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. 2012 Feb 9;7(2):e31451. doi: 10.1371/journal.pone.0031451

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Ettorre et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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A: Membrane proteins co-immunoprecipitated by anti-GluR1 antibody were analyzed by immunoblotting using rapsyn antibody. Results show that GluR1 strongly interacted with rapsyn only in cocultured myotubes. Western blot analysis of beta III-tubulin confirmed the presence of neuronal cells only in coculture cell extracts. B: Membrane proteins co-immunoprecipitated by anti-rapsyn antibody were analyzed by immunoblotting using antibodies against GluR1, SAP97, stargazin and PSD95. Results show that both cocoltured myotubes and pure myotubes expressed PSD95, stargazin and SAP97 at the cell membrane. Conversely GluR1 was strongly expressed only in cocultured myotubes. Immunoreactivity of rapsyn-interacting stargazin increased in cocoltured myotubes while that of SAP97 decreased. No change was observed in PSD95 immunoreactivity. C: Confocal images showing the distribution of GluR1, rapsyn, SAP97, stargazin and PSD95 in myotubes cocultured with neurons for 7 days and immunostained. Rapsyn, stargazin and PSD95 colocalize with the receptors, while SAP97 shows a diffuse distribution.