Journal article
The distribution, induction and isoenzyme profile of glutathione S-transferase and glutathione peroxidase in isolated rat liver parenchymal, Kupffer and endothelial cells
Biochemical journal, Vol.264(3), pp.737-744
12/15/1989
DOI: 10.1042/bj2640737
PMCID: PMC1133647
PMID: 2619713
Abstract
The distribution and inducibility of cytosolic glutathione S-transferase (EC 2.5.1.18) and glutathione peroxidase (EC 1.11.1.19) activities in rat liver parenchymal, Kupffer and endothelial cells were studied. In untreated rats glutathione S-transferase activity with 1-chloro-2,4-dinitrobenzene and 4-hydroxynon-2-trans-enal as substrates was 1.7-2.2-fold higher in parenchymal cells than in Kupffer and endothelial cells, whereas total, selenium-dependent and non-selenium-dependent glutathione peroxidase activities were similar in all three cell types. Glutathione S-transferase isoenzymes in parenchymal and non-parenchymal cells isolated from untreated rats were separated by chromatofocusing in an f.p.l.c. system: all glutathione S-transferase isoenzymes observed in the sinusoidal lining cells were also detected in the parenchymal cells, whereas Kupffer and endothelial cells lacked several glutathione S-transferase isoenzymes present in parenchymal cells. At 5 days after administration of Arocolor 1254 glutathione S-transferase activity was only enhanced in parenchymal cells; furthermore, selenium-dependent glutathione peroxidase activity decreased in parenchymal and non-parenchymal cells. At 13 days after a single injection of Aroclor 1254 a strong induction of glutathione S-transferase had taken place in all three cell types, whereas selenium-dependent glutathione peroxidase activity remained unchanged (endothelial cells) or was depressed (parenchymal and Kupffer cells). Hence these results clearly establish that glutathione S-transferase and glutathione peroxidase are differentially regulated in rat liver parenchymal as well as non-parenchymal cells. The presence of glutathione peroxidase and several glutathione S-transferase isoenzymes capable of detoxifying a variety of compounds in Kupffer and endothelial cells might be crucial to protect the liver from damage by potentially hepatotoxic substances.
Details
- Title: Subtitle
- The distribution, induction and isoenzyme profile of glutathione S-transferase and glutathione peroxidase in isolated rat liver parenchymal, Kupffer and endothelial cells
- Creators
- P Steinberg - Institut für Toxikologie, Universität Mainz, Obere Zahlbacher Strasse 67, D-6500 Mainz, Federal Republic of GermanyH Schramm - Institut für Toxikologie, Universität Mainz, Obere Zahlbacher Strasse 67, D-6500 Mainz, Federal Republic of GermanyL Schladt - Institut für Toxikologie, Universität Mainz, Obere Zahlbacher Strasse 67, D-6500 Mainz, Federal Republic of GermanyL W Robertson - Institut für Toxikologie, Universität Mainz, Obere Zahlbacher Strasse 67, D-6500 Mainz, Federal Republic of GermanyH Thomas - Institut für Toxikologie, Universität Mainz, Obere Zahlbacher Strasse 67, D-6500 Mainz, Federal Republic of GermanyF Oesch - Institut für Toxikologie, Universität Mainz, Obere Zahlbacher Strasse 67, D-6500 Mainz, Federal Republic of Germany
- Resource Type
- Journal article
- Publication Details
- Biochemical journal, Vol.264(3), pp.737-744
- DOI
- 10.1042/bj2640737
- PMID
- 2619713
- PMCID
- PMC1133647
- NLM abbreviation
- Biochem J
- ISSN
- 0264-6021
- eISSN
- 1470-8728
- Language
- English
- Date published
- 12/15/1989
- Academic Unit
- Occupational and Environmental Health
- Record Identifier
- 9984002438902771
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