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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Sainis, I. | en |
| dc.contributor.author | Angelidis, C. | en |
| dc.contributor.author | Pagoulatos, G. N. | en |
| dc.contributor.author | Lazaridis, I. | en |
| dc.date.accessioned | 2015-11-24T19:13:03Z | - |
| dc.date.available | 2015-11-24T19:13:03Z | - |
| dc.identifier.issn | 1355-8145 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/21148 | - |
| dc.rights | Default Licence | - |
| dc.subject | heat-shock protein | en |
| dc.subject | large t-antigen | en |
| dc.subject | vaccinia virus-infection | en |
| dc.subject | simian-virus-40 large-t | en |
| dc.subject | human hsp70 gene | en |
| dc.subject | j-domain | en |
| dc.subject | molecular chaperone | en |
| dc.subject | association | en |
| dc.subject | stimulation | en |
| dc.subject | expression | en |
| dc.title | HSC70 interactions with SV40 viral proteins differ between permissive and nonpermissive mammalian cells | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.secondary | <Go to ISI>://000089442400007 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.publicationDate | 2000 | - |
| heal.abstract | SV40 belongs to a group of DNA tumor viruses which induce the expression of the 70 Kd heat shock proteins, but the meaning of this induction remains unclear. Investigating the role of hsc70 in the SV40 life cycle, we found that the protein translocates to the nucleus late in infection of permissive CVI cells, in contrast to infected nonpermissive BALB/3T3 and NIH/3T3 cells in which hsc70 remains cytoplasmic. Moreover, the pattern of hsc70 nuclear staining was diffused and clearly distinguishable from that observed after heat shock. In addition hsc70 late in infection coimmunoprecipitated with the viral capsid protein VPI, suggesting a role in the process of viral packaging. Interactions of hsc70 with the early viral oncoprotein T antigen were observed only in nonpermissive cells, indicating that the binding of the above proteins is specific to cells that do not support viral propagation. Finally, treatment of permissive CVI cells with interferon gamma, a known antiviral cytokine, resulted in hsc70 binding to T antigen. Our results suggest that the role of hsc70 in the process of SV40 infection is directly related to the ability of the host cells to support viral propagation and is clearly different between permissive and nonpermissive cell lines. | en |
| heal.journalName | Cell Stress & Chaperones | en |
| heal.journalType | peer-reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ | |
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