Abstract
CYP2C19 is a clinically important enzyme involved in the metabolism of therapeutic drugs such as (S)-mephenytoin, omeprazole, proguanil, and diazepam. Individuals can be characterized as either extensive metabolizers (EM) or poor metabolizers (PM) on the basis of CYP2C19 enzyme activity. The PM phenotype occurs in 2-5% of Caucasian populations, but at higher frequencies (18-23%) in Asians. CYP2C19*2 and CYP2C19*3, which are single-nucleotide polymorphisms of CYP2C19, are the main cause of PM phenotyping in homozygotes or compound heterozygotes. We report two novel mutations in the CYP2C19 gene identified by direct sequencing and subcloning procedures. One of these mutations was considered to be CYP2C19*3 by polymerase chain reaction restriction fragment length polymorphism (PCR-RFLP). This result suggests that mutations classed as CYP2C19*3 might include other mutations. Further studies are needed to clarify the relationship between these novel mutations and enzyme activity.
| Original language | English |
|---|---|
| Pages (from-to) | 118-123 |
| Number of pages | 6 |
| Journal | Journal of Human Genetics |
| Volume | 51 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 01-02-2006 |
Fingerprint
All Science Journal Classification (ASJC) codes
- Genetics
- Genetics(clinical)
Cite this
}
Novel mutations in the cytochrome P450 2C19 gene : A pitfall of the PCR-RFLP method for identifying a common mutation. / Ohkubo, Yumiko; Ueta, Akihito; Ando, Naoki; Ito, Tetsuya; Yamaguchi, Sachiko; Mizuno, Kantaro; Sumi, Satoshi; Maeda, Tohru; Yamazaki, Daiju; Kurono, Yukihisa; Fujimoto, Shinji; Togari, Hajime.
In: Journal of Human Genetics, Vol. 51, No. 2, 01.02.2006, p. 118-123.Research output: Contribution to journal › Article
TY - JOUR
T1 - Novel mutations in the cytochrome P450 2C19 gene
T2 - A pitfall of the PCR-RFLP method for identifying a common mutation
AU - Ohkubo, Yumiko
AU - Ueta, Akihito
AU - Ando, Naoki
AU - Ito, Tetsuya
AU - Yamaguchi, Sachiko
AU - Mizuno, Kantaro
AU - Sumi, Satoshi
AU - Maeda, Tohru
AU - Yamazaki, Daiju
AU - Kurono, Yukihisa
AU - Fujimoto, Shinji
AU - Togari, Hajime
PY - 2006/2/1
Y1 - 2006/2/1
N2 - CYP2C19 is a clinically important enzyme involved in the metabolism of therapeutic drugs such as (S)-mephenytoin, omeprazole, proguanil, and diazepam. Individuals can be characterized as either extensive metabolizers (EM) or poor metabolizers (PM) on the basis of CYP2C19 enzyme activity. The PM phenotype occurs in 2-5% of Caucasian populations, but at higher frequencies (18-23%) in Asians. CYP2C19*2 and CYP2C19*3, which are single-nucleotide polymorphisms of CYP2C19, are the main cause of PM phenotyping in homozygotes or compound heterozygotes. We report two novel mutations in the CYP2C19 gene identified by direct sequencing and subcloning procedures. One of these mutations was considered to be CYP2C19*3 by polymerase chain reaction restriction fragment length polymorphism (PCR-RFLP). This result suggests that mutations classed as CYP2C19*3 might include other mutations. Further studies are needed to clarify the relationship between these novel mutations and enzyme activity.
AB - CYP2C19 is a clinically important enzyme involved in the metabolism of therapeutic drugs such as (S)-mephenytoin, omeprazole, proguanil, and diazepam. Individuals can be characterized as either extensive metabolizers (EM) or poor metabolizers (PM) on the basis of CYP2C19 enzyme activity. The PM phenotype occurs in 2-5% of Caucasian populations, but at higher frequencies (18-23%) in Asians. CYP2C19*2 and CYP2C19*3, which are single-nucleotide polymorphisms of CYP2C19, are the main cause of PM phenotyping in homozygotes or compound heterozygotes. We report two novel mutations in the CYP2C19 gene identified by direct sequencing and subcloning procedures. One of these mutations was considered to be CYP2C19*3 by polymerase chain reaction restriction fragment length polymorphism (PCR-RFLP). This result suggests that mutations classed as CYP2C19*3 might include other mutations. Further studies are needed to clarify the relationship between these novel mutations and enzyme activity.
UR - http://www.scopus.com/inward/record.url?scp=31544461302&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=31544461302&partnerID=8YFLogxK
U2 - 10.1007/s10038-005-0332-y
DO - 10.1007/s10038-005-0332-y
M3 - Article
C2 - 16307177
AN - SCOPUS:31544461302
VL - 51
SP - 118
EP - 123
JO - Journal of Human Genetics
JF - Journal of Human Genetics
SN - 1434-5161
IS - 2
ER -