The molecular basis of the human serum paraoxonase activity polymorphism
The organophosphate cholinesterase inhibitor paraoxon is hydrolysed by serum paraoxonase/arylesterase. A genetic polymorphism of paraoxonase (PON) activity which determines high versus low paraoxon hydrolysis in human populations, may determine sensitivity to parathion poisoning. We demonstrate that...
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| Veröffentlicht in: | Nature genetics 1993-01, Vol.3 (1), p.73-76 |
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| container_title | Nature genetics |
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| creator | Humbert, Richard Adler, David A. Disteche, Christine M. Hassett, Christopher Omiecinski, Curtis J. Furlong, Clement E. |
| description | The organophosphate cholinesterase inhibitor paraoxon is hydrolysed by serum paraoxonase/arylesterase. A genetic polymorphism of paraoxonase (PON) activity which determines high versus low paraoxon hydrolysis in human populations, may determine sensitivity to parathion poisoning. We demonstrate that arginine at position 192 specifies high activity PON whereas a glutamine specifies the low activity variant. Allele–specific probes or restriction enzyme analysis of amplified DNA allow for the genotyping of individuals. PON maps to chromosome 7q21–22, proximal to the cystic fibrosis gene, in agreement with previous genetic linkage studies. |
| doi_str_mv | 10.1038/ng0193-73 |
| format | Article |
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A genetic polymorphism of paraoxonase (PON) activity which determines high versus low paraoxon hydrolysis in human populations, may determine sensitivity to parathion poisoning. We demonstrate that arginine at position 192 specifies high activity PON whereas a glutamine specifies the low activity variant. Allele–specific probes or restriction enzyme analysis of amplified DNA allow for the genotyping of individuals. PON maps to chromosome 7q21–22, proximal to the cystic fibrosis gene, in agreement with previous genetic linkage studies.</description><identifier>ISSN: 1061-4036</identifier><identifier>EISSN: 1546-1718</identifier><identifier>DOI: 10.1038/ng0193-73</identifier><identifier>PMID: 8098250</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Agriculture ; Animal Genetics and Genomics ; Aryldialkylphosphatase ; arylesterase ; Base Sequence ; Biomedical and Life Sciences ; Biomedicine ; Cancer Research ; chromosome 7 ; Chromosomes, Human, Pair 7 ; Cloning, Molecular ; DNA ; Gene Function ; Human Genetics ; Humans ; man ; mapping ; Molecular Sequence Data ; Paraoxon ; Phosphoric Monoester Hydrolases - blood ; Phosphoric Monoester Hydrolases - genetics ; Polymorphism, Restriction Fragment Length ; restriction fragment length polymorphism</subject><ispartof>Nature genetics, 1993-01, Vol.3 (1), p.73-76</ispartof><rights>Springer Nature America, Inc. 1993</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-2fe9080c161b30e1a81621a78f613fb0ee0b30fbcf10fc1ce551dfcfb8e6d8913</citedby><cites>FETCH-LOGICAL-c412t-2fe9080c161b30e1a81621a78f613fb0ee0b30fbcf10fc1ce551dfcfb8e6d8913</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/ng0193-73$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/ng0193-73$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8098250$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Humbert, Richard</creatorcontrib><creatorcontrib>Adler, David A.</creatorcontrib><creatorcontrib>Disteche, Christine M.</creatorcontrib><creatorcontrib>Hassett, Christopher</creatorcontrib><creatorcontrib>Omiecinski, Curtis J.</creatorcontrib><creatorcontrib>Furlong, Clement E.</creatorcontrib><title>The molecular basis of the human serum paraoxonase activity polymorphism</title><title>Nature genetics</title><addtitle>Nat Genet</addtitle><addtitle>Nat Genet</addtitle><description>The organophosphate cholinesterase inhibitor paraoxon is hydrolysed by serum paraoxonase/arylesterase. A genetic polymorphism of paraoxonase (PON) activity which determines high versus low paraoxon hydrolysis in human populations, may determine sensitivity to parathion poisoning. We demonstrate that arginine at position 192 specifies high activity PON whereas a glutamine specifies the low activity variant. Allele–specific probes or restriction enzyme analysis of amplified DNA allow for the genotyping of individuals. PON maps to chromosome 7q21–22, proximal to the cystic fibrosis gene, in agreement with previous genetic linkage studies.</description><subject>Agriculture</subject><subject>Animal Genetics and Genomics</subject><subject>Aryldialkylphosphatase</subject><subject>arylesterase</subject><subject>Base Sequence</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cancer Research</subject><subject>chromosome 7</subject><subject>Chromosomes, Human, Pair 7</subject><subject>Cloning, Molecular</subject><subject>DNA</subject><subject>Gene Function</subject><subject>Human Genetics</subject><subject>Humans</subject><subject>man</subject><subject>mapping</subject><subject>Molecular Sequence Data</subject><subject>Paraoxon</subject><subject>Phosphoric Monoester Hydrolases - blood</subject><subject>Phosphoric Monoester Hydrolases - genetics</subject><subject>Polymorphism, Restriction Fragment Length</subject><subject>restriction fragment length polymorphism</subject><issn>1061-4036</issn><issn>1546-1718</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkEFLw0AQhRdRaq0e_AFCToJCdCabbLZHKWqFgpd6DpvtbJuSZONuIvbfu5LiydM83vt4MI-xa4QHBC4f2y3gnMc5P2FTzFIRY47yNGgQGKfAxTm78H4PgGkKcsImEuYyyWDKlusdRY2tSQ-1clGpfOUja6I-2LuhUW3kyQ1N1Cmn7LdtladI6b76qvpD1Nn60FjX7SrfXLIzo2pPV8c7Yx8vz-vFMl69v74tnlaxTjHp48TQHCRoFFhyIFQSRYIql0YgNyUQQfBNqQ2C0agpy3BjtCkliY2cI5-x27G3c_ZzIN8XTeU11bVqyQ6-QJEmXIg8gHcjqJ313pEpOlc1yh0KhOJ3tWJcrch5YG-OpUPZ0OaPPM4U8vsx9yFpt-SKvR1cG_78p-wH7Ad2bw</recordid><startdate>19930101</startdate><enddate>19930101</enddate><creator>Humbert, Richard</creator><creator>Adler, David A.</creator><creator>Disteche, Christine M.</creator><creator>Hassett, Christopher</creator><creator>Omiecinski, Curtis J.</creator><creator>Furlong, Clement E.</creator><general>Springer US</general><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>7T3</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>19930101</creationdate><title>The molecular basis of the human serum paraoxonase activity polymorphism</title><author>Humbert, Richard ; 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A genetic polymorphism of paraoxonase (PON) activity which determines high versus low paraoxon hydrolysis in human populations, may determine sensitivity to parathion poisoning. We demonstrate that arginine at position 192 specifies high activity PON whereas a glutamine specifies the low activity variant. Allele–specific probes or restriction enzyme analysis of amplified DNA allow for the genotyping of individuals. PON maps to chromosome 7q21–22, proximal to the cystic fibrosis gene, in agreement with previous genetic linkage studies.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>8098250</pmid><doi>10.1038/ng0193-73</doi><tpages>4</tpages></addata></record> |
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| ispartof | Nature genetics, 1993-01, Vol.3 (1), p.73-76 |
| issn | 1061-4036 1546-1718 |
| language | eng |
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| source | MEDLINE; Nature Journals Online; SpringerLink Journals - AutoHoldings |
| subjects | Agriculture Animal Genetics and Genomics Aryldialkylphosphatase arylesterase Base Sequence Biomedical and Life Sciences Biomedicine Cancer Research chromosome 7 Chromosomes, Human, Pair 7 Cloning, Molecular DNA Gene Function Human Genetics Humans man mapping Molecular Sequence Data Paraoxon Phosphoric Monoester Hydrolases - blood Phosphoric Monoester Hydrolases - genetics Polymorphism, Restriction Fragment Length restriction fragment length polymorphism |
| title | The molecular basis of the human serum paraoxonase activity polymorphism |
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