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http://hdl.handle.net/10662/19492
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Campo DC | Valor | idioma |
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dc.contributor.author | Jardín Polo, Isaac | - |
dc.contributor.author | Diez-Bello, Raquel | - |
dc.contributor.author | Falcón, Débora | - |
dc.contributor.author | Alvarado Monterroso, Sandra | - |
dc.contributor.author | Regodón Mena, Sergio | - |
dc.contributor.author | Salido Ruiz, G. M. | - |
dc.contributor.author | Smani, Tarik | - |
dc.contributor.author | Rosado, Juan A. | - |
dc.date.accessioned | 2024-01-30T12:57:20Z | - |
dc.date.available | 2024-01-30T12:57:20Z | - |
dc.date.issued | 2021-06 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/10662/19492 | - |
dc.description.abstract | Melatonin has been reported to induce effective reduction in growth and development in a variety of tumors, including breast cancer. In triple-negative breast cancer (TNBC) cells, melatonin attenuates a variety of cancer features, such as tumor growth and apoptosis resistance, through a number of still poorly characterized mechanisms. One biological process that is important for TNBC cells is store-operated Ca2+ entry (SOCE), which is modulated by TRPC6 expression and function. We wondered whether melatonin might intersect with this pathway as part of its anticancer activity. We show that melatonin, in the nanomolar range, significantly attenuates TNBC MDA-MB-231 cell viability, proliferation, and migration in a time- and concentration-dependent manner, without having any effect on nontumoral breast epithelial MCF10A cells. Pretreatment with different concentrations of melatonin significantly reduced SOCE in MDA-MB-231 cells without altering Ca2+ release from the intracellular stores. By contrast, SOCE in MCF10A cells was unaffected by melatonin. In the TNBC MDA-MB-468 cell line, melatonin not only attenuated viability, migration, and SOCE, but also reduced TRPC6 expression in a time- and concentration-dependent manner, without altering expression or function of the Ca2+ channel Orai1. The expression of exogenous TRPC6 overcame the effect of melatonin on SOCE and cell proliferation, and silencing or inhibition of TRPC6 impaired the inhibitory effect of melatonin on SOCE. These findings indicate that TRPC6 downregulation might be involved in melatonin's inhibitory effects on Ca2+ influx and the maintenance of cancer hallmarks and point toward a novel antitumoral mechanism of melatonin in TNBC cells. | es_ES |
dc.description.sponsorship | Supported by MICINN (Grants BFU2016-74932-C2-1-P, BFU2016-74932-C2-2-P, PID2019-104084GB-C21 and PID2019-104084GB-C22) and Junta de Extremadura-Fondo Europeo de Desarrollo Regional (Grants IB16046 and GR18061). S. A., R. D.-B., and I. J. (contract TA18054) are supported by contracts from Junta de Extremadura-FEDER. D. F. is supported by Jordi Soler grant from CIBERCV (ISCIII, Madrid). | es_ES |
dc.format.extent | 17 p. | es_ES |
dc.format.mimetype | application/pdf | en_US |
dc.language.iso | eng | es_ES |
dc.publisher | Elsevier | es_ES |
dc.rights | Attribution-NoDerivatives 4.0 International | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nd/4.0/ | * |
dc.subject | Melatonin | es_ES |
dc.subject | TRPC6 | es_ES |
dc.subject | Triple-negative breast cancer cells | es_ES |
dc.subject | Calcium entry | es_ES |
dc.subject | SOCE | es_ES |
dc.title | Melatonin downregulates TRPC6, impairing store-operated calcium entry in triple-negative breast cancer cells | es_ES |
dc.type | article | es_ES |
dc.description.version | peerReviewed | es_ES |
europeana.type | TEXT | en_US |
dc.rights.accessRights | openAccess | es_ES |
dc.subject.unesco | 3201.01 Oncología | es_ES |
europeana.dataProvider | Universidad de Extremadura. España | es_ES |
dc.identifier.bibliographicCitation | Isaac Jardin, Raquel Diez-Bello, Debora Falcon, Sandra Alvarado, Sergio Regodon, Gines M. Salido, Tarik Smani, Juan A. Rosado, Melatonin downregulates TRPC6, impairing store-operated calcium entry in triple-negative breast cancer cells, Journal of Biological Chemistry, Volume 296, 2021, 100254, ISSN 0021-9258, https://doi.org/10.1074/jbc.RA120.015769. | es_ES |
dc.type.version | publishedVersion | es_ES |
dc.contributor.affiliation | N/A | es_ES |
dc.contributor.affiliation | Universidad de Extremadura. Departamento de Fisiología | es_ES |
dc.relation.publisherversion | https://www.jbc.org/article/S0021-9258(21)00021-1/fulltext | es_ES |
dc.identifier.doi | 10.1074/jbc.RA120.015769 | - |
dc.identifier.publicationtitle | Journal of Biological Chemistry | es_ES |
dc.identifier.publicationissue | 296 | es_ES |
dc.identifier.publicationfirstpage | 100254-1 | es_ES |
dc.identifier.publicationlastpage | 100254-17 | es_ES |
dc.identifier.orcid | 0000-0002-9749-2325 | es_ES |
dc.identifier.orcid | 0000-0003-4575-8264 | es_ES |
Colección: | DFSIO - Artículos |
Archivos
Archivo | Descripción | Tamaño | Formato | |
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PIIS0021925821000211.pdf | 6,51 MB | Adobe PDF | Descargar |
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