Source:http://linkedlifedata.com/resource/pubmed/id/17596210
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2007-6-28
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| pubmed:abstractText |
Damage or stress in many organelles may trigger apoptosis by several not yet fully elucidated mechanisms. A cell death pathway is induced by endoplasmic reticulum (ER) stress elicited by the unfolded protein response and/or by aberrant Ca(2+) signalling. Reticulon-1C (RTN-1C) belongs to the reticulon family, neuroendocrine-specific proteins localized primarily on the ER membrane. In the present study, we demonstrate that RTN-1C is able to modulate, in a mutually exclusive way, the cellular sensitivity to different apoptosis pathways in human neuroblastoma cells. In fact, the increase of RTN-1C protein levels per se results in ER stress-induced cell death, mediated by an increase of cytosolic Ca(2+), and significantly sensitizes cells to different ER stress inducers. In line with these findings, the reduction of RTN-1C, by antisense DNA expression, reduced the sensitivity to ER-stressors. In the presence of high RTN-1C levels, genotoxic drugs become ineffective as a consequence of the cytoplasm translocation of p53 protein, while the silencing of endogenous RTN-1C results in the potentiation of the genotoxic drugs action. These data indicate that RTN-1C is able to modulate the cellular sensitivity to different apoptotic pathways representing a promising molecular target for new drug development.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides, Antisense,
http://linkedlifedata.com/resource/pubmed/chemical/RTN1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Protein p53
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jul
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| pubmed:issn |
0022-3042
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
102
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
345-53
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| pubmed:meshHeading |
pubmed-meshheading:17596210-Apoptosis,
pubmed-meshheading:17596210-DNA Damage,
pubmed-meshheading:17596210-Down-Regulation,
pubmed-meshheading:17596210-Endoplasmic Reticulum,
pubmed-meshheading:17596210-Humans,
pubmed-meshheading:17596210-Intracellular Membranes,
pubmed-meshheading:17596210-Microscopy, Electron, Transmission,
pubmed-meshheading:17596210-Nerve Degeneration,
pubmed-meshheading:17596210-Nerve Tissue Proteins,
pubmed-meshheading:17596210-Neuroblastoma,
pubmed-meshheading:17596210-Neurodegenerative Diseases,
pubmed-meshheading:17596210-Neurons,
pubmed-meshheading:17596210-Nuclear Envelope,
pubmed-meshheading:17596210-Oligodeoxyribonucleotides, Antisense,
pubmed-meshheading:17596210-Oxidative Stress,
pubmed-meshheading:17596210-Protein Transport,
pubmed-meshheading:17596210-Signal Transduction,
pubmed-meshheading:17596210-Tumor Cells, Cultured,
pubmed-meshheading:17596210-Tumor Suppressor Protein p53
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| pubmed:year |
2007
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| pubmed:articleTitle |
Reticulon-1C acts as a molecular switch between endoplasmic reticulum stress and genotoxic cell death pathway in human neuroblastoma cells.
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| pubmed:affiliation |
Department of Biology, University of Rome Tor Vergata, Via della Ricerca Scientifica, Rome, Italy.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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