Chiquet-Ehrismann R. Tenascins, a growing family of extracellular matrix proteins. Experientia. 51:1995;853-862.
    • (1995) Experientia , vol.51 , pp. 853-862
    • Chiquet-Ehrismann, R.1
  • 14
    • 0019395642 scopus 로고
    • The Mr 165,000 M-protein myomesin: A specific protein of cross-striated muscle cells
    • Eppenberger H. M., Perriard J. C., Rosenberg U. B., Strehler E. E. The Mr 165,000 M-protein myomesin: A specific protein of cross-striated muscle cells. J. Cell Biol. 89:1981;185-193.
    • (1981) J. Cell Biol. , vol.89 , pp. 185-193
    • Eppenberger, H.M.1    Perriard, J.C.2    Rosenberg, U.B.3    Strehler, E.E.4
  • 15
    • 0028694581 scopus 로고
    • Evolution of the tenascin family - Implications for function of the C-terminal fibrinogen-like domain
    • Erickson H. P. Evolution of the tenascin family - implications for function of the C-terminal fibrinogen-like domain. Perspect. Dev. Neurobiol. 2:1994;9-19.
    • (1994) Perspect. Dev. Neurobiol. , vol.2 , pp. 9-19
    • Erickson, H.P.1
  • 16
    • 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., Chiquet M. A single heparin binding region within the fibrinogen-like domain is functional in chick tenascin-C. J. Biol. Chem. 270:1995;3378-3384.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3378-3384
    • Fischer, D.1    Chiquet-Ehrismann, R.2    Bernasconi, C.3    Chiquet, M.4
  • 17
    • 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., Adams J. C. Cell-adhesive responses to tenascin-C splice variants involve formation of fascin microspikes. Mol. Biol. Cell. 8:1997;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
  • 18
    • 0032935413 scopus 로고    scopus 로고
    • Modulation of cell proliferation and differentiation through substrate-dependent changes in fibronectin conformation
    • Garcia A. J., Vega M. D., Boettiger D. Modulation of cell proliferation and differentiation through substrate-dependent changes in fibronectin conformation. Mol. Biol. Cell. 10:1999;785-798.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 785-798
    • Garcia, A.J.1    Vega, M.D.2    Boettiger, D.3
  • 19
    • 0029072597 scopus 로고
    • Distinct tissue distribution in pigs of tenascin-X and tenascin-C transcripts
    • Geffrotin C., Garrido J. J., Tremet L., Vaiman M. Distinct tissue distribution in pigs of tenascin-X and tenascin-C transcripts. Eur. J. Biochem. 231:1995;83-92.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 83-92
    • Geffrotin, C.1    Garrido, J.J.2    Tremet, L.3    Vaiman, M.4
  • 21
    • 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., Chiquet-Ehrismann R. Tenascin-Y: A protein of novel domain structure is secreted by differentiated fibroblasts of muscle connective tissue. J. Cell Biol. 134:1996;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
  • 22
    • 0025113405 scopus 로고
    • Identification and characterization of a dimeric chicken fibronectin receptor: Subunit-specific monoclonal antibodies to the putative chicken alpha 5 beta 1 integrin
    • Hofer U., Syfrig J., Chiquet-Ehrismann R. Identification and characterization of a dimeric chicken fibronectin receptor: Subunit-specific monoclonal antibodies to the putative chicken alpha 5 beta 1 integrin. J. Biol. Chem. 265:1990;14561-14565.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14561-14565
    • Hofer, U.1    Syfrig, J.2    Chiquet-Ehrismann, R.3
  • 23
    • 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., Engel J. Tenascin-C hexabrachion assembly is a sequential two-step process initiated by coiled-coil alpha-helices. J. Biol. Chem. 273:1998;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
  • 24
    • 77956990868 scopus 로고
    • Reduction of disulfide bonds in proteins with dithiothreitol
    • Konigsberg W. Reduction of disulfide bonds in proteins with dithiothreitol. Methods Enzymol. 25:1971;185-188.
    • (1971) Methods Enzymol. , vol.25 , pp. 185-188
    • Konigsberg, W.1
  • 25
    • 0029887154 scopus 로고    scopus 로고
    • Flexilin: A new extracellular matrix glycoprotein localized on collagen fibrils
    • Lethias C., Descollonges Y., Boutillon M. M., Garrone R. Flexilin: A new extracellular matrix glycoprotein localized on collagen fibrils. Matrix Biol. 15:1996;11-19.
    • (1996) Matrix Biol. , vol.15 , pp. 11-19
    • Lethias, C.1    Descollonges, Y.2    Boutillon, M.M.3    Garrone, R.4
  • 26
    • 0026606265 scopus 로고
    • Cluster of fibronectin type III repeats found in the human major histocompatibility complex class III region shows the highest homology with the repeats in an extracellular matrix protein, tenascin
    • Matsumoto K., Arai M., Ishihara N., Ando A., Inoko H., Ikemura T. Cluster of fibronectin type III repeats found in the human major histocompatibility complex class III region shows the highest homology with the repeats in an extracellular matrix protein, tenascin. Genomics. 12:1992;485-491.
    • (1992) Genomics , vol.12 , pp. 485-491
    • Matsumoto, K.1    Arai, M.2    Ishihara, N.3    Ando, A.4    Inoko, H.5    Ikemura, T.6
  • 27
    • 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., Chiquet-Ehrismann R. The distribution of tenascin-X is distinct and often reciprocal to that of tenascin-C. J. Cell Biol. 125:1994;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
  • 28
    • 1542382015 scopus 로고
    • Transcript encoded on the opposite strand of the human steroid 21-hydroxylase/complement component C4 gene locus
    • Morel Y., Bristow J., Gitelman S. E., Miller W. L. Transcript encoded on the opposite strand of the human steroid 21-hydroxylase/complement component C4 gene locus. Proc. Natl. Acad. Sci. USA. 86:1989;6582-6586.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6582-6586
    • Morel, Y.1    Bristow, J.2    Gitelman, S.E.3    Miller, W.L.4
  • 29
    • 0026633247 scopus 로고
    • The chicken neural extracellular matrix molecule restrictin: Similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs
    • Nörenberg U., Wille H., Wolff J. M., Frank R., Rathjen F. G. The chicken neural extracellular matrix molecule restrictin: similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs. Neuron. 8:1992;849-863.
    • (1992) Neuron , vol.8 , pp. 849-863
    • Nörenberg, U.1    Wille, H.2    Wolff, J.M.3    Frank, R.4    Rathjen, F.G.5
  • 30
    • 0023875632 scopus 로고
    • Laminin alters cell shape and stimulates motility and proliferation of murine skeletal myoblasts
    • Ocalan M., Goodman S. L., Kuhl U., Hauschka S. D., von der Mark K. Laminin alters cell shape and stimulates motility and proliferation of murine skeletal myoblasts. Dev. Biol. 125:1988;158-167.
    • (1988) Dev. Biol. , vol.125 , pp. 158-167
    • Ocalan, M.1    Goodman, S.L.2    Kuhl, U.3    Hauschka, S.D.4    Von Der Mark, K.5
  • 31
    • 0026856971 scopus 로고
    • Expression of fibronectin, the integrin alpha 5, and alpha-smooth muscle actin in heart and lung development
    • Roman J., McDonald J. A. Expression of fibronectin, the integrin alpha 5, and alpha-smooth muscle actin in heart and lung development. Am. J. Respir. Cell Mol. Biol. 6:1992;472-480.
    • (1992) Am. J. Respir. Cell Mol. Biol. , vol.6 , pp. 472-480
    • Roman, J.1    McDonald, J.A.2
  • 32
    • 0024347096 scopus 로고
    • Two contrary functions of tenascin: Dissection of the active sites by recombinant tenascin fragments
    • Spring J., Beck K., Chiquet-Ehrismann R. Two contrary functions of tenascin: Dissection of the active sites by recombinant tenascin fragments. Cell. 59:1989;325-334.
    • (1989) Cell , vol.59 , pp. 325-334
    • Spring, J.1    Beck, K.2    Chiquet-Ehrismann, R.3
  • 34
    • 0032858637 scopus 로고    scopus 로고
    • Tenascin-Y in the developing and adult avian nervous system
    • Tucker R. P., Hagios C., Chiquet-Ehrismann R. Tenascin-Y in the developing and adult avian nervous system. Dev. Neurosci. 21:1999;126-133.
    • (1999) Dev. Neurosci. , vol.21 , pp. 126-133
    • Tucker, R.P.1    Hagios, C.2    Chiquet-Ehrismann, R.3
  • 35
    • 0024359714 scopus 로고
    • Anatagonistic effects of laminin and fibronectin on the expression of the myogenic phenotype
    • von der Mark K., Ocalan M. Anatagonistic effects of laminin and fibronectin on the expression of the myogenic phenotype. Differentiation. 40:1989;150-157.
    • (1989) Differentiation , vol.40 , pp. 150-157
    • Von Der Mark, K.1    Ocalan, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.