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Effects of inducers of drug metabolism on basic hepatic forms of mouse glutathione transferase
The cytosolic glutathione transferases (GSTs) with basic pI values have been studied in mouse liver after treatment with 2,3-t-butylhydroxyanisole (BHA), cafestol palmitate (CAF), phenobarbital (PB), 3-methylcholanthrene (3-MC) and trans-stilbene oxide (t-SBO). The cytosolic GST activity was induced...
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Published in: | Biochemical journal 1989-11, Vol.263 (3), p.679-685 |
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description | The cytosolic glutathione transferases (GSTs) with basic pI values have been studied in mouse liver after treatment with 2,3-t-butylhydroxyanisole (BHA), cafestol palmitate (CAF), phenobarbital (PB), 3-methylcholanthrene (3-MC) and trans-stilbene oxide (t-SBO). The cytosolic GST activity was induced by all compounds except for 3-MC. Three forms of GST were isolated by means of affinity chromatography and f.p.l.c. The examination of protein profiles and enzymic activities with specific substrates showed that the three GSTs correspond to those found in control animals, i.e. GSTs MI, MII and MIII. The class Mu GST MIII accounted for the major effect of induction, whereas the class Alpha GST MI and the class Pi GST MII were unchanged or somewhat down-regulated. The greatest induction was obtained with BHA, PB and CAF. The activities of other glutathione-dependent enzymes were also studied. An increase in glutathione reductase and thioltransferase activities was observed after BHA, PB or CAF treatment; glyoxalase I and Se-dependent glutathione peroxidase were depressed in comparison with the control group in all cases studied. |
doi_str_mv | 10.1042/bj2630679 |
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The cytosolic GST activity was induced by all compounds except for 3-MC. Three forms of GST were isolated by means of affinity chromatography and f.p.l.c. The examination of protein profiles and enzymic activities with specific substrates showed that the three GSTs correspond to those found in control animals, i.e. GSTs MI, MII and MIII. The class Mu GST MIII accounted for the major effect of induction, whereas the class Alpha GST MI and the class Pi GST MII were unchanged or somewhat down-regulated. The greatest induction was obtained with BHA, PB and CAF. The activities of other glutathione-dependent enzymes were also studied. An increase in glutathione reductase and thioltransferase activities was observed after BHA, PB or CAF treatment; glyoxalase I and Se-dependent glutathione peroxidase were depressed in comparison with the control group in all cases studied.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj2630679</identifier><identifier>PMID: 2597126</identifier><language>eng</language><publisher>England</publisher><subject>Animals ; Butylated Hydroxyanisole - pharmacology ; Cytosol - enzymology ; Diterpenes - pharmacology ; Enzyme Induction - drug effects ; Glutaredoxins ; Glutathione Peroxidase - metabolism ; Glutathione Reductase - metabolism ; Glutathione Transferase - biosynthesis ; Glutathione Transferase - metabolism ; Isoenzymes - biosynthesis ; Isoenzymes - metabolism ; Lactoylglutathione Lyase - metabolism ; liver ; Liver - anatomy & histology ; Liver - enzymology ; Methylcholanthrene - pharmacology ; Mice ; Organ Size - drug effects ; Oxidoreductases - metabolism ; Phenobarbital - pharmacology ; Protein Disulfide Reductase (Glutathione) ; Stilbenes - pharmacology</subject><ispartof>Biochemical journal, 1989-11, Vol.263 (3), p.679-685</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c401t-e7d8a7e02e506d745bd7fafa53162923c994c1c480da901a84348701d57ae5853</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1133486/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1133486/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2597126$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Di Simplicio, P</creatorcontrib><creatorcontrib>Jensson, H</creatorcontrib><creatorcontrib>Mannervik, B</creatorcontrib><title>Effects of inducers of drug metabolism on basic hepatic forms of mouse glutathione transferase</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>The cytosolic glutathione transferases (GSTs) with basic pI values have been studied in mouse liver after treatment with 2,3-t-butylhydroxyanisole (BHA), cafestol palmitate (CAF), phenobarbital (PB), 3-methylcholanthrene (3-MC) and trans-stilbene oxide (t-SBO). The cytosolic GST activity was induced by all compounds except for 3-MC. Three forms of GST were isolated by means of affinity chromatography and f.p.l.c. The examination of protein profiles and enzymic activities with specific substrates showed that the three GSTs correspond to those found in control animals, i.e. GSTs MI, MII and MIII. The class Mu GST MIII accounted for the major effect of induction, whereas the class Alpha GST MI and the class Pi GST MII were unchanged or somewhat down-regulated. The greatest induction was obtained with BHA, PB and CAF. The activities of other glutathione-dependent enzymes were also studied. An increase in glutathione reductase and thioltransferase activities was observed after BHA, PB or CAF treatment; glyoxalase I and Se-dependent glutathione peroxidase were depressed in comparison with the control group in all cases studied.</description><subject>Animals</subject><subject>Butylated Hydroxyanisole - pharmacology</subject><subject>Cytosol - enzymology</subject><subject>Diterpenes - pharmacology</subject><subject>Enzyme Induction - drug effects</subject><subject>Glutaredoxins</subject><subject>Glutathione Peroxidase - metabolism</subject><subject>Glutathione Reductase - metabolism</subject><subject>Glutathione Transferase - biosynthesis</subject><subject>Glutathione Transferase - metabolism</subject><subject>Isoenzymes - biosynthesis</subject><subject>Isoenzymes - metabolism</subject><subject>Lactoylglutathione Lyase - metabolism</subject><subject>liver</subject><subject>Liver - anatomy & histology</subject><subject>Liver - enzymology</subject><subject>Methylcholanthrene - pharmacology</subject><subject>Mice</subject><subject>Organ Size - drug effects</subject><subject>Oxidoreductases - metabolism</subject><subject>Phenobarbital - pharmacology</subject><subject>Protein Disulfide Reductase (Glutathione)</subject><subject>Stilbenes - pharmacology</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><recordid>eNpVkUtLxDAUhYMo4zi68AcIXQkuqjdpmrQbQQZfMOBGt4Y0vZnp0DZjkgr-e-s4DLo6F-7HuY9DyDmFawqc3VRrJjIQsjwgU8olpIVkxSGZAhM8FcDoMTkJYQ1AOXCYkAnLS0mZmJL3e2vRxJA4mzR9PRj027r2wzLpMOrKtU3oEtcnlQ6NSVa40XFU63y3JTs3BEyW7RB1XDWuxyR63QeLXgc8JUdWtwHPdjojbw_3r_OndPHy-Dy_W6SGA40pyrrQEoFhDqKWPK9qabXVeUYFK1lmypIbangBtS6B6oJnvJBA61xqzIs8m5HbX9_NUHVYG-zHJVq18U2n_ZdyulH_O32zUkv3qSjNRisxGlzuDLz7GDBE1TXBYNvqHscDFc15JrgoRvDqFzTeheDR7odQUD9hqH0YI3vxd6s9uft-9g2z9YY1</recordid><startdate>19891101</startdate><enddate>19891101</enddate><creator>Di Simplicio, P</creator><creator>Jensson, H</creator><creator>Mannervik, B</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>5PM</scope></search><sort><creationdate>19891101</creationdate><title>Effects of inducers of drug metabolism on basic hepatic forms of mouse glutathione transferase</title><author>Di Simplicio, P ; Jensson, H ; Mannervik, B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c401t-e7d8a7e02e506d745bd7fafa53162923c994c1c480da901a84348701d57ae5853</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Animals</topic><topic>Butylated Hydroxyanisole - pharmacology</topic><topic>Cytosol - enzymology</topic><topic>Diterpenes - pharmacology</topic><topic>Enzyme Induction - drug effects</topic><topic>Glutaredoxins</topic><topic>Glutathione Peroxidase - metabolism</topic><topic>Glutathione Reductase - metabolism</topic><topic>Glutathione Transferase - biosynthesis</topic><topic>Glutathione Transferase - metabolism</topic><topic>Isoenzymes - biosynthesis</topic><topic>Isoenzymes - metabolism</topic><topic>Lactoylglutathione Lyase - metabolism</topic><topic>liver</topic><topic>Liver - anatomy & histology</topic><topic>Liver - enzymology</topic><topic>Methylcholanthrene - pharmacology</topic><topic>Mice</topic><topic>Organ Size - drug effects</topic><topic>Oxidoreductases - metabolism</topic><topic>Phenobarbital - pharmacology</topic><topic>Protein Disulfide Reductase (Glutathione)</topic><topic>Stilbenes - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Di Simplicio, P</creatorcontrib><creatorcontrib>Jensson, H</creatorcontrib><creatorcontrib>Mannervik, B</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Di Simplicio, P</au><au>Jensson, H</au><au>Mannervik, B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effects of inducers of drug metabolism on basic hepatic forms of mouse glutathione transferase</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1989-11-01</date><risdate>1989</risdate><volume>263</volume><issue>3</issue><spage>679</spage><epage>685</epage><pages>679-685</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>The cytosolic glutathione transferases (GSTs) with basic pI values have been studied in mouse liver after treatment with 2,3-t-butylhydroxyanisole (BHA), cafestol palmitate (CAF), phenobarbital (PB), 3-methylcholanthrene (3-MC) and trans-stilbene oxide (t-SBO). The cytosolic GST activity was induced by all compounds except for 3-MC. Three forms of GST were isolated by means of affinity chromatography and f.p.l.c. The examination of protein profiles and enzymic activities with specific substrates showed that the three GSTs correspond to those found in control animals, i.e. GSTs MI, MII and MIII. The class Mu GST MIII accounted for the major effect of induction, whereas the class Alpha GST MI and the class Pi GST MII were unchanged or somewhat down-regulated. The greatest induction was obtained with BHA, PB and CAF. The activities of other glutathione-dependent enzymes were also studied. An increase in glutathione reductase and thioltransferase activities was observed after BHA, PB or CAF treatment; glyoxalase I and Se-dependent glutathione peroxidase were depressed in comparison with the control group in all cases studied.</abstract><cop>England</cop><pmid>2597126</pmid><doi>10.1042/bj2630679</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Animals Butylated Hydroxyanisole - pharmacology Cytosol - enzymology Diterpenes - pharmacology Enzyme Induction - drug effects Glutaredoxins Glutathione Peroxidase - metabolism Glutathione Reductase - metabolism Glutathione Transferase - biosynthesis Glutathione Transferase - metabolism Isoenzymes - biosynthesis Isoenzymes - metabolism Lactoylglutathione Lyase - metabolism liver Liver - anatomy & histology Liver - enzymology Methylcholanthrene - pharmacology Mice Organ Size - drug effects Oxidoreductases - metabolism Phenobarbital - pharmacology Protein Disulfide Reductase (Glutathione) Stilbenes - pharmacology |
title | Effects of inducers of drug metabolism on basic hepatic forms of mouse glutathione transferase |
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