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RECORD NUMBER: 21 OF 75

OLS Field Name OLS Field Data
Main Title Effect of Phenobarbital and 3-Methylcholanthrene on Aldehyde Dehydrogenase Activity in Cultures of HepG2 Cells and Normal Human Hepatocytes. (Revised).
Author Marselos, M. ; Strom, S. C. ; Michalopoulos, G. ;
CORP Author Ioannina Univ. (Greece). Dept. of Pharmacology. ;Duke Univ. Medical Center, Durham, NC. Dept. of Pathology.;Health Effects Research Lab., Research Triangle Park, NC.
Year Published 1987
Report Number EPA-R-811687; EPA/600/J-87/285;
Stock Number PB88-185228
Additional Subjects Phenobarbital ; Methylcholanthrene ; Drug therapy ; Liver ; Metabolism ; Deoxyribonucleic acids ; Cells(Biology) ; Reprints ; Aldehyde dehydrogenase ; Hepatoma
Holdings
Library Call Number Additional Info Location Last
Modified
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Status
NTIS  PB88-185228 Most EPA libraries have a fiche copy filed under the call number shown. Check with individual libraries about paper copy. 09/04/1988
Collation 16p
Abstract
Aldehyde dehydrogenase (ALDH) activity was measured in primary cultures of normal human hepatocytes and of the human hepatoma cell line HepG2 after application of phenobarbital (PB) or 3-methylcholanthrene (MC) for 5 days. Treatment with PB alone resulted in a significant increase on both protein and DNA content at concentrations of 2 and 3mM. Treatment with MC at a concentration as low as 5 micro M led to a significant loss of cells when it lasted more than 5 days. Concentrations of 3-5mM of PB in the media of HepG2 cell cultures caused a 2-fold enhancement of the activity of ALDH, as measured with NAD and propionaldehyde (P/NAD) or benzaldehyde (B/NAD). On the other hand, MC-treated cultures (5 micro M) showed a 20-fold increase in enzyme activity measured with NADPO and benzaldehyde (B/NADP), and a 2-fold increase in B/NAD activity. Combined treatment with both PB and MC led to an effect of dynamic synergism as far as B/NAD and B/NADP activities are concerned, suggesting a metabolite of MC as the mediator for the increase of ALDH activity. Normal human hepatocytes in primary cultures responded to PB (3mM) in a similar way as HepG2 cells as far as DNA and protein content and AKDH activity are concerned. It is concluded, that HepG2 hepatoma cells behave similar to the normal hepatocytes in terms of ALDH regulation and can be used for studies on the activity of ALDH as modified by added xenobiotics. (Copyright (c) 1987 Elsevier Scientific Publishers Ireland Ltd.)