Extracellular glycoproteins at acetylcholine receptor clusters of rat myotubes are organized into domains

Dmytrenko, George M.; Scher, Malka G.; Poiana, Giancarlo; Baetscher, Manfred; Bloch, Robert J.

doi:10.1016/0014-4827(90)90254-8

Cited by 7 publications

(3 citation statements)

References 43 publications

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“…Other reports (5,16,20,21) have identified the nAChR as the initial rabies virus cell target. Interestingly, extracellular matrix molecules, including fibronectin, codistribute with nAChR clusters (12,13). Thus, fibronectin should be considered as part and parcel of the VHSV and other fish rhabdovirus cell receptor complexes, playing a role in the initial binding step, which is probably followed by a secondary binding, allowing the virus to enter into the cell by fusion or by endocytosis (19).…”

Section: Discussionmentioning

confidence: 99%

Fish Rhabdovirus Cell Entry Is Mediated by Fibronectin

Béarzotti

Delmas

Lamoureux

et al. 1999

J Virol

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Three monoclonal antibodies (MAbs) generated against rainbow trout gonad cells (RTG-2) have been selected for their ability to protect cells from the viral hemorrhagic septicemia virus (VHSV) infection, a salmonid rhabdovirus. Protection from infection was restricted to the salmonid-derived cell lines indicating species specificity of the blocking MAbs. Surprisingly, the blocking activity of these MAbs was also effective against other nonantigenically related fish rhabdoviruses. Indirect immunofluorescence and immunoelectron microscopy observations demonstrated that the three MAbs were all directed against an abundant cell plasma membrane component, and immunoprecipitation studies indicated that the target consisted of a heterodimeric complex with molecular masses of 200 and 44 kDa. Biochemical data provided the following evidence that fibronectin is part of this complex and that it could represent the main receptor for fish rhabdoviruses. (i) An antiserum generated against the 200-kDa protein reacted against the recombinant rainbow trout fibronectin expressed in Escherichia coli. (ii) The purified rainbow trout fibronectin was able to bind specifically to VHSV. To our knowledge, this is the first identification of a cellular component acting as a primary receptor for a virus replicating in lower vertebrates and, more interestingly, for viruses belonging to theRhabdoviridae family.

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Section: Discussionmentioning

confidence: 99%

Fish Rhabdovirus Cell Entry Is Mediated by Fibronectin

Béarzotti

Delmas

Lamoureux

et al. 1999

J Virol

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“…So far, three BL HSPGs have been identified: perlecan, agrin, and type XVIII collagen (Noonan et al, 1991;Tsen et al, 1995;Halfter et al, 1998). HSPGs are implicated in developmental processes underlying myogenesis and synaptogenesis (Anderson and Fambrough, 1983;Anderson et al, 1984;Bayne et al, 1984;Dmytrenko et al, 1990). Perlecan may effect neuromuscular junction (NMJ) formation by binding growth factors (Peng et al, 1998).…”

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confidence: 99%

Heparan Sulfate Heterogeneity in Skeletal Muscle Basal Lamina: Demonstration by Phage Display-Derived Antibodies

et al. 2000

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The basal lamina (BL) enveloping skeletal muscle fibers contains different glycoproteins, including proteoglycans. To obtain more information on the glycosaminoglycan moiety of proteoglycans, we have selected a panel of anti-heparan sulfate (HS) antibodies from a semisynthetic antibody phage display library by panning against glycosaminoglycan preparations derived from skeletal muscle. Epitope recognition by the antibodies is strongly dependent on O- and N-sulfation of the heparan sulfate. Immunostaining with these antibodies showed a distinct distribution of heparan sulfate epitopes in muscle basal lamina of various species. Clear differences in staining intensity were observed between neural, synaptic, and extrasynaptic basal laminae. Moreover, temporal and regional changes in abundancy of heparan sulfate epitopes were observed during muscle development both in vitro and in vivo. Taken together, these data suggest a role for specific heparan sulfate domains/species in myogenesis and synaptogenesis. Detailed analysis of the functions of heparan sulfate epitopes in muscle morphogenesis has now become feasible with the isolation of antibodies specific for distinct heparan sulfate epitopes.

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“…contractile proteins into sarcomeres and interactions between fibers and nerve cells results in the formation of functional muscle, responsive to neuronal input . Extracellular matrix proteins may promote sarcomere assembly (Volk et al ., 1990) as well as localize acetylcholine receptors (Axelrod et al ., 1976;Dymtrenko et al, 1990) . Neuromuscular junctions are formed and stabilized by further molecular interactions, each cell type providing specific proteins (Fallon et al, 1985 ;Bloch and Froehner, 1987;Hunter et al, 1989;Carr et al, 1989) .…”

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confidence: 99%

H36-alpha 7 is a novel integrin alpha chain that is developmentally regulated during skeletal myogenesis [published erratum appears in J Cell Biol 1992 Jul;118(1):213]

Song

1992

The Journal of Cell Biology

231

150

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Abstract. H36 is a 120,000-D membrane glycoprotein that is expressed during the differentiation of skeletal muscle . H36 cDNA clones were isolated from a lambda UniZapXR rat myotube cDNA library and sequenced . The deduced amino acid sequence demonstrates that H36 is a novel integrin alpha chain that shares extensive homology with other alpha integrins that includes : (a) the GFFKR sequence found in all alpha integrins; (b) a single membrane spanning region ; (c) conservation of 18 of 22 cysteines ; and (d) a protease cleavage site found in the non-I region integrin alpha chains . The cytoplasmic domain of H36 is unique and additional regions of nonhomology further indicate H36 is distinct from all other alpha chains . In keeping with current nomenclature we designate this alpha chain 0. Northern blots demonstrate that expression of H36-a7 mRNA is regulated both early in the development of the myogenic lineage and later, during terminal differentiation . Detection of H36-a7 mRNA coincides with conversion of H36-myogenic precursor A A continuum of cell interactions takes place throughout the differentiation of skeletal muscle : distinct cell and molecular interactions underlie the development and function ofeach stage. In the early stages ofmyogenesis cells replicate, migrate, and maintain an autonomy from one another that is typical of most other cells . During this stage the primary interactions of cells are with their molecular environment that includes nutrients, growth factors, and extracellular matrix proteins. This serves to increase cell mass and localize the sites of future development . Subsequently, upon termination of the proliferative stage, the cells interact and fuse to form elongate fibers . At this same stage of development the genes that encode the myofibrillar proteins and ATP-generating enzymes are expressed . The transition between these stages of myogenic development is regulated by the interactions of heterodimeric complexes of helix-loophelix proteins with regulatory sites in the genome (Murre et al., 1989;Davis et al ., 1990 ; for review see Olson, 1990) and by the interactions of cells with growth factors (Lim and Hauschka, 1984;Ewton and Florini, 1990;Massague et al., 1986;Jin et al., 1991) and extracellular matrix proteins (Foster et al., 1987;Ocalan et al., 1988) . The assembly of the

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Extracellular glycoproteins at acetylcholine receptor clusters of rat myotubes are organized into domains

Cited by 7 publications

References 43 publications

Fish Rhabdovirus Cell Entry Is Mediated by Fibronectin

Fish Rhabdovirus Cell Entry Is Mediated by Fibronectin

Heparan Sulfate Heterogeneity in Skeletal Muscle Basal Lamina: Demonstration by Phage Display-Derived Antibodies

H36-alpha 7 is a novel integrin alpha chain that is developmentally regulated during skeletal myogenesis [published erratum appears in J Cell Biol 1992 Jul;118(1):213]

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