CYP2D6-debrisoquine hydroxylase gene polymorphism in multiple system atrophy.
Identifieur interne : 004721 ( Ncbi/Checkpoint ); précédent : 004720; suivant : 004722CYP2D6-debrisoquine hydroxylase gene polymorphism in multiple system atrophy.
Auteurs : V. Planté-Bordeneuve [Royaume-Uni] ; O. Bandmann ; G. Wenning ; N P Quinn ; S E Daniel ; A E HardingSource :
- Movement disorders : official journal of the Movement Disorder Society [ 0885-3185 ] ; 1995.
English descriptors
- KwdEn :
- Alleles, Cytochrome P-450 CYP2D6, Cytochrome P-450 Enzyme System (genetics), DNA Mutational Analysis, Gene Expression (physiology), Gene Frequency (genetics), Genotype, Humans, Mixed Function Oxygenases (genetics), Olivopontocerebellar Atrophies (genetics), Parkinson Disease (genetics), Polymorphism, Genetic (genetics).
- MESH :
- chemical , genetics : Cytochrome P-450 Enzyme System, Mixed Function Oxygenases.
- chemical : Cytochrome P-450 CYP2D6.
- genetics : Gene Frequency, Olivopontocerebellar Atrophies, Parkinson Disease, Polymorphism, Genetic.
- physiology : Gene Expression.
- Alleles, DNA Mutational Analysis, Genotype, Humans.
Abstract
Molecular genetic studies of the cytochrome P450 system enzyme CYP2D6, which hydroxylates debrisoquine, have indicated an excess of mutant alleles in large series of patients with Parkinson's disease (PD) when compared with controls. We have investigated CYP2D6 polymorphism in 91 patients with multiple system atrophy (MSA) in order to determine if this finding is specific to PD or if there is similar evidence of genetic susceptibility to neurotoxicity in MSA. The distribution of CYP2D6 alleles was not significantly different between MSA patients and controls, and there were fewer poor metabolisers in the MSA group than in the control group.
DOI: 10.1002/mds.870100307
PubMed: 7651442
Affiliations:
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pubmed:7651442Le document en format XML
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<country>Royaume-Uni</country>
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<wicri:cityArea>University Department of Clinical Neurology (Neurogenetics and Movement Disorders Sections and Parkinson's Disease Society Brain Bank), Institute of Neurology, London</wicri:cityArea>
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<author><name sortKey="Quinn, N P" sort="Quinn, N P" uniqKey="Quinn N" first="N P" last="Quinn">N P Quinn</name>
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<author><name sortKey="Daniel, S E" sort="Daniel, S E" uniqKey="Daniel S" first="S E" last="Daniel">S E Daniel</name>
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<author><name sortKey="Harding, A E" sort="Harding, A E" uniqKey="Harding A" first="A E" last="Harding">A E Harding</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">CYP2D6-debrisoquine hydroxylase gene polymorphism in multiple system atrophy.</title>
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<term>DNA Mutational Analysis</term>
<term>Gene Expression (physiology)</term>
<term>Gene Frequency (genetics)</term>
<term>Genotype</term>
<term>Humans</term>
<term>Mixed Function Oxygenases (genetics)</term>
<term>Olivopontocerebellar Atrophies (genetics)</term>
<term>Parkinson Disease (genetics)</term>
<term>Polymorphism, Genetic (genetics)</term>
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<term>Polymorphism, Genetic</term>
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<front><div type="abstract" xml:lang="en">Molecular genetic studies of the cytochrome P450 system enzyme CYP2D6, which hydroxylates debrisoquine, have indicated an excess of mutant alleles in large series of patients with Parkinson's disease (PD) when compared with controls. We have investigated CYP2D6 polymorphism in 91 patients with multiple system atrophy (MSA) in order to determine if this finding is specific to PD or if there is similar evidence of genetic susceptibility to neurotoxicity in MSA. The distribution of CYP2D6 alleles was not significantly different between MSA patients and controls, and there were fewer poor metabolisers in the MSA group than in the control group.</div>
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<name sortKey="Quinn, N P" sort="Quinn, N P" uniqKey="Quinn N" first="N P" last="Quinn">N P Quinn</name>
<name sortKey="Wenning, G" sort="Wenning, G" uniqKey="Wenning G" first="G" last="Wenning">G. Wenning</name>
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<country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Plante Bordeneuve, V" sort="Plante Bordeneuve, V" uniqKey="Plante Bordeneuve V" first="V" last="Planté-Bordeneuve">V. Planté-Bordeneuve</name>
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