Enhanced protein denaturation in indomethacin-treated cells
| dc.contributor.author | Roussou, I. | en |
| dc.contributor.author | Nguyen, T. | en |
| dc.contributor.author | Pagoulatos, G. N. | en |
| dc.contributor.author | Bensaude, O. | en |
| dc.date.accessioned | 2015-11-24T19:19:16Z | |
| dc.date.available | 2015-11-24T19:19:16Z | |
| dc.identifier.issn | 1355-8145 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/21947 | |
| dc.rights | Default Licence | - |
| dc.subject | 3T3 Cells/drug effects/metabolism | en |
| dc.subject | Animals | en |
| dc.subject | Anti-Inflammatory Agents, Non-Steroidal/*pharmacology | en |
| dc.subject | Cell Nucleus/metabolism | en |
| dc.subject | Clone Cells/metabolism | en |
| dc.subject | Cytoplasm/metabolism | en |
| dc.subject | DNA-Binding Proteins/*physiology | en |
| dc.subject | HSP70 Heat-Shock Proteins/chemistry/*metabolism | en |
| dc.subject | *Hot Temperature | en |
| dc.subject | Indomethacin/*pharmacology | en |
| dc.subject | Mice | en |
| dc.subject | Protein Denaturation/*drug effects | en |
| dc.subject | Recombinant Fusion Proteins/metabolism | en |
| dc.subject | Stress, Physiological/genetics/metabolism | en |
| dc.subject | Transcription Factors | en |
| dc.subject | Transcription, Genetic | en |
| dc.title | Enhanced protein denaturation in indomethacin-treated cells | en |
| heal.abstract | Indomethacin, a potent anti-inflammatory drug, activates the DNA-binding activity of human heat shock transcription factor 1 (HSF1), but this is insufficient to elevate heat shock gene expression. However, indomethacin pretreatment leads to a complete heat shock response at temperatures that are by themselves insufficient. Here, we showed that the heat-induced loss of enzymatic activity of a nuclear or a cytoplasmic luciferase expressed in murine cells was enhanced when cells had been pretreated with indomethacin. Additionally, in these cells the 70-kDa constitutive heat shock protein exhibited an enhanced aggregation in the presence of indomethacin. Similarly an increase in the aggregation of beta-galactosidase was observed. These data suggest that indomethacin at moderate temperatures accelerates the presence of denatured proteins in the cell, thus lowering the temperature threshold for a heat shock response. | en |
| heal.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.secondary | http://www.ncbi.nlm.nih.gov/pubmed/10701834 | - |
| heal.journalName | Cell Stress Chaperones | en |
| heal.journalType | peer-reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 2000 | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.type | journalArticle | - |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.type.en | Journal article | en |
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