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The kinetics of ER fusion protein activation in vivo
Reversibly switchable proteins are powerful tools with which to explore protein function in vitro and in vivo. For example, the activity of many proteins fused to the hormone-binding domain of the modified estrogen receptor (ER(TAM)) can be regulated by provision or removal of 4-hydroxytamoxifen (4-...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4076531/ https://www.ncbi.nlm.nih.gov/pubmed/24662815 http://dx.doi.org/10.1038/onc.2014.78 |
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author | Wilson, Catherine H. Gamper, Ivonne Perfetto, Alessandra Auw, Jeremy Littlewood, Trevor D. Evan, Gerard I. |
author_facet | Wilson, Catherine H. Gamper, Ivonne Perfetto, Alessandra Auw, Jeremy Littlewood, Trevor D. Evan, Gerard I. |
author_sort | Wilson, Catherine H. |
collection | PubMed |
description | Reversibly switchable proteins are powerful tools with which to explore protein function in vitro and in vivo. For example, the activity of many proteins fused to the hormone-binding domain of the modified estrogen receptor (ER(TAM)) can be regulated by provision or removal of 4-hydroxytamoxifen (4-OHT). Despite the widespread use of ER(TAM) fusions in vivo, inadequate data are available as to the most efficacious routes for systemic tamoxifen delivery. In this study, we have used two well-characterised ER(TAM) fusion proteins, both reversibly activated by 4-OHT, to compare the effectiveness and kinetics of 4-OHT delivery in mice in vivo by either tamoxifen in food or by intraperitoneal injection. Our data indicate that dietary tamoxifen offers an effective, facile and ethically preferable means for long term activation of ER(TAM) fusion proteins in vivo. |
format | Online Article Text |
id | pubmed-4076531 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
record_format | MEDLINE/PubMed |
spelling | pubmed-40765312015-04-02 The kinetics of ER fusion protein activation in vivo Wilson, Catherine H. Gamper, Ivonne Perfetto, Alessandra Auw, Jeremy Littlewood, Trevor D. Evan, Gerard I. Oncogene Article Reversibly switchable proteins are powerful tools with which to explore protein function in vitro and in vivo. For example, the activity of many proteins fused to the hormone-binding domain of the modified estrogen receptor (ER(TAM)) can be regulated by provision or removal of 4-hydroxytamoxifen (4-OHT). Despite the widespread use of ER(TAM) fusions in vivo, inadequate data are available as to the most efficacious routes for systemic tamoxifen delivery. In this study, we have used two well-characterised ER(TAM) fusion proteins, both reversibly activated by 4-OHT, to compare the effectiveness and kinetics of 4-OHT delivery in mice in vivo by either tamoxifen in food or by intraperitoneal injection. Our data indicate that dietary tamoxifen offers an effective, facile and ethically preferable means for long term activation of ER(TAM) fusion proteins in vivo. 2014-03-24 2014-10-02 /pmc/articles/PMC4076531/ /pubmed/24662815 http://dx.doi.org/10.1038/onc.2014.78 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Wilson, Catherine H. Gamper, Ivonne Perfetto, Alessandra Auw, Jeremy Littlewood, Trevor D. Evan, Gerard I. The kinetics of ER fusion protein activation in vivo |
title | The kinetics of ER fusion protein activation in vivo |
title_full | The kinetics of ER fusion protein activation in vivo |
title_fullStr | The kinetics of ER fusion protein activation in vivo |
title_full_unstemmed | The kinetics of ER fusion protein activation in vivo |
title_short | The kinetics of ER fusion protein activation in vivo |
title_sort | kinetics of er fusion protein activation in vivo |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4076531/ https://www.ncbi.nlm.nih.gov/pubmed/24662815 http://dx.doi.org/10.1038/onc.2014.78 |
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