메뉴 건너뛰기




Volumn 8, Issue 4, 2003, Pages 409-419

Dystroglycan: Emerging roles in mammary gland function

Author keywords

Breast; Carcinoma; Dystroglycan; Epithelial; Laminin; Mammary

Indexed keywords

ACTIN; AGRIN; AMINO ACID; BIGLYCAN; DYSTROGLYCAN; GLYCOPROTEIN; LAMININ 1; LIGAND; MEMBRANE PROTEIN; MEROSIN; PERLECAN; PROTEIN SH2; PROTEIN SUBUNIT;

EID: 4344637856     PISSN: 10833021     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:JOMG.0000017428.38034.a7     Document Type: Review
Times cited : (18)

References (81)
  • 1
    • 0039827497 scopus 로고
    • Influence of a reconstituted basement membrane and its components on casein gene expression and secretion in mouse mammary epithelial cells
    • M. L. Li, J. Aggeler, D. A. Farson, C. Hatier, J. Hassell, and M. J. Bissell (1987). Influence of a reconstituted basement membrane and its components on casein gene expression and secretion in mouse mammary epithelial cells. Proc. Natl. Acad. Sci. US.A. 84:136-140.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 136-140
    • Li, M.L.1    Aggeler, J.2    Farson, D.A.3    Hatier, C.4    Hassell, J.5    Bissell, M.J.6
  • 2
    • 0024505367 scopus 로고
    • Functional differentiation and alveolar morphogenesis of primary mammary cultures on reconstituted basement membrane
    • M. H. Barcellos-Hoff, J. Aggeler, T. G. Ram, and M. J. Bissell (1989). Functional differentiation and alveolar morphogenesis of primary mammary cultures on reconstituted basement membrane. Development 105:223-235.
    • (1989) Development , vol.105 , pp. 223-235
    • Barcellos-Hoff, M.H.1    Aggeler, J.2    Ram, T.G.3    Bissell, M.J.4
  • 4
    • 0032586951 scopus 로고    scopus 로고
    • Division of labor among the alpha6beta4 integrin, beta1 integrins, and an E3 laminin receptor to signal morphogenesis and beta-casein expression in mammary epithelial cells
    • J. Muschler, A. Lochter, C. D. Roskelley, P. Yurchenco, and M. J. Bissell (1999). Division of labor among the alpha6beta4 integrin, beta1 integrins, and an E3 laminin receptor to signal morphogenesis and beta-casein expression in mammary epithelial cells. Mol. Biol. Cell 10:2817-2828.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2817-2828
    • Muschler, J.1    Lochter, A.2    Roskelley, C.D.3    Yurchenco, P.4    Bissell, M.J.5
  • 5
    • 0036990109 scopus 로고    scopus 로고
    • The organizing principle: Microenvironmental influences in the normal and malignant breast
    • M. J. Bissell, D. C. Radisky, A. Rizki, V. M. Weaver, and O. W. Petersen (2002). The organizing principle: Microenvironmental influences in the normal and malignant breast. Differentiation 70:537-546.
    • (2002) Differentiation , vol.70 , pp. 537-546
    • Bissell, M.J.1    Radisky, D.C.2    Rizki, A.3    Weaver, V.M.4    Petersen, O.W.5
  • 6
    • 0036894605 scopus 로고    scopus 로고
    • A role for dystroglycan in epithelial polarization: Loss of function in breast tumor cells
    • J. Muschler, D. Levy, R. Boudreau, M. Henry, K. Campbell, and M. J. Bissell (2002). A role for dystroglycan in epithelial polarization: Loss of function in breast tumor cells. Cancer Res. 62:7102-7109.
    • (2002) Cancer Res. , vol.62 , pp. 7102-7109
    • Muschler, J.1    Levy, D.2    Boudreau, R.3    Henry, M.4    Campbell, K.5    Bissell, M.J.6
  • 7
    • 0035085253 scopus 로고    scopus 로고
    • Discoidin domain receptor 1 tyrosine kinase has an essential role in mammary gland development
    • W. F. Vogel, A. Aszodi, F. Alves, and T. Pawson (2001). Discoidin domain receptor 1 tyrosine kinase has an essential role in mammary gland development. Mol. Cell Biol. 21:2906-2917.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 2906-2917
    • Vogel, W.F.1    Aszodi, A.2    Alves, F.3    Pawson, T.4
  • 8
    • 0033557707 scopus 로고    scopus 로고
    • Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, suffatides, alpha-dystroglycan and several extracellular matrix proteins
    • J. F. Talts, Z. Andac, W. Gohring, A. Brancaccio, and R. Timpl (1999). Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, suffatides, alpha-dystroglycan and several extracellular matrix proteins. EMBO J. 18:863-870.
    • (1999) EMBO J. , vol.18 , pp. 863-870
    • Talts, J.F.1    Andac, Z.2    Gohring, W.3    Brancaccio, A.4    Timpl, R.5
  • 9
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • J. M. Ervasti and K. P. Campbell (1993). A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J. Cell Biol. 122:809-823.
    • (1993) J. Cell Biol. , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 11
    • 0028178082 scopus 로고
    • Dystroglycan-alpha, a dystrophin-associated glycoprotein, is a functional agrin receptor
    • S. H. Gee, F. Montanaro, M. H. Lindenbaum, and S. Carbonetto (1994). Dystroglycan-alpha, a dystrophin-associated glycoprotein, is a functional agrin receptor. Cell 77:675-686.
    • (1994) Cell , vol.77 , pp. 675-686
    • Gee, S.H.1    Montanaro, F.2    Lindenbaum, M.H.3    Carbonetto, S.4
  • 12
    • 0034695928 scopus 로고    scopus 로고
    • The small leucine-rich repeat proteoglycan biglycan binds to alpha-dystroglycan and is upregulated in dystrophic muscle
    • M. A. Bowe, D. B. Mendis, and J. R. Fallon (2000). The small leucine-rich repeat proteoglycan biglycan binds to alpha-dystroglycan and is upregulated in dystrophic muscle. J. Cell Biol. 148:801-810.
    • (2000) J. Cell Biol. , vol.148 , pp. 801-810
    • Bowe, M.A.1    Mendis, D.B.2    Fallon, J.R.3
  • 13
    • 0031770342 scopus 로고    scopus 로고
    • The relationship between perlecan and dystroglycan and its implication in the formation of the neuromuscular junction
    • H. B. Peng, A. A. Ali, D. F. Daggett, H. Rauvala, J. R. Hassell, and N. R. Smalheiser (1998). The relationship between perlecan and dystroglycan and its implication in the formation of the neuromuscular junction. Cell Adhes. Commun. 5:475-489.
    • (1998) Cell Adhes. Commun. , vol.5 , pp. 475-489
    • Peng, H.B.1    Ali, A.A.2    Daggett, D.F.3    Rauvala, H.4    Hassell, J.R.5    Smalheiser, N.R.6
  • 14
    • 0028318185 scopus 로고
    • Deficiency of merosin in dystrophic dy mice and genetic linkage of laminin M chain gene to dy locus
    • Y. Sunada, S. M. Bernier, C. A. Kozak, Y. Yamada, and K. P. Campbell (1994). Deficiency of merosin in dystrophic dy mice and genetic linkage of laminin M chain gene to dy locus. J. Biol. Chem. 269:13729-13732.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13729-13732
    • Sunada, Y.1    Bernier, S.M.2    Kozak, C.A.3    Yamada, Y.4    Campbell, K.P.5
  • 15
    • 0038182574 scopus 로고    scopus 로고
    • Dystrophin-glycoprotein complex: Posttranslational processing and dystroglycan function
    • D. E. Michele and K. P. Campbell (2003). Dystrophin-glycoprotein complex: Posttranslational processing and dystroglycan function. J. Biol. Chem. 278:15457-15460.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15457-15460
    • Michele, D.E.1    Campbell, K.P.2
  • 16
    • 0036591684 scopus 로고    scopus 로고
    • Muscular dystrophies involving the dystrophin-glycoprotein complex: An overview of current mouse models
    • M. Durbeej and K. P. Campbell (2002). Muscular dystrophies involving the dystrophin-glycoprotein complex: An overview of current mouse models. Curr. Opin. Genet. Dev. 12:349-361.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 349-361
    • Durbeej, M.1    Campbell, K.P.2
  • 17
    • 0025272250 scopus 로고
    • Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle
    • J. M. Ervasti, K. Ohlendieck, S. D. Kahl, M. G. Gaver, and K. P. Campbell (1990). Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle. Nature 345:315-319.
    • (1990) Nature , vol.345 , pp. 315-319
    • Ervasti, J.M.1    Ohlendieck, K.2    Kahl, S.D.3    Gaver, M.G.4    Campbell, K.P.5
  • 18
    • 0025815479 scopus 로고
    • Membrane organization of the dystrophin-glycoprotein complex
    • J. M. Ervasti and K. P. Campbell (1991). Membrane organization of the dystrophin-glycoprotein complex. Cell 66:1121-1131.
    • (1991) Cell , vol.66 , pp. 1121-1131
    • Ervasti, J.M.1    Campbell, K.P.2
  • 20
    • 0029072703 scopus 로고
    • Purification of cranin, a laminin binding membrane protein. Identity with dystroglycan and reassessment of its carbohydrate moieties
    • N. R. Smalheiser and E. Kim (1995). Purification of cranin, a laminin binding membrane protein. Identity with dystroglycan and reassessment of its carbohydrate moieties. J. Biol. Chem. 270:15425-15433.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15425-15433
    • Smalheiser, N.R.1    Kim, E.2
  • 21
    • 0027321171 scopus 로고
    • Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin
    • S. H. Gee, R. W. Blacher, P. J. Douville, P. R. Provost, P. D. Yurchenco, and S. Carbonetto (1993). Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin. J. Biol. Chem. 268:14972-14980.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14972-14980
    • Gee, S.H.1    Blacher, R.W.2    Douville, P.J.3    Provost, P.R.4    Yurchenco, P.D.5    Carbonetto, S.6
  • 24
    • 0030480912 scopus 로고    scopus 로고
    • Localization of cranin (dystroglycan) at sites of cell-matrix and cell-cell contact: Recruitment to focal adhesions is dependent upon extracellular ligands
    • A. M. Belkin and N. R. Smalheiser (1996). Localization of cranin (dystroglycan) at sites of cell-matrix and cell-cell contact: Recruitment to focal adhesions is dependent upon extracellular ligands. Cell Adhes. Commun. 4:281-296.
    • (1996) Cell Adhes. Commun. , vol.4 , pp. 281-296
    • Belkin, A.M.1    Smalheiser, N.R.2
  • 25
    • 0033543647 scopus 로고    scopus 로고
    • Biochemical characterization of the epithelial dystroglycan complex
    • M. Durbeej and K. P. Campbell (1999). Biochemical characterization of the epithelial dystroglycan complex. J. Biol. Chem. 274:26609-26616.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26609-26616
    • Durbeej, M.1    Campbell, K.P.2
  • 29
    • 0345593814 scopus 로고    scopus 로고
    • A PDZ-containing scaffold related to the dystrophin complex at the basolateral membrane of epithelial cells
    • A. M. Kachinsky, S. C. Froehner, and S. L. Milgram (1999). A PDZ-containing scaffold related to the dystrophin complex at the basolateral membrane of epithelial cells. J. Cell. Biol. 145:391-402.
    • (1999) J. Cell. Biol. , vol.145 , pp. 391-402
    • Kachinsky, A.M.1    Froehner, S.C.2    Milgram, S.L.3
  • 30
    • 0033837115 scopus 로고    scopus 로고
    • Assembly of multiple dystrobrevin-containing complexes in the kidney
    • N. Y. Loh, S. E. Newey, K. E. Davies, and D. J. Blake (2000). Assembly of multiple dystrobrevin-containing complexes in the kidney. J. Cell Sci. 113(Pt. 15):2715-2724.
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 15 , pp. 2715-2724
    • Loh, N.Y.1    Newey, S.E.2    Davies, K.E.3    Blake, D.J.4
  • 31
    • 0031568332 scopus 로고    scopus 로고
    • Transient expression of Dp140, a product of the Duchenne muscular dystrophy locus, during kidney tubulogenesis
    • M. Durbeej, D. Jung, T. Hjalt, K. P. Campbell, and P. Ekblom (1997). Transient expression of Dp140, a product of the Duchenne muscular dystrophy locus, during kidney tubulogenesis. Dev. Biol. 181:156-167.
    • (1997) Dev. Biol. , vol.181 , pp. 156-167
    • Durbeej, M.1    Jung, D.2    Hjalt, T.3    Campbell, K.P.4    Ekblom, P.5
  • 34
    • 0029790012 scopus 로고    scopus 로고
    • Cloning and expression analyses of mouse dystroglycan gene: Specific expression in maternal decidua at the peri-implantation stage
    • S. Yotsumoto, H. Fujiwara, J. H. Horton, T. A. Mosby, X. Wang, Y. Cui, and M. S. Ko (1996). Cloning and expression analyses of mouse dystroglycan gene: Specific expression in maternal decidua at the peri-implantation stage. Hum. Mol. Genet. 5:1259-1267.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1259-1267
    • Yotsumoto, S.1    Fujiwara, H.2    Horton, J.H.3    Mosby, T.A.4    Wang, X.5    Cui, Y.6    Ko, M.S.7
  • 35
    • 0036126711 scopus 로고    scopus 로고
    • Cadherin-like domains in alpha-dystroglycan, alpha/epsilon-sarcoglycan and yeast and bacterial proteins
    • N. J. Dickens, S. Beatson, and C. P. Ponting (2002). Cadherin-like domains in alpha-dystroglycan, alpha/epsilon-sarcoglycan and yeast and bacterial proteins. Curr. Biol. 12:R197-R199.
    • (2002) Curr. Biol. , vol.12
    • Dickens, N.J.1    Beatson, S.2    Ponting, C.P.3
  • 36
    • 0031697295 scopus 로고    scopus 로고
    • Sequence analysis suggests the presence of an IG-like domain in the N-terminal region of alpha-dystroglycan which was crystallized after mutation of a protease susceptible site (Arg168→His)
    • D. Bozic, J. Engel, and A. Brancaccio (1998). Sequence analysis suggests the presence of an IG-like domain in the N-terminal region of alpha-dystroglycan which was crystallized after mutation of a protease susceptible site (Arg168→His). Matrix Biol. 17:495-500.
    • (1998) Matrix Biol. , vol.17 , pp. 495-500
    • Bozic, D.1    Engel, J.2    Brancaccio, A.3
  • 37
    • 0029063024 scopus 로고
    • Electron microscopic evidence for a mucin-like region in chick muscle alpha-dystroglycan
    • A. Brancaccio, T. Schulthess, M. Gesemann, and J. Engel (1995). Electron microscopic evidence for a mucin-like region in chick muscle alpha-dystroglycan. FEBS Lett. 368:139-142.
    • (1995) FEBS Lett. , vol.368 , pp. 139-142
    • Brancaccio, A.1    Schulthess, T.2    Gesemann, M.3    Engel, J.4
  • 39
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • T. Pawson and J. D. Scott (1997). Signaling through scaffold, anchoring, and adaptor proteins. Science 278:2075-2080.
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 40
    • 0034903234 scopus 로고    scopus 로고
    • The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation
    • J. L. Ilsley, M. Sudol, and S. J. Winder (2001). The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation. Cell. Signal. 13:625-632.
    • (2001) Cell. Signal. , vol.13 , pp. 625-632
    • Ilsley, J.L.1    Sudol, M.2    Winder, S.J.3
  • 41
    • 0034027602 scopus 로고    scopus 로고
    • Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan regulates its interaction with utrophin
    • M. James, A. Nuttall, J. L. Ilsley, K. Ottersbach, J. M. Tinsley, M. Sudol, and S. J. Winder (2000). Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan regulates its interaction with utrophin. J. Cell Sci. 113(Pt. 10):1717-1726.
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 10 , pp. 1717-1726
    • James, M.1    Nuttall, A.2    Ilsley, J.L.3    Ottersbach, K.4    Tinsley, J.M.5    Sudol, M.6    Winder, S.J.7
  • 43
    • 0035933537 scopus 로고    scopus 로고
    • A synthetic peptide corresponding to the 550-585 region of alpha-dystroglycan binds beta-dystroglycan as revealed by NMR spectroscopy
    • M. Bozzi, G. Veglia, M. Paci, F. Sciandra, B. Giardina, and A. Brancaccio (2001). A synthetic peptide corresponding to the 550-585 region of alpha-dystroglycan binds beta-dystroglycan as revealed by NMR spectroscopy. FEBS Lett. 499:210-214.
    • (2001) FEBS Lett. , vol.499 , pp. 210-214
    • Bozzi, M.1    Veglia, G.2    Paci, M.3    Sciandra, F.4    Giardina, B.5    Brancaccio, A.6
  • 44
    • 0038414615 scopus 로고    scopus 로고
    • Beta1 Integrin and alpha-dystroglycan binding sites are localized to different laminin-G-domain-like (LG) modules within the laminin alpha5 chain G domain
    • H. Yu and J. F. Talts (2003). beta1 Integrin and alpha-dystroglycan binding sites are localized to different laminin-G-domain-like (LG) modules within the laminin alpha5 chain G domain. Biochem. J. 371:289-299.
    • (2003) Biochem. J. , vol.371 , pp. 289-299
    • Yu, H.1    Talts, J.F.2
  • 48
    • 0030026572 scopus 로고    scopus 로고
    • Differential heparin inhibition of skeletal muscle alpha-dystroglycan binding to laminins
    • E. A. Pall, K. M. Bolton, and J. M. Ervasti (1996). Differential heparin inhibition of skeletal muscle alpha-dystroglycan binding to laminins. J. Biol. Chem. 271:3817-3821.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3817-3821
    • Pall, E.A.1    Bolton, K.M.2    Ervasti, J.M.3
  • 49
    • 0034600063 scopus 로고    scopus 로고
    • Structure of the C-terminal laminin G-like domain pair of the laminin alpha2 chain harbouring binding sites for alpha-dystroglycan and heparin
    • D. Tisi, J. F. Talts, R. Timpl, and E. Hohenester (2000). Structure of the C-terminal laminin G-like domain pair of the laminin alpha2 chain harbouring binding sites for alpha-dystroglycan and heparin. EMBO J. 19:1432-1440.
    • (2000) EMBO J. , vol.19 , pp. 1432-1440
    • Tisi, D.1    Talts, J.F.2    Timpl, R.3    Hohenester, E.4
  • 52
    • 0033037910 scopus 로고    scopus 로고
    • Association of the dystroglycan complex isolated from bovine brain synaptosomes with proteins involved in signal transduction
    • M. Cavaldesi, G. Macchia, S. Barca, P. Defilippi, G. Tarone, and T. C. Petrucci (1999). Association of the dystroglycan complex isolated from bovine brain synaptosomes with proteins involved in signal transduction. J. Neurochem. 72:1648-1655.
    • (1999) J. Neurochem. , vol.72 , pp. 1648-1655
    • Cavaldesi, M.1    Macchia, G.2    Barca, S.3    Defilippi, P.4    Tarone, G.5    Petrucci, T.C.6
  • 54
    • 0036157980 scopus 로고    scopus 로고
    • The WW domain: Linking cell signalling to the membrane cytoskeleton
    • J. L. Ilsley, M. Sudol, and S. J. Winder (2002). The WW domain: Linking cell signalling to the membrane cytoskeleton. Cell. Signal. 14:183-189.
    • (2002) Cell. Signal. , vol.14 , pp. 183-189
    • Ilsley, J.L.1    Sudol, M.2    Winder, S.J.3
  • 55
    • 0035807788 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins
    • F. Sotgia, H. Lee, M. T. Bedford, T. Petrucci, M. Sudol, and M. P. Lisanti (2001). Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins. Biochemistry 40:14585-14592.
    • (2001) Biochemistry , vol.40 , pp. 14585-14592
    • Sotgia, F.1    Lee, H.2    Bedford, M.T.3    Petrucci, T.4    Sudol, M.5    Lisanti, M.P.6
  • 56
    • 0029664392 scopus 로고    scopus 로고
    • Ca2+-calmodulin binds to the carboxyl-terminal domain of dystrophin
    • J. T. Anderson, R. P. Rogers, and H. W. Jarrett (1996). Ca2+-calmodulin binds to the carboxyl-terminal domain of dystrophin. J. Biol. Chem. 271:6605-6610.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6605-6610
    • Anderson, J.T.1    Rogers, R.P.2    Jarrett, H.W.3
  • 57
    • 0034646942 scopus 로고    scopus 로고
    • Contribution of the different modules in the utrophin carboxy-terminal region to the formation and regulation of the DAP complex
    • A. Tommasi di Vignano, G. Di Zenzo, M. Sudol, G. Cesareni, and L. Dente (2000). Contribution of the different modules in the utrophin carboxy-terminal region to the formation and regulation of the DAP complex. FEBS Lett. 471:229-234.
    • (2000) FEBS Lett. , vol.471 , pp. 229-234
    • Tommasi di Vignano, A.1    Di Zenzo, G.2    Sudol, M.3    Cesareni, G.4    Dente, L.5
  • 59
    • 0035930547 scopus 로고    scopus 로고
    • Prolactin negatively regulates caveolin-1 gene expression in the mammary gland during lactation, via a Ras-dependent mechanism
    • D. S. Park, H. Lee, C. Riedel, J. Hulit, P. E. Scherer, R. G. Pestell, and M. P. Lisanti (2001). Prolactin negatively regulates caveolin-1 gene expression in the mammary gland during lactation, via a Ras-dependent mechanism. J. Biol. Chem. 276:48389-48397.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48389-48397
    • Park, D.S.1    Lee, H.2    Riedel, C.3    Hulit, J.4    Scherer, P.E.5    Pestell, R.G.6    Lisanti, M.P.7
  • 61
    • 0032079525 scopus 로고    scopus 로고
    • Evidence for in situ and in vitro association between beta-dystroglycan and the subsynaptic 43K rapsyn protein. Consequence for acetylcholine receptor clustering at the synapse
    • A. Cartaud, S. Coutant, T. C. Petrucci, and J. Cartaud (1998). Evidence for in situ and in vitro association between beta-dystroglycan and the subsynaptic 43K rapsyn protein. Consequence for acetylcholine receptor clustering at the synapse. J. Biol. Chem. 273:11321-11326.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11321-11326
    • Cartaud, A.1    Coutant, S.2    Petrucci, T.C.3    Cartaud, J.4
  • 62
    • 0024562843 scopus 로고
    • The mammalian 43-kD acetylcholine receptor-associated protein (RAPsyn) is expressed in some nonmuscle cells
    • L. S. Musil, D. E. Frail, and J. P. Merlie (1989). The mammalian 43-kD acetylcholine receptor-associated protein (RAPsyn) is expressed in some nonmuscle cells. J. Cell Biol. 108:1833-1840.
    • (1989) J. Cell Biol. , vol.108 , pp. 1833-1840
    • Musil, L.S.1    Frail, D.E.2    Merlie, J.P.3
  • 64
    • 0041710928 scopus 로고    scopus 로고
    • Chimaeric mice deficient in dystroglycans develop muscular dystrophy and have disrupted myoneural synapses
    • P. D. Cote, H. Moukhles, M. Lindenbaum, and S. Carbonetto (1999). Chimaeric mice deficient in dystroglycans develop muscular dystrophy and have disrupted myoneural synapses. Nat. Genet. 23:338-342.
    • (1999) Nat. Genet. , vol.23 , pp. 338-342
    • Cote, P.D.1    Moukhles, H.2    Lindenbaum, M.3    Carbonetto, S.4
  • 68
    • 0035755874 scopus 로고    scopus 로고
    • Dystroglycan binding to laminin alpha1LG4 module influences epithelial morphogenesis of salivary gland and lung in vitro
    • M. Durbeej, J. F. Talts, M. D. Henry, P. D. Yurchenco, K. P. Campbell, and P. Ekblom (2001). Dystroglycan binding to laminin alpha1LG4 module influences epithelial morphogenesis of salivary gland and lung in vitro. Differentiation 69:121-134.
    • (2001) Differentiation , vol.69 , pp. 121-134
    • Durbeej, M.1    Talts, J.F.2    Henry, M.D.3    Yurchenco, P.D.4    Campbell, K.P.5    Ekblom, P.6
  • 69
    • 0028960136 scopus 로고
    • Antibodies against domain E3 of laminin-1 and integrin alpha 6 subunit perturb branching epithelial morphogenesis of submandibular gland, but by different modes
    • Y. Kadoya, K. Kadoya, M. Durbeej, K. Holmvall, L. Sorokin, and P. Ekblom (1995). Antibodies against domain E3 of laminin-1 and integrin alpha 6 subunit perturb branching epithelial morphogenesis of submandibular gland, but by different modes. J. Cell Biol. 129:521-534.
    • (1995) J. Cell Biol. , vol.129 , pp. 521-534
    • Kadoya, Y.1    Kadoya, K.2    Durbeej, M.3    Holmvall, K.4    Sorokin, L.5    Ekblom, P.6
  • 70
    • 0038330238 scopus 로고    scopus 로고
    • The role of laminin in embryonic cell polarization and tissue organization
    • S. Li, D. Edgar, R. Fassler, W. Wadsworth, and P. D. Yurchenco (2003). The role of laminin in embryonic cell polarization and tissue organization. Dev. Cell 4:613-624.
    • (2003) Dev. Cell , vol.4 , pp. 613-624
    • Li, S.1    Edgar, D.2    Fassler, R.3    Wadsworth, W.4    Yurchenco, P.D.5
  • 71
    • 0032445403 scopus 로고    scopus 로고
    • A role for dystroglycan in basement membrane assembly
    • M. D. Henry and K. P. Campbell (1998). A role for dystroglycan in basement membrane assembly. Cell 95:859-870.
    • (1998) Cell , vol.95 , pp. 859-870
    • Henry, M.D.1    Campbell, K.P.2
  • 72
    • 0037166935 scopus 로고    scopus 로고
    • Matrix assembly, regulation, and survival functions of laminin and its receptors in embryonic stem cell differentiation
    • S. Li, D. Harrison, S. Carbonetto, R. Fassler, N. Smyth, D. Edgar, and P. D. Yurchenco (2002). Matrix assembly, regulation, and survival functions of laminin and its receptors in embryonic stem cell differentiation. J. Cell Biol. 157:1279-1290.
    • (2002) J. Cell Biol. , vol.157 , pp. 1279-1290
    • Li, S.1    Harrison, D.2    Carbonetto, S.3    Fassler, R.4    Smyth, N.5    Edgar, D.6    Yurchenco, P.D.7
  • 73
    • 0033519279 scopus 로고    scopus 로고
    • Laminin polymerization induces a receptor-cytoskeleton network
    • H. Colognato, D. A. Winkelmann, and P. D. Yurchenco (1999). Laminin polymerization induces a receptor-cytoskeleton network. J. Cell Biol. 145:619-631.
    • (1999) J. Cell Biol. , vol.145 , pp. 619-631
    • Colognato, H.1    Winkelmann, D.A.2    Yurchenco, P.D.3
  • 75
    • 0030936450 scopus 로고    scopus 로고
    • Reversion of the malignant phenotype of human breast cells in three-dimensional culture and in vivo by integrin blocking antibodies
    • V. M. Weaver, O. W. Petersen, F. Wang, C. A. Larabell, P. Briand, C. Damsky, and M. J. Bissell (1997). Reversion of the malignant phenotype of human breast cells in three-dimensional culture and in vivo by integrin blocking antibodies. J. Cell Biol. 137:231-245.
    • (1997) J. Cell Biol. , vol.137 , pp. 231-245
    • Weaver, V.M.1    Petersen, O.W.2    Wang, F.3    Larabell, C.A.4    Briand, P.5    Damsky, C.6    Bissell, M.J.7
  • 77
    • 0034870766 scopus 로고    scopus 로고
    • Reduced expression of dystroglycan in breast and prostate cancer
    • M. D. Henry, M. B. Cohen, and K. P. Campbell (2001). Reduced expression of dystroglycan in breast and prostate cancer. Hum. Pathol. 32:791-795.
    • (2001) Hum. Pathol. , vol.32 , pp. 791-795
    • Henry, M.D.1    Cohen, M.B.2    Campbell, K.P.3
  • 80
    • 0033597343 scopus 로고    scopus 로고
    • Adhesion of cultured bovine aortic endothelial cells to laminin-1 mediated by dystroglycan
    • H. Shimizu, H. Hosokawa, H. Ninomiya, J. H. Miner, and T. Masaki (1999). Adhesion of cultured bovine aortic endothelial cells to laminin-1 mediated by dystroglycan. J. Biol. Chem. 274:11995-12000.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11995-12000
    • Shimizu, H.1    Hosokawa, H.2    Ninomiya, H.3    Miner, J.H.4    Masaki, T.5
  • 81
    • 0035878554 scopus 로고    scopus 로고
    • Processing of beta-dystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycan complex
    • H. Yamada, F. Saito, H. Fukuta-Ohi, D. Zhong, A. Hase, K. Arai, A. Okuyama, R. Maekawa, T. Shimizu, and K. Matsumura (2001). Processing of beta-dystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycan complex. Hum. Mol. Genet. 10:1563-1569.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1563-1569
    • Yamada, H.1    Saito, F.2    Fukuta-Ohi, H.3    Zhong, D.4    Hase, A.5    Arai, K.6    Okuyama, A.7    Maekawa, R.8    Shimizu, T.9    Matsumura, K.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.