Polymorphisms of CYP2A6 and its practical consequences
Identifieur interne : 004771 ( Pmc/Corpus ); précédent : 004770; suivant : 004772Polymorphisms of CYP2A6 and its practical consequences
Auteurs : Hannu Raunio ; Arja Rautio ; Harriet Gullstén ; Olavi PelkonenSource :
- British Journal of Clinical Pharmacology [ 0306-5251 ] ; 2001.
Abstract
CYP2A6 is an hepatic enzyme predominantly with some expression in specialized extrahepatic cell types. The CYP2A6 enzyme has a somewhat restricted active site, accepting only a few xenobiotics as substrates. Interest in CYP2A6 has risen considerably after nicotine and some tobacco specific nitrosamines were established as high-affinity substrates for this enzyme. Recently, the organization and structures of the
Url:
DOI: 10.1046/j.0306-5251.2001.01500.x
PubMed: 11678779
PubMed Central: 2014580
Links to Exploration step
PMC:2014580Le document en format XML
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<author><name sortKey="Raunio, Hannu" sort="Raunio, Hannu" uniqKey="Raunio H" first="Hannu" last="Raunio">Hannu Raunio</name>
<affiliation><nlm:aff id="au1"><institution>Department of Pharmacology and Toxicology, University of Kuopio</institution>
<addr-line>Box1627, 70211 Kuopio, Finland</addr-line>
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<author><name sortKey="Rautio, Arja" sort="Rautio, Arja" uniqKey="Rautio A" first="Arja" last="Rautio">Arja Rautio</name>
<affiliation><nlm:aff id="au2"><institution>Department of Pharmacology and Toxicology, University of Oulu</institution>
<addr-line>Box 5000, 90014 Oulu, Finland</addr-line>
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<author><name sortKey="Gullsten, Harriet" sort="Gullsten, Harriet" uniqKey="Gullsten H" first="Harriet" last="Gullstén">Harriet Gullstén</name>
<affiliation><nlm:aff id="au2"><institution>Department of Pharmacology and Toxicology, University of Oulu</institution>
<addr-line>Box 5000, 90014 Oulu, Finland</addr-line>
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<author><name sortKey="Pelkonen, Olavi" sort="Pelkonen, Olavi" uniqKey="Pelkonen O" first="Olavi" last="Pelkonen">Olavi Pelkonen</name>
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<author><name sortKey="Rautio, Arja" sort="Rautio, Arja" uniqKey="Rautio A" first="Arja" last="Rautio">Arja Rautio</name>
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<author><name sortKey="Gullsten, Harriet" sort="Gullsten, Harriet" uniqKey="Gullsten H" first="Harriet" last="Gullstén">Harriet Gullstén</name>
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<author><name sortKey="Pelkonen, Olavi" sort="Pelkonen, Olavi" uniqKey="Pelkonen O" first="Olavi" last="Pelkonen">Olavi Pelkonen</name>
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<series><title level="j">British Journal of Clinical Pharmacology</title>
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<front><div type="abstract" xml:lang="en"><p>CYP2A6 is an hepatic enzyme predominantly with some expression in specialized extrahepatic cell types. The CYP2A6 enzyme has a somewhat restricted active site, accepting only a few xenobiotics as substrates. Interest in CYP2A6 has risen considerably after nicotine and some tobacco specific nitrosamines were established as high-affinity substrates for this enzyme. Recently, the organization and structures of the <italic>CYP2A</italic>
gene cluster and several polymorphic alleles of the <italic>CYP2A6</italic>
gene have been characterized. Two alleles with a point mutation and at least three different types of gene deletion, all leading to deficient gene function, have been found. The frequencies of these alleles vary considerably among different ethnic populations, the deletion alleles being most common in Orientals (up to 20%). The frequency of point mutations are low in all populations studied thus far (< 3%). Several case-control studies have addressed the relationship between CYP2A6 status and smoking habits as well as the role of CYP2A6 polymorphism in lung cancer risk. Studies in Japanese suggest that CYP2A6 poor metabolizer genotypes result in altered nicotine kinetics and may lower cigarette smoking elicited lung cancer risk, whereas similar studies in Caucasian populations have not revealed any clear associations between variant CYP2A6 genotypes and smoking behaviour or lung cancer predisposition.</p>
</div>
</front>
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<pmc article-type="review-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Br J Clin Pharmacol</journal-id>
<journal-id journal-id-type="publisher-id">bcp</journal-id>
<journal-title>British Journal of Clinical Pharmacology</journal-title>
<issn pub-type="ppub">0306-5251</issn>
<issn pub-type="epub">1365-2125</issn>
<publisher><publisher-name>Blackwell Science Inc</publisher-name>
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<article-id pub-id-type="doi">10.1046/j.0306-5251.2001.01500.x</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Review Series Review Series on Pharmacogenomics edited by Prof. M. Pirmohamed</subject>
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<title-group><article-title>Polymorphisms of CYP2A6 and its practical consequences</article-title>
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<contrib-group><contrib contrib-type="author"><name><surname>Raunio</surname>
<given-names>Hannu</given-names>
</name>
<xref ref-type="aff" rid="au1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Rautio</surname>
<given-names>Arja</given-names>
</name>
<xref ref-type="aff" rid="au2">2</xref>
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<contrib contrib-type="author"><name><surname>Gullstén</surname>
<given-names>Harriet</given-names>
</name>
<xref ref-type="aff" rid="au2">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Pelkonen</surname>
<given-names>Olavi</given-names>
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<xref ref-type="aff" rid="au2">2</xref>
</contrib>
<aff id="au1"><label>1</label>
<institution>Department of Pharmacology and Toxicology, University of Kuopio</institution>
<addr-line>Box1627, 70211 Kuopio, Finland</addr-line>
</aff>
<aff id="au2"><label>2</label>
<institution>Department of Pharmacology and Toxicology, University of Oulu</institution>
<addr-line>Box 5000, 90014 Oulu, Finland</addr-line>
</aff>
</contrib-group>
<author-notes><corresp id="cor1">Correspondence: Hannu Raunio, Department of Pharmacology and Toxicology, University of Kuopio, Box 1627, 70211 Kuopio, Finland. Tel.: + 358 17 162406; Fax: + 358 17 162424; E-mail: <email>hannu.raunio@uku.fi</email>
</corresp>
</author-notes>
<pub-date pub-type="ppub"><month>10</month>
<year>2001</year>
</pub-date>
<volume>52</volume>
<issue>4</issue>
<fpage>357</fpage>
<lpage>363</lpage>
<history><date date-type="received"><day>20</day>
<month>6</month>
<year>2000</year>
</date>
<date date-type="accepted"><day>12</day>
<month>7</month>
<year>2001</year>
</date>
</history>
<copyright-statement>© 2001 Blackwell Science Ltd</copyright-statement>
<copyright-year>2001</copyright-year>
<abstract><p>CYP2A6 is an hepatic enzyme predominantly with some expression in specialized extrahepatic cell types. The CYP2A6 enzyme has a somewhat restricted active site, accepting only a few xenobiotics as substrates. Interest in CYP2A6 has risen considerably after nicotine and some tobacco specific nitrosamines were established as high-affinity substrates for this enzyme. Recently, the organization and structures of the <italic>CYP2A</italic>
gene cluster and several polymorphic alleles of the <italic>CYP2A6</italic>
gene have been characterized. Two alleles with a point mutation and at least three different types of gene deletion, all leading to deficient gene function, have been found. The frequencies of these alleles vary considerably among different ethnic populations, the deletion alleles being most common in Orientals (up to 20%). The frequency of point mutations are low in all populations studied thus far (< 3%). Several case-control studies have addressed the relationship between CYP2A6 status and smoking habits as well as the role of CYP2A6 polymorphism in lung cancer risk. Studies in Japanese suggest that CYP2A6 poor metabolizer genotypes result in altered nicotine kinetics and may lower cigarette smoking elicited lung cancer risk, whereas similar studies in Caucasian populations have not revealed any clear associations between variant CYP2A6 genotypes and smoking behaviour or lung cancer predisposition.</p>
</abstract>
<kwd-group><kwd>coumarin</kwd>
<kwd>lung cancer</kwd>
<kwd>nicotine</kwd>
<kwd>tobacco smoke</kwd>
</kwd-group>
</article-meta>
</front>
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