Monoclonal antibody-directed analysis of cytochrome P-450-dependent monooxygenases and mutagen activation in the livers of DBA/2 and C57BL/6 mice
Monoclonal antibodies (MAb 1-7-1 and Mab 2-66-3) specific for cytochrome P-450 (cyt. P-450) isozymes inhibited the metabolism of carcinogens, other xenobiotics, and endogenous compounds in two strains of mice. Postmitochondrial liver supernatant (S9) was prepared from untreated, 3-methylcholanthrene...
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| Veröffentlicht in: | Cancer research (Chicago, Ill.) Ill.), 1986-02, Vol.46 (2), p.524-531 |
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| creator | HIETANEN, E MALAVEILLE, C FRIEDMAN, F. K PARK, S. S BEREZIAT, J.-C BRUN, G BARTSCH, H GELBOIN, H. V |
| description | Monoclonal antibodies (MAb 1-7-1 and Mab 2-66-3) specific for cytochrome P-450 (cyt. P-450) isozymes inhibited the metabolism of carcinogens, other xenobiotics, and endogenous compounds in two strains of mice. Postmitochondrial liver supernatant (S9) was prepared from untreated, 3-methylcholanthrene-treated, phenobarbital-treated, and pregnenolone 16 alpha-carbonitrile-treated C57BL/6 (B6) and DBA/2 (D2) mice. The modifying effect of two types of MAb to a 3-methylcholanthrene-induced cyt. P-450 and a phenobarbital-induced cyt. P-450 was investigated for: (a) S9-mediated mutagenicity of aflatoxin B1, benzo(a)pyrene 7,8-dihydrodiol, 2-acetylaminofluorene, and N-nitrosomorpholine in Salmonella typhimurium strains; and (b) the activity of aryl hydrocarbon hydroxylase, ethoxycoumarin O-deethylase, ethoxyresorufin O-deethylase, aminopyrine N-demethylase, and testosterone 6 beta-, 7 alpha-, and 16 beta-hydroxylases. With certain S9s, MAb-1-7-1 inhibited only those cytochrome P-450 isozymes involved predominantly in activity of aryl hydrocarbon hydroxylase, ethoxyresorufin O-deethylase, and ethoxycoumarin O-deethylase and mutagenicity of 2-acetylaminofluorene and benzo(a)pyrene 7,8-dihydrodiol; MAb 2-66-3 inhibited only those involved in aminopyrine N-demethylase and testosterone 6 beta-, 7 alpha, and 16 beta-hydroxylase activity and aflatoxin B1 mutagenicity. Both Mab 1-7-1 and MAb 2-66-3 inhibited cytochrome P-450 isozyme(s) implicated predominantly in testosterone 7 alpha-hydroxylation in S9 from pregnenolone 16 alpha-carbonitrile-treated B6 mice. MAb 1-7-1 did not inhibit N-nitrosomorpholine mutagenicity and MAb 2-66-3 increased it by 2- to 6-fold depending on the source of S9. Using these MAbs, it is thus possible to identify the contribution of the epitope-defined single or class of cyt. P-450 to specific metabolic reactions in S9 from untreated and inducer-treated mice. |
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K ; PARK, S. S ; BEREZIAT, J.-C ; BRUN, G ; BARTSCH, H ; GELBOIN, H. V</creator><creatorcontrib>HIETANEN, E ; MALAVEILLE, C ; FRIEDMAN, F. K ; PARK, S. S ; BEREZIAT, J.-C ; BRUN, G ; BARTSCH, H ; GELBOIN, H. V</creatorcontrib><description>Monoclonal antibodies (MAb 1-7-1 and Mab 2-66-3) specific for cytochrome P-450 (cyt. P-450) isozymes inhibited the metabolism of carcinogens, other xenobiotics, and endogenous compounds in two strains of mice. Postmitochondrial liver supernatant (S9) was prepared from untreated, 3-methylcholanthrene-treated, phenobarbital-treated, and pregnenolone 16 alpha-carbonitrile-treated C57BL/6 (B6) and DBA/2 (D2) mice. The modifying effect of two types of MAb to a 3-methylcholanthrene-induced cyt. P-450 and a phenobarbital-induced cyt. P-450 was investigated for: (a) S9-mediated mutagenicity of aflatoxin B1, benzo(a)pyrene 7,8-dihydrodiol, 2-acetylaminofluorene, and N-nitrosomorpholine in Salmonella typhimurium strains; and (b) the activity of aryl hydrocarbon hydroxylase, ethoxycoumarin O-deethylase, ethoxyresorufin O-deethylase, aminopyrine N-demethylase, and testosterone 6 beta-, 7 alpha-, and 16 beta-hydroxylases. With certain S9s, MAb-1-7-1 inhibited only those cytochrome P-450 isozymes involved predominantly in activity of aryl hydrocarbon hydroxylase, ethoxyresorufin O-deethylase, and ethoxycoumarin O-deethylase and mutagenicity of 2-acetylaminofluorene and benzo(a)pyrene 7,8-dihydrodiol; MAb 2-66-3 inhibited only those involved in aminopyrine N-demethylase and testosterone 6 beta-, 7 alpha, and 16 beta-hydroxylase activity and aflatoxin B1 mutagenicity. Both Mab 1-7-1 and MAb 2-66-3 inhibited cytochrome P-450 isozyme(s) implicated predominantly in testosterone 7 alpha-hydroxylation in S9 from pregnenolone 16 alpha-carbonitrile-treated B6 mice. MAb 1-7-1 did not inhibit N-nitrosomorpholine mutagenicity and MAb 2-66-3 increased it by 2- to 6-fold depending on the source of S9. Using these MAbs, it is thus possible to identify the contribution of the epitope-defined single or class of cyt. P-450 to specific metabolic reactions in S9 from untreated and inducer-treated mice.</description><identifier>ISSN: 0008-5472</identifier><identifier>EISSN: 1538-7445</identifier><identifier>PMID: 3510075</identifier><identifier>CODEN: CNREA8</identifier><language>eng</language><publisher>Philadelphia, PA: American Association for Cancer Research</publisher><subject>Animals ; Antibodies, Monoclonal ; Biological and medical sciences ; Biotransformation ; Carcinogens - metabolism ; Cytochrome P-450 Enzyme System - immunology ; Cytochrome P-450 Enzyme System - metabolism ; Enzyme Activation - drug effects ; Fundamental and applied biological sciences. Psychology ; Isoenzymes - metabolism ; Liver - enzymology ; Male ; Methylcholanthrene - pharmacology ; Mice ; Mice, Inbred C57BL ; Mice, Inbred DBA ; Mixed Function Oxygenases - metabolism ; Molecular and cellular biology ; Molecular genetics ; Mutagenesis. Repair ; Mutagenicity Tests ; Phenobarbital - pharmacology ; Pregnenolone Carbonitrile - pharmacology ; Salmonella typhimurium - genetics</subject><ispartof>Cancer research (Chicago, Ill.), 1986-02, Vol.46 (2), p.524-531</ispartof><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7880905$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3510075$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>HIETANEN, E</creatorcontrib><creatorcontrib>MALAVEILLE, C</creatorcontrib><creatorcontrib>FRIEDMAN, F. K</creatorcontrib><creatorcontrib>PARK, S. S</creatorcontrib><creatorcontrib>BEREZIAT, J.-C</creatorcontrib><creatorcontrib>BRUN, G</creatorcontrib><creatorcontrib>BARTSCH, H</creatorcontrib><creatorcontrib>GELBOIN, H. V</creatorcontrib><title>Monoclonal antibody-directed analysis of cytochrome P-450-dependent monooxygenases and mutagen activation in the livers of DBA/2 and C57BL/6 mice</title><title>Cancer research (Chicago, Ill.)</title><addtitle>Cancer Res</addtitle><description>Monoclonal antibodies (MAb 1-7-1 and Mab 2-66-3) specific for cytochrome P-450 (cyt. P-450) isozymes inhibited the metabolism of carcinogens, other xenobiotics, and endogenous compounds in two strains of mice. Postmitochondrial liver supernatant (S9) was prepared from untreated, 3-methylcholanthrene-treated, phenobarbital-treated, and pregnenolone 16 alpha-carbonitrile-treated C57BL/6 (B6) and DBA/2 (D2) mice. The modifying effect of two types of MAb to a 3-methylcholanthrene-induced cyt. P-450 and a phenobarbital-induced cyt. P-450 was investigated for: (a) S9-mediated mutagenicity of aflatoxin B1, benzo(a)pyrene 7,8-dihydrodiol, 2-acetylaminofluorene, and N-nitrosomorpholine in Salmonella typhimurium strains; and (b) the activity of aryl hydrocarbon hydroxylase, ethoxycoumarin O-deethylase, ethoxyresorufin O-deethylase, aminopyrine N-demethylase, and testosterone 6 beta-, 7 alpha-, and 16 beta-hydroxylases. With certain S9s, MAb-1-7-1 inhibited only those cytochrome P-450 isozymes involved predominantly in activity of aryl hydrocarbon hydroxylase, ethoxyresorufin O-deethylase, and ethoxycoumarin O-deethylase and mutagenicity of 2-acetylaminofluorene and benzo(a)pyrene 7,8-dihydrodiol; MAb 2-66-3 inhibited only those involved in aminopyrine N-demethylase and testosterone 6 beta-, 7 alpha, and 16 beta-hydroxylase activity and aflatoxin B1 mutagenicity. Both Mab 1-7-1 and MAb 2-66-3 inhibited cytochrome P-450 isozyme(s) implicated predominantly in testosterone 7 alpha-hydroxylation in S9 from pregnenolone 16 alpha-carbonitrile-treated B6 mice. MAb 1-7-1 did not inhibit N-nitrosomorpholine mutagenicity and MAb 2-66-3 increased it by 2- to 6-fold depending on the source of S9. Using these MAbs, it is thus possible to identify the contribution of the epitope-defined single or class of cyt. P-450 to specific metabolic reactions in S9 from untreated and inducer-treated mice.</description><subject>Animals</subject><subject>Antibodies, Monoclonal</subject><subject>Biological and medical sciences</subject><subject>Biotransformation</subject><subject>Carcinogens - metabolism</subject><subject>Cytochrome P-450 Enzyme System - immunology</subject><subject>Cytochrome P-450 Enzyme System - metabolism</subject><subject>Enzyme Activation - drug effects</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Isoenzymes - metabolism</subject><subject>Liver - enzymology</subject><subject>Male</subject><subject>Methylcholanthrene - pharmacology</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Mice, Inbred DBA</subject><subject>Mixed Function Oxygenases - metabolism</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Mutagenesis. Repair</subject><subject>Mutagenicity Tests</subject><subject>Phenobarbital - pharmacology</subject><subject>Pregnenolone Carbonitrile - pharmacology</subject><subject>Salmonella typhimurium - genetics</subject><issn>0008-5472</issn><issn>1538-7445</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kMFOwzAQRC0EKqXwCUg-cLXqJt7YObaFAlIRHOBcOfaGGiV2FbsV-Qz-mKhUnEazM_sOc0bGM8gVk0LAORlzzhUDIbNLchXj12BhxmFERvmgXMKY_LwEH0wTvG6o9slVwfbMug5NQjtcdNNHF2moqelTMNsutEjfmADOLO7QW_SJtgMjfPef6HXEOHxZ2u6THjzVJrmDTi546jxNW6SNO2B3JN4v5tPs2F6CXKynBW2dwWtyUesm4s1JJ-Rj9fC-fGLr18fn5XzNtlkhEysFCkBUUIOtRQYqMwK0qosKuEAwJaBQpZSCY2Zyk1WlstyWHKEsao1FPiG3f9zdvmrRbnada3XXb07TDPndKdfR6KbutDcu_tekUrzkkP8CkMRuLg</recordid><startdate>19860201</startdate><enddate>19860201</enddate><creator>HIETANEN, E</creator><creator>MALAVEILLE, C</creator><creator>FRIEDMAN, F. K</creator><creator>PARK, S. 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Psychology</topic><topic>Isoenzymes - metabolism</topic><topic>Liver - enzymology</topic><topic>Male</topic><topic>Methylcholanthrene - pharmacology</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Mice, Inbred DBA</topic><topic>Mixed Function Oxygenases - metabolism</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Mutagenesis. Repair</topic><topic>Mutagenicity Tests</topic><topic>Phenobarbital - pharmacology</topic><topic>Pregnenolone Carbonitrile - pharmacology</topic><topic>Salmonella typhimurium - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>HIETANEN, E</creatorcontrib><creatorcontrib>MALAVEILLE, C</creatorcontrib><creatorcontrib>FRIEDMAN, F. K</creatorcontrib><creatorcontrib>PARK, S. S</creatorcontrib><creatorcontrib>BEREZIAT, J.-C</creatorcontrib><creatorcontrib>BRUN, G</creatorcontrib><creatorcontrib>BARTSCH, H</creatorcontrib><creatorcontrib>GELBOIN, H. V</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><jtitle>Cancer research (Chicago, Ill.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>HIETANEN, E</au><au>MALAVEILLE, C</au><au>FRIEDMAN, F. K</au><au>PARK, S. S</au><au>BEREZIAT, J.-C</au><au>BRUN, G</au><au>BARTSCH, H</au><au>GELBOIN, H. V</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Monoclonal antibody-directed analysis of cytochrome P-450-dependent monooxygenases and mutagen activation in the livers of DBA/2 and C57BL/6 mice</atitle><jtitle>Cancer research (Chicago, Ill.)</jtitle><addtitle>Cancer Res</addtitle><date>1986-02-01</date><risdate>1986</risdate><volume>46</volume><issue>2</issue><spage>524</spage><epage>531</epage><pages>524-531</pages><issn>0008-5472</issn><eissn>1538-7445</eissn><coden>CNREA8</coden><abstract>Monoclonal antibodies (MAb 1-7-1 and Mab 2-66-3) specific for cytochrome P-450 (cyt. P-450) isozymes inhibited the metabolism of carcinogens, other xenobiotics, and endogenous compounds in two strains of mice. Postmitochondrial liver supernatant (S9) was prepared from untreated, 3-methylcholanthrene-treated, phenobarbital-treated, and pregnenolone 16 alpha-carbonitrile-treated C57BL/6 (B6) and DBA/2 (D2) mice. The modifying effect of two types of MAb to a 3-methylcholanthrene-induced cyt. P-450 and a phenobarbital-induced cyt. P-450 was investigated for: (a) S9-mediated mutagenicity of aflatoxin B1, benzo(a)pyrene 7,8-dihydrodiol, 2-acetylaminofluorene, and N-nitrosomorpholine in Salmonella typhimurium strains; and (b) the activity of aryl hydrocarbon hydroxylase, ethoxycoumarin O-deethylase, ethoxyresorufin O-deethylase, aminopyrine N-demethylase, and testosterone 6 beta-, 7 alpha-, and 16 beta-hydroxylases. With certain S9s, MAb-1-7-1 inhibited only those cytochrome P-450 isozymes involved predominantly in activity of aryl hydrocarbon hydroxylase, ethoxyresorufin O-deethylase, and ethoxycoumarin O-deethylase and mutagenicity of 2-acetylaminofluorene and benzo(a)pyrene 7,8-dihydrodiol; MAb 2-66-3 inhibited only those involved in aminopyrine N-demethylase and testosterone 6 beta-, 7 alpha, and 16 beta-hydroxylase activity and aflatoxin B1 mutagenicity. Both Mab 1-7-1 and MAb 2-66-3 inhibited cytochrome P-450 isozyme(s) implicated predominantly in testosterone 7 alpha-hydroxylation in S9 from pregnenolone 16 alpha-carbonitrile-treated B6 mice. MAb 1-7-1 did not inhibit N-nitrosomorpholine mutagenicity and MAb 2-66-3 increased it by 2- to 6-fold depending on the source of S9. Using these MAbs, it is thus possible to identify the contribution of the epitope-defined single or class of cyt. P-450 to specific metabolic reactions in S9 from untreated and inducer-treated mice.</abstract><cop>Philadelphia, PA</cop><pub>American Association for Cancer Research</pub><pmid>3510075</pmid><tpages>8</tpages></addata></record> |
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| ispartof | Cancer research (Chicago, Ill.), 1986-02, Vol.46 (2), p.524-531 |
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| source | MEDLINE; American Association for Cancer Research; EZB-FREE-00999 freely available EZB journals |
| subjects | Animals Antibodies, Monoclonal Biological and medical sciences Biotransformation Carcinogens - metabolism Cytochrome P-450 Enzyme System - immunology Cytochrome P-450 Enzyme System - metabolism Enzyme Activation - drug effects Fundamental and applied biological sciences. Psychology Isoenzymes - metabolism Liver - enzymology Male Methylcholanthrene - pharmacology Mice Mice, Inbred C57BL Mice, Inbred DBA Mixed Function Oxygenases - metabolism Molecular and cellular biology Molecular genetics Mutagenesis. Repair Mutagenicity Tests Phenobarbital - pharmacology Pregnenolone Carbonitrile - pharmacology Salmonella typhimurium - genetics |
| title | Monoclonal antibody-directed analysis of cytochrome P-450-dependent monooxygenases and mutagen activation in the livers of DBA/2 and C57BL/6 mice |
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