α-Dystroglycan Is a Laminin Receptor Involved in Extracellular Matrix Assembly on Myotubes and Muscle Cell Viability

Montanaro, Federica; Lindenbaum, Michael; Carbonetto, Salvatore

doi:10.1083/jcb.145.6.1325

Cited by 112 publications

(94 citation statements)

References 99 publications

(191 reference statements)

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“…This finding is consistent with previous data demonstrating that overexpression of DG caused a decreased growth rate in vascular endothelial cells. 33 It is also consistent with recent data demonstrating that DG is a suppressor of integrin-mediated extracellular signal-regulated kinase (ERK) activation 34 and with the observation that α-DG-dependent signal transduction pathway can stimulate differentiation, thus inhibiting proliferation, of both muscle 26 and epithelial 7,35 cells. Cell adhesion to matrigel-coated dishes, as well as plating efficiency, was also increased in the DG-overexpressing derivatives of the MCF10F cells, as compared to control cells (Table 1 and Fig.…”

Section: Discussionsupporting

confidence: 84%

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Increased expression of dystroglycan inhibits the growth and tumorigenicity of human mammary epithelial cells

Sgambato¹,

Camerini²,

Faraglia³

et al. 2004

Cancer Biology & Therapy

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Dystroglycan (DG) is an adhesion molecule formed by two subunits, α (extracellular) and β (transmembrane) DG, which are codified by a single gene and form a continuous link from the extracellular matrix to the intracellular cytoskeleton. Reduction or loss of expression of DG has been observed in human cancer cell lines and primary tumors and has been suggested to promote tumor development and invasiveness.In this study, the human breast epithelial non-tumorigenic MCF10F and the breast cancer MCF7 cell lines were engineered to stably express an exogenous DG cDNA and the effects on the phenotype of both cell lines were evaluated. The MCF10F transfected cells displayed an increased expression of both DG subunits which was associated with inhibition of the anchorage-dependent growth, accumulation of cells in the G 0 /G 1 phase of the cell cycle and increased adhesion to a substratum. The MCF7 transfected cells were unable to restore α-DG despite an increased expression of the β-DG subunit. Anchoragedependent and independent growth and the in vivo tumorigenicity were reduced in these derivatives that also displayed a reduced adhesion to a substratum and were shown to release α-DG in the culture medium.These findings confirm and extend previous evidence that transformation of mammary epithelial cells is associated with loss of their ability to retain α-DG on the cell membrane. Moreover, they indicate that DG is involved in cell functions other than cell adhesion to the extracellular matrix, and that its loss of function might predispose to tumor progression by compromising regulatory controls over cell growth and proliferation.

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Section: Discussionsupporting

confidence: 84%

“…11 In fact, several evidence suggest that DG plays an important role in modulating attachment of cells to matrigel. 24,26 We found that the conditioned medium from the MCF7, but not from the MCF10F cells, caused a significant inhibition of cell adhesion to matrigel-coated dishes (Fig. 5).…”

Section: α-Dg Is Secreted In the Culture Medium Of Cancer But Not Normalmentioning

confidence: 87%

Increased expression of dystroglycan inhibits the growth and tumorigenicity of human mammary epithelial cells

Sgambato¹,

Camerini²,

Faraglia³

et al. 2004

Cancer Biology & Therapy

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“…For exam ple, cultured myoblasts have improved myogenic prop erties when grown on a synthetic basement membrane (Matrigel) compared to individual matrix components such as fibronectin, collagen, and laminin (32,47,48,51). In addition, myoblasts cannot survive long term in vitro if their expression of the laminin-binding protein a-dystroglycan is inhibited (53). The temporal expression of calpain, and its inhibitor calpastatin, is closely associ ated with myoblast fusion (3)(4)(5)10,11,64), and this is linked to the degradation of certain extracellular matrix molecules (12).…”

Section: Effects Of Proteolytic Enzymesmentioning

confidence: 99%

Exposure to Tissue Culture Conditions Can Adversely Affect Myoblast Behavior in Vivo in Whole Muscle Grafts: Implications for Myoblast Transfer Therapy

Smythe

Grounds

2000

Cell Transplant

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The effects of tissue culture conditions on the viability of myoblasts in whole muscles transplanted in vivo were investigated. Whole male (SJL/J) donor muscles were exposed to various tissue culture reagents and proteolytic enzymes, and allografted into female (SJL/J) host mice. Desmin immunohistochemistry was used to assess the numbers of myogenic cells (as an index of myoblast viability and the extent of regeneration) in tissue sections of whole-muscle grafts sampled on days 7 and 14. DNA quantitation with a Y-chromosome-specific probe was used to determine the total Y-l sequence DNA (as an index of myoblast survival and proliferation) in whole-muscle grafts sampled on days 1, 3, and 7. In grafts exposed to serum-free medium, there was a delay in myoblast fusion at 7 days that was recovered by 14 days, but exposure to serum (10% or 20%) had a prolonged adverse effect on myotube formation at 14 days. DNA quantitation demonstrated that either serum-free culture medium or 10% serum enhanced the number of male cells within whole-muscle grafts at 7 days. Proteolytic digestion (even for 5 min) of whole muscles prior to grafting was extremely detrimental to myoblast survival and viability at 7 and 14 days. The unexpected finding of adverse effects of tissue culture conditions on the regeneration of whole-muscle grafts in vivo appears to parallel the major problem of the rapid death of isolated cultured donor myoblasts after injection in myoblast transfer therapy. The use of whole-muscle grafts provides an alternative and sensitive model to analyze the crucial effects of various tissue culture components on the subsequent survival and proliferation of myogenic cells in vivo.

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“…The complex is composed of several transmembrane, cytoplasmic and extracellular protein subunits, with dystrophin, a large intracellular rod-like protein, serving as a tether between cytoskeletal actin and -dystroglycan, the core transmembrane subunit of the DGC (Ervasti and Campbell, 1993;Lapidos et al, 2004). The extracellular domain of -dystroglycan is linked to a peripheral protein subunit, -dystroglycan, which serves as a receptor for laminin in the basal lamina (Montanaro et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

β-Dystroglycan binds caveolin-1 in smooth muscle: a functional role in caveolae distribution and Ca2+ release

Sharma

Ghavami

Stelmack

et al. 2010

Journal of Cell Science

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SummaryThe dystrophin-glycoprotein complex (DGC) links the extracellular matrix and actin cytoskeleton. Caveolae form membrane arrays on smooth muscle cells; we investigated the mechanism for this organization. Caveolin-1 and -dystroglycan, the core transmembrane DGC subunit, colocalize in airway smooth muscle. Immunoprecipitation revealed the association of caveolin-1 with -dystroglycan. Disruption of actin filaments disordered caveolae arrays, reduced association of -dystroglycan and caveolin-1 to lipid rafts, and suppressed the sensitivity and responsiveness of methacholine-induced intracellular Ca 2+ release. We generated novel human airway smooth muscle cell lines expressing shRNA to stably silence -dystroglycan expression. In these myocytes, caveolae arrays were disorganized, caveolae structural proteins caveolin-1 and PTRF/cavin were displaced, the signaling proteins PLC1 and G q , which are required for receptor-mediated Ca 2+ release, were absent from caveolae, and the sensitivity and responsiveness of methacholineinduced intracellular Ca 2+ release, was diminished. These data reveal an interaction between caveolin-1 and -dystroglycan and demonstrate that this association, in concert with anchorage to the actin cytoskeleton, underpins the spatial organization and functional role of caveolae in receptor-mediated Ca 2+ release, which is an essential initiator step in smooth muscle contraction.

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α-Dystroglycan Is a Laminin Receptor Involved in Extracellular Matrix Assembly on Myotubes and Muscle Cell Viability

Cited by 112 publications

References 99 publications

Increased expression of dystroglycan inhibits the growth and tumorigenicity of human mammary epithelial cells

Increased expression of dystroglycan inhibits the growth and tumorigenicity of human mammary epithelial cells

Exposure to Tissue Culture Conditions Can Adversely Affect Myoblast Behavior in Vivo in Whole Muscle Grafts: Implications for Myoblast Transfer Therapy

β-Dystroglycan binds caveolin-1 in smooth muscle: a functional role in caveolae distribution and Ca2+ release

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