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Regulation of acetylcholine receptor synthesis at the level of translation in rat primary muscle cells

Previous studies have shown that rat primary muscle cells do not respond to crude rat brain extract or one of its active components, ascorbic acid, with a significant increase in surface acetylcholine receptor (AChR) number. We report here that, although little or no response is seen on the cell sur...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1989
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115538/
https://www.ncbi.nlm.nih.gov/pubmed/2469678
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collection PubMed
description Previous studies have shown that rat primary muscle cells do not respond to crude rat brain extract or one of its active components, ascorbic acid, with a significant increase in surface acetylcholine receptor (AChR) number. We report here that, although little or no response is seen on the cell surface, rat primary muscle cells do respond to both crude brain extract and to ascorbic acid with an approximately threefold increase in AChR alpha-subunit mRNA. The response of the mRNA is similar to that seen in the cloned L5 cells. However, while in L5 cells the increase in alpha-subunit mRNA is further translated into increased levels of alpha-subunit protein, there is no such increase in alpha-subunit synthesis in the primary cells. This study thus shows a regulation of surface AChR synthesis in rat primary cells at the level of alpha-subunit translation. This level of regulation is different from that involving subunit transcription or subunit assembly reported by others.
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spelling pubmed-21155382008-05-01 Regulation of acetylcholine receptor synthesis at the level of translation in rat primary muscle cells J Cell Biol Articles Previous studies have shown that rat primary muscle cells do not respond to crude rat brain extract or one of its active components, ascorbic acid, with a significant increase in surface acetylcholine receptor (AChR) number. We report here that, although little or no response is seen on the cell surface, rat primary muscle cells do respond to both crude brain extract and to ascorbic acid with an approximately threefold increase in AChR alpha-subunit mRNA. The response of the mRNA is similar to that seen in the cloned L5 cells. However, while in L5 cells the increase in alpha-subunit mRNA is further translated into increased levels of alpha-subunit protein, there is no such increase in alpha-subunit synthesis in the primary cells. This study thus shows a regulation of surface AChR synthesis in rat primary cells at the level of alpha-subunit translation. This level of regulation is different from that involving subunit transcription or subunit assembly reported by others. The Rockefeller University Press 1989-05-01 /pmc/articles/PMC2115538/ /pubmed/2469678 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Regulation of acetylcholine receptor synthesis at the level of translation in rat primary muscle cells
title Regulation of acetylcholine receptor synthesis at the level of translation in rat primary muscle cells
title_full Regulation of acetylcholine receptor synthesis at the level of translation in rat primary muscle cells
title_fullStr Regulation of acetylcholine receptor synthesis at the level of translation in rat primary muscle cells
title_full_unstemmed Regulation of acetylcholine receptor synthesis at the level of translation in rat primary muscle cells
title_short Regulation of acetylcholine receptor synthesis at the level of translation in rat primary muscle cells
title_sort regulation of acetylcholine receptor synthesis at the level of translation in rat primary muscle cells
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115538/
https://www.ncbi.nlm.nih.gov/pubmed/2469678