Suicidal inactivation of haemoproteins by reductive metabolites of halomethanes: a structure-activity relationship study
Human haemoglobin (Hb), methaemalbumin (MHA) or rat liver microsomal cytochrome P-450 (P-450) were incubated anaerobically at μM concentrations with 1 mM carbon tetrachloride (CCl 4), trichlorobromomethane (CCl 3Br), chloroform (CHCl 3) or methylene chloride (CH 2Cl 2) in presence of 1 mM sodium dit...
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| Veröffentlicht in: | Toxicology (Amsterdam) 1995-06, Vol.100 (1), p.175-183 |
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| creator | Manno, Maurizio Tolando, Roberto Ferrara, Roberta Rezzadore, Michela Cazzaro, Stefano |
| description | Human haemoglobin (Hb), methaemalbumin (MHA) or rat liver microsomal cytochrome P-450 (P-450) were incubated anaerobically at μM concentrations with 1 mM carbon tetrachloride (CCl
4), trichlorobromomethane (CCl
3Br), chloroform (CHCl
3) or methylene chloride (CH
2Cl
2) in presence of 1 mM sodium dithionite as the reducing agent. At the end of a 5-min incubation, haem was measured by various methods i.e. binding spectrum with CO, pyridine-haemochromogen haem assay and porphyrin fluorescence, and compared for the four analogues. Statistically significant losses were observed, with all three haemoprotein systems, for CCl
3Br, CCl
4 and CHCl
3, but not CH
2Cl
2. For Hb, the loss was greater with CCl
3Br (haem assay, 63%; porphyrin fluorescence, 48%; CO binding, 24%) than with CCl
4 (haem assay, 31%) or CHCl
3 (haem assay, 13%). On the other hand, with MHA, CCl
4 gave a dramatic loss (haem assay, 88%; porphyrin fluorescence, 83%; CO binding, 67%), which was greater than that observed with CCl
3Br (haem assay, 49%; porphyrin fluorescence, 38%; CO binding, 25%). No loss was found with CHCl
3. Finally, with microsomes, the inactivation was larger with CCl
4 (CO binding, 58%; haem assay, 50%; porphyrin fluorescence, 33%) than with CCl
3Br (CO binding, 33%; haem assay, 10%) or CHCl
3 (haem assay, 9%; CO binding, 6%). In a separate set of similar experiments, an ion-pairing reverse phase HPLC method showed the formation of substrate-dependent haemderived products during incubation of CCl
3Br with Hb or microsomes, and of CCl
3 with Hb. A correlation between potential for free radical formation (
CCl
3
Br >
CCl
4 >
CHCl
3 >
CH
2
Cl
2) and extent of haem inactivation was observed with all methods for Hb, but not for microsomal P-450 or MHA. The results indicate that these halomethanes may be activated differently by different haemoproteins and suggest that their potential ability to undergo reductive metabolism may not be the only critical factor involved in P-450 haem inactivation by these chemicals. |
| doi_str_mv | 10.1016/0300-483X(95)03083-R |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_16850681</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0300483X9503083R</els_id><sourcerecordid>16850681</sourcerecordid><originalsourceid>FETCH-LOGICAL-c332t-726ce963c335839fb28da564fb3df1acbaca4346f94bb9c36cafa50e1e0cfb623</originalsourceid><addsrcrecordid>eNp9kF9rFDEUxYNY6rb6DRTmQaQ-TE0mk2ymD4IU_xQKQlXwLdxkbtjIzGRNMqX77c3sLvvoU7g5v3u45xDymtFrRpn8QDmldav476tOvC-D4vXDM7Jiat3VnCnxnKxOyAtykdIfSmnDW3lOzteyadVarMjTj9lb38NQ-Qls9o-QfZiq4KoN4Bi2MWT0U6rMrorYzwuB1YgZTBh8xnQgh1C-NjBhuqmgSjkWcI5Y7x19XnaHvXHa-G3R5373kpw5GBK-Or6X5NeXzz9vv9X337_e3X66ry3nTa7XjbTYSV4moXjnTKN6ELJ1hveOgTVgoS2ZXNca01kuLTgQFBlS64xs-CV5d_AtUf7OmLIefbI4DOXaMCfNpBJUKlbA9gDaGFKK6PQ2-hHiTjOql8L10qZe2tSd0PvC9UNZe3P0n82I_Wnp2HDR3x51SBYGF2GyPp2wkqprxYJ9PGBYunj0GHWyHieLvY9os-6D__8d_wBioqE-</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16850681</pqid></control><display><type>article</type><title>Suicidal inactivation of haemoproteins by reductive metabolites of halomethanes: a structure-activity relationship study</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Manno, Maurizio ; Tolando, Roberto ; Ferrara, Roberta ; Rezzadore, Michela ; Cazzaro, Stefano</creator><creatorcontrib>Manno, Maurizio ; Tolando, Roberto ; Ferrara, Roberta ; Rezzadore, Michela ; Cazzaro, Stefano</creatorcontrib><description>Human haemoglobin (Hb), methaemalbumin (MHA) or rat liver microsomal cytochrome P-450 (P-450) were incubated anaerobically at μM concentrations with 1 mM carbon tetrachloride (CCl
4), trichlorobromomethane (CCl
3Br), chloroform (CHCl
3) or methylene chloride (CH
2Cl
2) in presence of 1 mM sodium dithionite as the reducing agent. At the end of a 5-min incubation, haem was measured by various methods i.e. binding spectrum with CO, pyridine-haemochromogen haem assay and porphyrin fluorescence, and compared for the four analogues. Statistically significant losses were observed, with all three haemoprotein systems, for CCl
3Br, CCl
4 and CHCl
3, but not CH
2Cl
2. For Hb, the loss was greater with CCl
3Br (haem assay, 63%; porphyrin fluorescence, 48%; CO binding, 24%) than with CCl
4 (haem assay, 31%) or CHCl
3 (haem assay, 13%). On the other hand, with MHA, CCl
4 gave a dramatic loss (haem assay, 88%; porphyrin fluorescence, 83%; CO binding, 67%), which was greater than that observed with CCl
3Br (haem assay, 49%; porphyrin fluorescence, 38%; CO binding, 25%). No loss was found with CHCl
3. Finally, with microsomes, the inactivation was larger with CCl
4 (CO binding, 58%; haem assay, 50%; porphyrin fluorescence, 33%) than with CCl
3Br (CO binding, 33%; haem assay, 10%) or CHCl
3 (haem assay, 9%; CO binding, 6%). In a separate set of similar experiments, an ion-pairing reverse phase HPLC method showed the formation of substrate-dependent haemderived products during incubation of CCl
3Br with Hb or microsomes, and of CCl
3 with Hb. A correlation between potential for free radical formation (
CCl
3
Br >
CCl
4 >
CHCl
3 >
CH
2
Cl
2) and extent of haem inactivation was observed with all methods for Hb, but not for microsomal P-450 or MHA. The results indicate that these halomethanes may be activated differently by different haemoproteins and suggest that their potential ability to undergo reductive metabolism may not be the only critical factor involved in P-450 haem inactivation by these chemicals.</description><identifier>ISSN: 0300-483X</identifier><identifier>EISSN: 1879-3185</identifier><identifier>DOI: 10.1016/0300-483X(95)03083-R</identifier><identifier>PMID: 7624875</identifier><identifier>CODEN: TXICDD</identifier><language>eng</language><publisher>Shannon: Elsevier Ireland Ltd</publisher><subject>Animals ; Binding, Competitive ; Biological and medical sciences ; Bromotrichloromethane - metabolism ; Bromotrichloromethane - toxicity ; Carbon Tetrachloride - toxicity ; Chemical and industrial products toxicology. Toxic occupational diseases ; Chloroform - metabolism ; Chloroform - toxicity ; Chromatography, High Pressure Liquid ; Cytochrome P-450 ; Cytochrome P-450 Enzyme System - drug effects ; Cytochrome P-450 Enzyme System - metabolism ; Dithionite - chemistry ; Haemoglobin ; Haemoproteins ; Halomethanes ; Hemoglobins - drug effects ; Hemoglobins - metabolism ; Humans ; Hydrocarbons, Halogenated - toxicity ; Medical sciences ; Methemoglobin - drug effects ; Methemoglobin - metabolism ; Methylene Chloride - metabolism ; Methylene Chloride - toxicity ; Microsomes, Liver - drug effects ; Microsomes, Liver - enzymology ; Oxidation-Reduction ; Rats ; Structure-Activity Relationship ; Suicidal inactivation ; Toxicology ; Various organic compounds</subject><ispartof>Toxicology (Amsterdam), 1995-06, Vol.100 (1), p.175-183</ispartof><rights>1995</rights><rights>1995 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c332t-726ce963c335839fb28da564fb3df1acbaca4346f94bb9c36cafa50e1e0cfb623</citedby><cites>FETCH-LOGICAL-c332t-726ce963c335839fb28da564fb3df1acbaca4346f94bb9c36cafa50e1e0cfb623</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0300483X9503083R$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3589455$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7624875$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Manno, Maurizio</creatorcontrib><creatorcontrib>Tolando, Roberto</creatorcontrib><creatorcontrib>Ferrara, Roberta</creatorcontrib><creatorcontrib>Rezzadore, Michela</creatorcontrib><creatorcontrib>Cazzaro, Stefano</creatorcontrib><title>Suicidal inactivation of haemoproteins by reductive metabolites of halomethanes: a structure-activity relationship study</title><title>Toxicology (Amsterdam)</title><addtitle>Toxicology</addtitle><description>Human haemoglobin (Hb), methaemalbumin (MHA) or rat liver microsomal cytochrome P-450 (P-450) were incubated anaerobically at μM concentrations with 1 mM carbon tetrachloride (CCl
4), trichlorobromomethane (CCl
3Br), chloroform (CHCl
3) or methylene chloride (CH
2Cl
2) in presence of 1 mM sodium dithionite as the reducing agent. At the end of a 5-min incubation, haem was measured by various methods i.e. binding spectrum with CO, pyridine-haemochromogen haem assay and porphyrin fluorescence, and compared for the four analogues. Statistically significant losses were observed, with all three haemoprotein systems, for CCl
3Br, CCl
4 and CHCl
3, but not CH
2Cl
2. For Hb, the loss was greater with CCl
3Br (haem assay, 63%; porphyrin fluorescence, 48%; CO binding, 24%) than with CCl
4 (haem assay, 31%) or CHCl
3 (haem assay, 13%). On the other hand, with MHA, CCl
4 gave a dramatic loss (haem assay, 88%; porphyrin fluorescence, 83%; CO binding, 67%), which was greater than that observed with CCl
3Br (haem assay, 49%; porphyrin fluorescence, 38%; CO binding, 25%). No loss was found with CHCl
3. Finally, with microsomes, the inactivation was larger with CCl
4 (CO binding, 58%; haem assay, 50%; porphyrin fluorescence, 33%) than with CCl
3Br (CO binding, 33%; haem assay, 10%) or CHCl
3 (haem assay, 9%; CO binding, 6%). In a separate set of similar experiments, an ion-pairing reverse phase HPLC method showed the formation of substrate-dependent haemderived products during incubation of CCl
3Br with Hb or microsomes, and of CCl
3 with Hb. A correlation between potential for free radical formation (
CCl
3
Br >
CCl
4 >
CHCl
3 >
CH
2
Cl
2) and extent of haem inactivation was observed with all methods for Hb, but not for microsomal P-450 or MHA. The results indicate that these halomethanes may be activated differently by different haemoproteins and suggest that their potential ability to undergo reductive metabolism may not be the only critical factor involved in P-450 haem inactivation by these chemicals.</description><subject>Animals</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>Bromotrichloromethane - metabolism</subject><subject>Bromotrichloromethane - toxicity</subject><subject>Carbon Tetrachloride - toxicity</subject><subject>Chemical and industrial products toxicology. Toxic occupational diseases</subject><subject>Chloroform - metabolism</subject><subject>Chloroform - toxicity</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Cytochrome P-450</subject><subject>Cytochrome P-450 Enzyme System - drug effects</subject><subject>Cytochrome P-450 Enzyme System - metabolism</subject><subject>Dithionite - chemistry</subject><subject>Haemoglobin</subject><subject>Haemoproteins</subject><subject>Halomethanes</subject><subject>Hemoglobins - drug effects</subject><subject>Hemoglobins - metabolism</subject><subject>Humans</subject><subject>Hydrocarbons, Halogenated - toxicity</subject><subject>Medical sciences</subject><subject>Methemoglobin - drug effects</subject><subject>Methemoglobin - metabolism</subject><subject>Methylene Chloride - metabolism</subject><subject>Methylene Chloride - toxicity</subject><subject>Microsomes, Liver - drug effects</subject><subject>Microsomes, Liver - enzymology</subject><subject>Oxidation-Reduction</subject><subject>Rats</subject><subject>Structure-Activity Relationship</subject><subject>Suicidal inactivation</subject><subject>Toxicology</subject><subject>Various organic compounds</subject><issn>0300-483X</issn><issn>1879-3185</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kF9rFDEUxYNY6rb6DRTmQaQ-TE0mk2ymD4IU_xQKQlXwLdxkbtjIzGRNMqX77c3sLvvoU7g5v3u45xDymtFrRpn8QDmldav476tOvC-D4vXDM7Jiat3VnCnxnKxOyAtykdIfSmnDW3lOzteyadVarMjTj9lb38NQ-Qls9o-QfZiq4KoN4Bi2MWT0U6rMrorYzwuB1YgZTBh8xnQgh1C-NjBhuqmgSjkWcI5Y7x19XnaHvXHa-G3R5373kpw5GBK-Or6X5NeXzz9vv9X337_e3X66ry3nTa7XjbTYSV4moXjnTKN6ELJ1hveOgTVgoS2ZXNca01kuLTgQFBlS64xs-CV5d_AtUf7OmLIefbI4DOXaMCfNpBJUKlbA9gDaGFKK6PQ2-hHiTjOql8L10qZe2tSd0PvC9UNZe3P0n82I_Wnp2HDR3x51SBYGF2GyPp2wkqprxYJ9PGBYunj0GHWyHieLvY9os-6D__8d_wBioqE-</recordid><startdate>19950626</startdate><enddate>19950626</enddate><creator>Manno, Maurizio</creator><creator>Tolando, Roberto</creator><creator>Ferrara, Roberta</creator><creator>Rezzadore, Michela</creator><creator>Cazzaro, Stefano</creator><general>Elsevier Ireland Ltd</general><general>Elsevier Science</general><scope>IQODW</scope><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>7U7</scope><scope>C1K</scope></search><sort><creationdate>19950626</creationdate><title>Suicidal inactivation of haemoproteins by reductive metabolites of halomethanes: a structure-activity relationship study</title><author>Manno, Maurizio ; Tolando, Roberto ; Ferrara, Roberta ; Rezzadore, Michela ; Cazzaro, Stefano</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c332t-726ce963c335839fb28da564fb3df1acbaca4346f94bb9c36cafa50e1e0cfb623</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Animals</topic><topic>Binding, Competitive</topic><topic>Biological and medical sciences</topic><topic>Bromotrichloromethane - metabolism</topic><topic>Bromotrichloromethane - toxicity</topic><topic>Carbon Tetrachloride - toxicity</topic><topic>Chemical and industrial products toxicology. Toxic occupational diseases</topic><topic>Chloroform - metabolism</topic><topic>Chloroform - toxicity</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Cytochrome P-450</topic><topic>Cytochrome P-450 Enzyme System - drug effects</topic><topic>Cytochrome P-450 Enzyme System - metabolism</topic><topic>Dithionite - chemistry</topic><topic>Haemoglobin</topic><topic>Haemoproteins</topic><topic>Halomethanes</topic><topic>Hemoglobins - drug effects</topic><topic>Hemoglobins - metabolism</topic><topic>Humans</topic><topic>Hydrocarbons, Halogenated - toxicity</topic><topic>Medical sciences</topic><topic>Methemoglobin - drug effects</topic><topic>Methemoglobin - metabolism</topic><topic>Methylene Chloride - metabolism</topic><topic>Methylene Chloride - toxicity</topic><topic>Microsomes, Liver - drug effects</topic><topic>Microsomes, Liver - enzymology</topic><topic>Oxidation-Reduction</topic><topic>Rats</topic><topic>Structure-Activity Relationship</topic><topic>Suicidal inactivation</topic><topic>Toxicology</topic><topic>Various organic compounds</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Manno, Maurizio</creatorcontrib><creatorcontrib>Tolando, Roberto</creatorcontrib><creatorcontrib>Ferrara, Roberta</creatorcontrib><creatorcontrib>Rezzadore, Michela</creatorcontrib><creatorcontrib>Cazzaro, Stefano</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Toxicology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Toxicology (Amsterdam)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Manno, Maurizio</au><au>Tolando, Roberto</au><au>Ferrara, Roberta</au><au>Rezzadore, Michela</au><au>Cazzaro, Stefano</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Suicidal inactivation of haemoproteins by reductive metabolites of halomethanes: a structure-activity relationship study</atitle><jtitle>Toxicology (Amsterdam)</jtitle><addtitle>Toxicology</addtitle><date>1995-06-26</date><risdate>1995</risdate><volume>100</volume><issue>1</issue><spage>175</spage><epage>183</epage><pages>175-183</pages><issn>0300-483X</issn><eissn>1879-3185</eissn><coden>TXICDD</coden><abstract>Human haemoglobin (Hb), methaemalbumin (MHA) or rat liver microsomal cytochrome P-450 (P-450) were incubated anaerobically at μM concentrations with 1 mM carbon tetrachloride (CCl
4), trichlorobromomethane (CCl
3Br), chloroform (CHCl
3) or methylene chloride (CH
2Cl
2) in presence of 1 mM sodium dithionite as the reducing agent. At the end of a 5-min incubation, haem was measured by various methods i.e. binding spectrum with CO, pyridine-haemochromogen haem assay and porphyrin fluorescence, and compared for the four analogues. Statistically significant losses were observed, with all three haemoprotein systems, for CCl
3Br, CCl
4 and CHCl
3, but not CH
2Cl
2. For Hb, the loss was greater with CCl
3Br (haem assay, 63%; porphyrin fluorescence, 48%; CO binding, 24%) than with CCl
4 (haem assay, 31%) or CHCl
3 (haem assay, 13%). On the other hand, with MHA, CCl
4 gave a dramatic loss (haem assay, 88%; porphyrin fluorescence, 83%; CO binding, 67%), which was greater than that observed with CCl
3Br (haem assay, 49%; porphyrin fluorescence, 38%; CO binding, 25%). No loss was found with CHCl
3. Finally, with microsomes, the inactivation was larger with CCl
4 (CO binding, 58%; haem assay, 50%; porphyrin fluorescence, 33%) than with CCl
3Br (CO binding, 33%; haem assay, 10%) or CHCl
3 (haem assay, 9%; CO binding, 6%). In a separate set of similar experiments, an ion-pairing reverse phase HPLC method showed the formation of substrate-dependent haemderived products during incubation of CCl
3Br with Hb or microsomes, and of CCl
3 with Hb. A correlation between potential for free radical formation (
CCl
3
Br >
CCl
4 >
CHCl
3 >
CH
2
Cl
2) and extent of haem inactivation was observed with all methods for Hb, but not for microsomal P-450 or MHA. The results indicate that these halomethanes may be activated differently by different haemoproteins and suggest that their potential ability to undergo reductive metabolism may not be the only critical factor involved in P-450 haem inactivation by these chemicals.</abstract><cop>Shannon</cop><cop>Amsterdam</cop><pub>Elsevier Ireland Ltd</pub><pmid>7624875</pmid><doi>10.1016/0300-483X(95)03083-R</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0300-483X |
| ispartof | Toxicology (Amsterdam), 1995-06, Vol.100 (1), p.175-183 |
| issn | 0300-483X 1879-3185 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_16850681 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals Binding, Competitive Biological and medical sciences Bromotrichloromethane - metabolism Bromotrichloromethane - toxicity Carbon Tetrachloride - toxicity Chemical and industrial products toxicology. Toxic occupational diseases Chloroform - metabolism Chloroform - toxicity Chromatography, High Pressure Liquid Cytochrome P-450 Cytochrome P-450 Enzyme System - drug effects Cytochrome P-450 Enzyme System - metabolism Dithionite - chemistry Haemoglobin Haemoproteins Halomethanes Hemoglobins - drug effects Hemoglobins - metabolism Humans Hydrocarbons, Halogenated - toxicity Medical sciences Methemoglobin - drug effects Methemoglobin - metabolism Methylene Chloride - metabolism Methylene Chloride - toxicity Microsomes, Liver - drug effects Microsomes, Liver - enzymology Oxidation-Reduction Rats Structure-Activity Relationship Suicidal inactivation Toxicology Various organic compounds |
| title | Suicidal inactivation of haemoproteins by reductive metabolites of halomethanes: a structure-activity relationship study |
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