Phenyl acyl acids attenuate the unfolded protein response in tunicamycin-treated neuroblastoma cells.

Understanding how neural cells handle proteostasis stress in the endoplasmic reticulum (ER) is important to decipher the mechanisms that underlie the cell death associated with neurodegenerative diseases and to design appropriate therapeutic tools. Here we have compared the sensitivity of a human ne...

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Autores principales:	Marta Zamarbide, Eva Martinez-Pinilla, Ana Ricobaraza, Tomás Aragón, Rafael Franco, Alberto Pérez-Mediavilla
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e90813c3e0574b4ba4743db0ce5c6be7
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spelling	oai:doaj.org-article:e90813c3e0574b4ba4743db0ce5c6be72021-11-18T08:59:27ZPhenyl acyl acids attenuate the unfolded protein response in tunicamycin-treated neuroblastoma cells.1932-620310.1371/journal.pone.0071082https://doaj.org/article/e90813c3e0574b4ba4743db0ce5c6be72013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23976981/?tool=EBIhttps://doaj.org/toc/1932-6203Understanding how neural cells handle proteostasis stress in the endoplasmic reticulum (ER) is important to decipher the mechanisms that underlie the cell death associated with neurodegenerative diseases and to design appropriate therapeutic tools. Here we have compared the sensitivity of a human neuroblastoma cell line (SH-SY5H) to the ER stress caused by an inhibitor of protein glycosylation with that observed in human embryonic kidney (HEK-293T) cells. In response to stress, SH-SY5H cells increase the expression of mRNA encoding downstream effectors of ER stress sensors and transcription factors related to the unfolded protein response (the spliced X-box binding protein 1, CCAAT-enhancer-binding protein homologous protein, endoplasmic reticulum-localized DnaJ homologue 4 and asparagine synthetase). Tunicamycin-induced death of SH-SY5H cells was prevented by terminal aromatic substituted butyric or valeric acids, in association with a decrease in the mRNA expression of stress-related factors, and in the accumulation of the ATF4 protein. Interestingly, this decrease in ATF4 protein occurs without modifying the phosphorylation of the translation initiation factor eIF2α. Together, these results show that when short chain phenyl acyl acids alleviate ER stress in SH-SY5H cells their survival is enhanced.Marta ZamarbideEva Martinez-PinillaAna RicobarazaTomás AragónRafael FrancoAlberto Pérez-MediavillaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 8, p e71082 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Marta Zamarbide Eva Martinez-Pinilla Ana Ricobaraza Tomás Aragón Rafael Franco Alberto Pérez-Mediavilla Phenyl acyl acids attenuate the unfolded protein response in tunicamycin-treated neuroblastoma cells.
description	Understanding how neural cells handle proteostasis stress in the endoplasmic reticulum (ER) is important to decipher the mechanisms that underlie the cell death associated with neurodegenerative diseases and to design appropriate therapeutic tools. Here we have compared the sensitivity of a human neuroblastoma cell line (SH-SY5H) to the ER stress caused by an inhibitor of protein glycosylation with that observed in human embryonic kidney (HEK-293T) cells. In response to stress, SH-SY5H cells increase the expression of mRNA encoding downstream effectors of ER stress sensors and transcription factors related to the unfolded protein response (the spliced X-box binding protein 1, CCAAT-enhancer-binding protein homologous protein, endoplasmic reticulum-localized DnaJ homologue 4 and asparagine synthetase). Tunicamycin-induced death of SH-SY5H cells was prevented by terminal aromatic substituted butyric or valeric acids, in association with a decrease in the mRNA expression of stress-related factors, and in the accumulation of the ATF4 protein. Interestingly, this decrease in ATF4 protein occurs without modifying the phosphorylation of the translation initiation factor eIF2α. Together, these results show that when short chain phenyl acyl acids alleviate ER stress in SH-SY5H cells their survival is enhanced.
format	article
author	Marta Zamarbide Eva Martinez-Pinilla Ana Ricobaraza Tomás Aragón Rafael Franco Alberto Pérez-Mediavilla
author_facet	Marta Zamarbide Eva Martinez-Pinilla Ana Ricobaraza Tomás Aragón Rafael Franco Alberto Pérez-Mediavilla
author_sort	Marta Zamarbide
title	Phenyl acyl acids attenuate the unfolded protein response in tunicamycin-treated neuroblastoma cells.
title_short	Phenyl acyl acids attenuate the unfolded protein response in tunicamycin-treated neuroblastoma cells.
title_full	Phenyl acyl acids attenuate the unfolded protein response in tunicamycin-treated neuroblastoma cells.
title_fullStr	Phenyl acyl acids attenuate the unfolded protein response in tunicamycin-treated neuroblastoma cells.
title_full_unstemmed	Phenyl acyl acids attenuate the unfolded protein response in tunicamycin-treated neuroblastoma cells.
title_sort	phenyl acyl acids attenuate the unfolded protein response in tunicamycin-treated neuroblastoma cells.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/e90813c3e0574b4ba4743db0ce5c6be7
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Phenyl acyl acids attenuate the unfolded protein response in tunicamycin-treated neuroblastoma cells.

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