Please use this identifier to cite or link to this item:
https://olympias.lib.uoi.gr/jspui/handle/123456789/19312Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Marselos, M. | en |
| dc.contributor.author | Michalopoulos, G. | en |
| dc.date.accessioned | 2015-11-24T18:58:48Z | - |
| dc.date.available | 2015-11-24T18:58:48Z | - |
| dc.identifier.issn | 0001-6683 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/19312 | - |
| dc.rights | Default Licence | - |
| dc.subject | Aldehyde Dehydrogenase/*metabolism | en |
| dc.subject | Animals | en |
| dc.subject | DNA/metabolism | en |
| dc.subject | Enzyme Activation/drug effects | en |
| dc.subject | Isoenzymes/*metabolism | en |
| dc.subject | Liver/*enzymology | en |
| dc.subject | Male | en |
| dc.subject | Phenobarbital/*pharmacology | en |
| dc.subject | Rats | en |
| dc.subject | Substrate Specificity | en |
| dc.title | Phenobarbital enhances the aldehyde dehydrogenase activity of rat hepatocytes in vitro and in vivo | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.secondary | http://www.ncbi.nlm.nih.gov/pubmed/3811968 | - |
| heal.identifier.secondary | http://onlinelibrary.wiley.com/store/10.1111/j.1600-0773.1986.tb00191.x/asset/j.1600-0773.1986.tb00191.x.pdf?v=1&t=h095f11l&s=c47c7cfff02c7ca28d853e3d333e9c203b272d27 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.publicationDate | 1986 | - |
| heal.abstract | Aldehyde dehydrogenase (ALDH) was measured in primary cultures of hepatocytes obtained with collagenase perfusion from livers of Long-Evans rats. After seven days in culture, basal ALDH activity, protein content and DNA content are significantly decreased. Exposure of the cultures to phenobarbital (PB, 3 mM in the media) does not prevent the decrease of DNA content, although it keeps protein at relatively higher levels. The activity of ALDH is not only preserved, but also significantly enhanced, when propionaldehyde, phenylacetaldehyde, benzaldehyde and D-glucuronolactone are used as substrates and NAD as the coenzyme. A relative increase of activity is also noted when ALDH is measured with benzaldehyde and NADP. Treatment of Long-Evans animals with PB (1 mg/ml, in drinking water for 2 weeks) leads to similar relative increases of the ALDH activity. In absolute values, however, enzyme activities found after in vivo treatment with PB are higher, compared to those obtained after in vitro exposure. These results show that ALDH activity can be greatly enhanced by PB in primary hepatocyte cultures, free from any indirect endogenous influences. | en |
| heal.journalName | Acta Pharmacol Toxicol (Copenh) | en |
| heal.journalType | peer-reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Marselos-1986-Phenobarbital enhanc.pdf | 517.53 kB | Adobe PDF | View/Open Request a copy |
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