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Volumn 136, Issue 6, 1997, Pages 1349-1361

Progressive kidney degeneration in mice lacking tensin

Author keywords

[No Author keywords available]

Indexed keywords

CELL ADHESION MOLECULE; TENSIN; UNCLASSIFIED DRUG;

EID: 0000710224     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.136.6.1349     Document Type: Article
Times cited : (110)

References (41)
  • 2
    • 0023551350 scopus 로고
    • Cloning and expression of the mouse pgk-1 gene and the nucleotide sequence of its promoter
    • Adra, C.N., P.H. Boer, and M.W. McBurney. 1987. Cloning and expression of the mouse pgk-1 gene and the nucleotide sequence of its promoter. Gene (Amst.). 60:65-74.
    • (1987) Gene (Amst.) , vol.60 , pp. 65-74
    • Adra, C.N.1    Boer, P.H.2    McBurney, M.W.3
  • 3
    • 0029833286 scopus 로고    scopus 로고
    • Platelet-derived growth factor-induced formation of tensin and phosphoinositide 3-kinase complexes
    • Auger, K.R., Z. Songyang, S.H. Lo, T.M. Boberts, and L.B. Chen. 1996. Platelet-derived growth factor-induced formation of tensin and phosphoinositide 3-kinase complexes. J. Biol. Chem. 271:23452-23457.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23452-23457
    • Auger, K.R.1    Songyang, Z.2    Lo, S.H.3    Boberts, T.M.4    Chen, L.B.5
  • 4
    • 0027227263 scopus 로고
    • Cell spreading on extracellular matrix proteins induces tyrosine phosphorylation of tensin
    • Bockholt, S.M., and K. Burridge. 1993. Cell spreading on extracellular matrix proteins induces tyrosine phosphorylation of tensin. J. Biol. Chem. 268:14565-14567.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14565-14567
    • Bockholt, S.M.1    Burridge, K.2
  • 5
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cyloskeleton
    • Burridge, K., K. Fath, T. Kelly, G. Nuckolls, and C. Turner. 1988. Focal adhesions: transmembrane junctions between the extracellular matrix and the cyloskeleton. Annu. Rev. Cell Biol. 4:487-525.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, G.4    Turner, C.5
  • 6
    • 0030036465 scopus 로고    scopus 로고
    • PTP-NP, a new member of the receptor protein tyrosine phophatase family, implicated in development of nervous system and pancreatic endocrine cells
    • Chiang, M.K., and J.G. Flanagan. 1996. PTP-NP, a new member of the receptor protein tyrosine phophatase family, implicated in development of nervous system and pancreatic endocrine cells. Development (Camb.). 122:2239-2250.
    • (1996) Development (Camb.) , vol.122 , pp. 2239-2250
    • Chiang, M.K.1    Flanagan, J.G.2
  • 7
    • 0028956756 scopus 로고
    • Molecular cloning, expression, and mapping of the high affinity actin-capping domain of chicken cardiac tensin
    • Chuang, J.Z., D.C. Lin, and S. Lin. 1995. Molecular cloning, expression, and mapping of the high affinity actin-capping domain of chicken cardiac tensin. J. Cell Biol. 128:1095-1109.
    • (1995) J. Cell Biol. , vol.128 , pp. 1095-1109
    • Chuang, J.Z.1    Lin, D.C.2    Lin, S.3
  • 9
    • 0029666420 scopus 로고    scopus 로고
    • β4 integrin is required for hemidesmosome formation, cell adhesion and cell survival
    • Dowling, J., Q.C. Yu, and E. Fuchs. 1996. β4 integrin is required for hemidesmosome formation, cell adhesion and cell survival. J. Cell Biol. 134:559-572.
    • (1996) J. Cell Biol. , vol.134 , pp. 559-572
    • Dowling, J.1    Yu, Q.C.2    Fuchs, E.3
  • 10
    • 0030045345 scopus 로고    scopus 로고
    • Origins of cell polarity
    • Drubin, D.G., and W.J. Nelson. 1996. Origins of cell polarity. Cell. 84:335-344.
    • (1996) Cell , vol.84 , pp. 335-344
    • Drubin, D.G.1    Nelson, W.J.2
  • 11
    • 0029068244 scopus 로고
    • Apical, basal, and lateral cues for epithelial polarization
    • Eaton, E., and K. Simons. 1995. Apical, basal, and lateral cues for epithelial polarization. Cell. 82:5-8.
    • (1995) Cell , vol.82 , pp. 5-8
    • Eaton, E.1    Simons, K.2
  • 12
    • 0028979154 scopus 로고
    • Consequences of lack of β1 integrin gene expression in mice
    • Fassler, R., and M. Meyer. 1995. Consequences of lack of β1 integrin gene expression in mice. Genes & Dev. 9:1896-1908.
    • (1995) Genes & Dev. , vol.9 , pp. 1896-1908
    • Fassler, R.1    Meyer, M.2
  • 13
    • 0028783271 scopus 로고
    • Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK
    • Furuta, Y., D. Ilic, S. Kanazawa, N. Takeda, T. Yamamoto, and S. Aizawa. 1995. Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK. Oncogene. 11:1989-1995.
    • (1995) Oncogene , vol.11 , pp. 1989-1995
    • Furuta, Y.1    Ilic, D.2    Kanazawa, S.3    Takeda, N.4    Yamamoto, T.5    Aizawa, S.6
  • 15
    • 0024382542 scopus 로고
    • Novel tyrosine kinase substrates from Rous sarcoma virus-transformed cells are present in the membrane skeleton
    • Glenney, J., and L. Zokas. 1989. Novel tyrosine kinase substrates from Rous sarcoma virus-transformed cells are present in the membrane skeleton. J. Cell Biol. 108:2401-2408.
    • (1989) J. Cell Biol. , vol.108 , pp. 2401-2408
    • Glenney, J.1    Zokas, L.2
  • 16
    • 0024095524 scopus 로고
    • The role of the cell adhesion molecule uvomorulin in the formation and maintenance of the epithelial junctional complex
    • Gumbiner, B., B. Stevenson, and A. Grimaldi. 1988. The role of the cell adhesion molecule uvomorulin in the formation and maintenance of the epithelial junctional complex. J. Cell Biol. 107:1575-1588.
    • (1988) J. Cell Biol. , vol.107 , pp. 1575-1588
    • Gumbiner, B.1    Stevenson, B.2    Grimaldi, A.3
  • 17
    • 0029066406 scopus 로고
    • Gene targeting of BPAG1: Abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration
    • Guo, L., L. Degenstein, J. Dowling, Q.C. Yu, R. Wollmann, B. Perman, and E. Fuchs. 1995. Gene targeting of BPAG1: abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration. Cell. 81:233-244.
    • (1995) Cell , vol.81 , pp. 233-244
    • Guo, L.1    Degenstein, L.2    Dowling, J.3    Yu, Q.C.4    Wollmann, R.5    Perman, B.6    Fuchs, E.7
  • 18
    • 0022534722 scopus 로고
    • Interactions of plasma membrane fibronectin receptor with talin - A transmembrane linkage
    • Horwitz, A., K. Duggan, C. Buck, M.C. Beckerle, and K. Burridge. 1986. Interactions of plasma membrane fibronectin receptor with talin - a transmembrane linkage. Nature (Lond.). 320:531-533.
    • (1986) Nature (Lond.) , vol.320 , pp. 531-533
    • Horwitz, A.1    Duggan, K.2    Buck, C.3    Beckerle, M.C.4    Burridge, K.5
  • 19
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R.O. 1992. Integrins: versatility, modulation, and signaling in cell adhesion. Cell. 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 22
    • 0025376378 scopus 로고
    • Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases
    • Kanner, S.B., A.B. Reynolds, R.R. Vines, and J.T. Parsons. 1990. Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases. Proc. Natl. Acad. Sci. USA. 87:3328-3332.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3328-3332
    • Kanner, S.B.1    Reynolds, A.B.2    Vines, R.R.3    Parsons, J.T.4
  • 23
    • 0023709019 scopus 로고
    • Role of laminin A chain in the development of epithelial cell polarity
    • Klein, G., M. Langegger, R. Timpl, and P. Ekblom. 1988. Role of laminin A chain in the development of epithelial cell polarity. Cell. 55:331-341.
    • (1988) Cell , vol.55 , pp. 331-341
    • Klein, G.1    Langegger, M.2    Timpl, R.3    Ekblom, P.4
  • 25
    • 0000488695 scopus 로고
    • Interaction of tensin with actin and identification of its three distinct actin-binding domains
    • Lo, S.H., P.A. Janmey, J.H. Hartwig, and L.B. Chen. 1994b. Interaction of tensin with actin and identification of its three distinct actin-binding domains. J. Cell. Biol. 125:1067-1075.
    • (1994) J. Cell. Biol. , vol.125 , pp. 1067-1075
    • Lo, S.H.1    Janmey, P.A.2    Hartwig, J.H.3    Chen, L.B.4
  • 26
    • 0028533592 scopus 로고
    • Tensin: A potential link between the cytoskeleton and signal transduction
    • Lo, S.H., E. Weisberg, and L.B. Chen. 1994c. Tensin: a potential link between the cytoskeleton and signal transduction. Bioessays. 16:817-823.
    • (1994) Bioessays , vol.16 , pp. 817-823
    • Lo, S.H.1    Weisberg, E.2    Chen, L.B.3
  • 27
    • 0028954797 scopus 로고
    • Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
    • Miyamoto, S., S.K. Akiyama, and K.M. Yamada. 1995. Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science (Wash. DC). 267:883-885.
    • (1995) Science (Wash. DC) , vol.267 , pp. 883-885
    • Miyamoto, S.1    Akiyama, S.K.2    Yamada, K.M.3
  • 28
    • 0028324407 scopus 로고
    • Regulation of epithelial cell surface polarity reversal by β1 integrins
    • Ojakian, G.K., and R. Schwimmer. 1994. Regulation of epithelial cell surface polarity reversal by β1 integrins. J. Cell Sci. 107:561-576.
    • (1994) J. Cell Sci. , vol.107 , pp. 561-576
    • Ojakian, G.K.1    Schwimmer, R.2
  • 29
    • 0025291522 scopus 로고
    • An interaction between α-actinin and β1 integrin subunit in vitro
    • Otey, C.A., F.M. Pavalko, and K. Burridge. 1990. An interaction between α-actinin and β1 integrin subunit in vitro. J. Cell Biol. 111:721-729.
    • (1990) J. Cell Biol. , vol.111 , pp. 721-729
    • Otey, C.A.1    Pavalko, F.M.2    Burridge, K.3
  • 30
    • 0027990414 scopus 로고
    • A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner
    • Sakai, R., A. Iwamatsu, N. Hirano, S. Ogawa, T. Tanaka, H. Mano, Y. Yazaki, and H. Hirai. 1994. A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner. EMBO (Eur. Mol. Biol. Organ.) J. 13:3748-3756.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 3748-3756
    • Sakai, R.1    Iwamatsu, A.2    Hirano, N.3    Ogawa, S.4    Tanaka, T.5    Mano, H.6    Yazaki, Y.7    Hirai, H.8
  • 31
    • 0028875460 scopus 로고
    • Increased tyrosine phosphorylation of focal adhesion proteins in myeloid cell lines expressing p210BCR/ABL
    • Salgia, R., B. Brunkhorst, E. Pisick, J.L. Li, S.H. Lo, L.B. Chen, and J.D. Griffin. 1995. Increased tyrosine phosphorylation of focal adhesion proteins in myeloid cell lines expressing p210BCR/ABL. Oncogene. 11:1149-1155.
    • (1995) Oncogene , vol.11 , pp. 1149-1155
    • Salgia, R.1    Brunkhorst, B.2    Pisick, E.3    Li, J.L.4    Lo, S.H.5    Chen, L.B.6    Griffin, J.D.7
  • 33
    • 0025148993 scopus 로고
    • Recognition of laminin E8 cell-binding site by an integrin possessing the α6 subunit is essential for epithelial polarization in developing kidney tubules
    • Sorokin, L., A. Sonnenberg, M. Aumailley, R. Timpl, and P. Ekblom. 1990. Recognition of laminin E8 cell-binding site by an integrin possessing the α6 subunit is essential for epithelial polarization in developing kidney tubules. J. Cell Biol. 111:1265-1273.
    • (1990) J. Cell Biol. , vol.111 , pp. 1265-1273
    • Sorokin, L.1    Sonnenberg, A.2    Aumailley, M.3    Timpl, R.4    Ekblom, P.5
  • 36
    • 0030015434 scopus 로고    scopus 로고
    • Epithelial detachment due to absence of hemidesmosomes in integrin β4 null mice
    • Van der Neut, R., P. Krimpenfort, J. Calafat, C. Niessen, and A. Sonnenberg. 1996. Epithelial detachment due to absence of hemidesmosomes in integrin β4 null mice. Nat. Genet. 13:366-369.
    • (1996) Nat. Genet. , vol.13 , pp. 366-369
    • Van Der Neut, R.1    Krimpenfort, P.2    Calafat, J.3    Niessen, C.4    Sonnenberg, A.5
  • 37
    • 0023198134 scopus 로고
    • Formation of the apical pole of epithelial (Madin-Darby canine kidney) cells: Polarity of an apical protein is independent of tight junctions while segregation of a basolateral marker requires cell-cell interactions
    • Vega-Salas, D.E., P.J. Salas, D. Gundersen, and E. Rodriguez-Boulan. 1987. Formation of the apical pole of epithelial (Madin-Darby canine kidney) cells: polarity of an apical protein is independent of tight junctions while segregation of a basolateral marker requires cell-cell interactions. J. Cell Biol. 104:905-916.
    • (1987) J. Cell Biol. , vol.104 , pp. 905-916
    • Vega-Salas, D.E.1    Salas, P.J.2    Gundersen, D.3    Rodriguez-Boulan, E.4
  • 38
    • 0027427492 scopus 로고
    • Bcl-2-deficient mice demonstrate fulminant lymphoid apoptosis, polycystic kidneys, and hypopigmented hair
    • Veis, D.J., C.M. Sorenson, J.R. Shutter, and S.J. Korsmeyer. 1993. Bcl-2-deficient mice demonstrate fulminant lymphoid apoptosis, polycystic kidneys, and hypopigmented hair. Cell. 75:229-240.
    • (1993) Cell , vol.75 , pp. 229-240
    • Veis, D.J.1    Sorenson, C.M.2    Shutter, J.R.3    Korsmeyer, S.J.4
  • 39
    • 0025023525 scopus 로고
    • Steps in the morphogenesis of a polarized epithelium. I. Uncoupling the roles of cell-cell and cell-substratum contact in establishing plasma membrane polarity in multicellular epithelial (MDCK) cysts
    • Wang, A.Z., G.K. Ojakian, and W.J. Nelson. 1990a. Steps in the morphogenesis of a polarized epithelium. I. Uncoupling the roles of cell-cell and cell-substratum contact in establishing plasma membrane polarity in multicellular epithelial (MDCK) cysts. J. Cell Sci. 95:137-151.
    • (1990) J. Cell Sci. , vol.95 , pp. 137-151
    • Wang, A.Z.1    Ojakian, G.K.2    Nelson, W.J.3
  • 40
    • 0025191452 scopus 로고
    • Steps in the morphogenesis of a polarized epithelium. II. Disassembly and assembly of plasma membrane domains during reversal of epithelial cell polarity in multicellular epithelial (MDCK) cysts
    • Wang, A.Z., G.K. Ojakian, and W.J. Nelson. 1990b. Steps in the morphogenesis of a polarized epithelium. II. Disassembly and assembly of plasma membrane domains during reversal of epithelial cell polarity in multicellular epithelial (MDCK) cysts. J. Cell Sci. 95:153-165.
    • (1990) J. Cell Sci. , vol.95 , pp. 153-165
    • Wang, A.Z.1    Ojakian, G.K.2    Nelson, W.J.3
  • 41
    • 0002715815 scopus 로고    scopus 로고
    • Desmosomal disorganization and epidermal abnormalities in transgenic mouse expressing mutant desmoglein-3
    • Yu, Q.C., E. Allen, and E.V. Fuchs. 1996. Desmosomal disorganization and epidermal abnormalities in transgenic mouse expressing mutant desmoglein-3. Proc. Microscopy Microanalysis. 34-35.
    • (1996) Proc. Microscopy Microanalysis , pp. 34-35
    • Yu, Q.C.1    Allen, E.2    Fuchs, E.V.3


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