Takamiya M

References (8)

Title : A novel polymorphic allele of human arylacetamide deacetylase leads to decreased enzyme activity - Shimizu_2012_Drug.Metab.Dispos_40_1183
Author(s) : Shimizu M , Fukami T , Kobayashi Y , Takamiya M , Aoki Y , Nakajima M , Yokoi T
Ref : Drug Metabolism & Disposition: The Biological Fate of Chemicals , 40 :1183 , 2012
Abstract : Human arylacetamide deacetylase (AADAC) is responsible for the hydrolysis of clinically used drugs such as flutamide, phenacetin, and rifamycins. Our recent studies suggested that human AADAC is a relevant enzyme pharmacologically and toxicologically. To date, the genetic polymorphisms that affect enzyme activity in AADAC have been unknown. In this study, we found single-nucleotide polymorphisms in the human AADAC gene in a liver sample that showed remarkably low flutamide hydrolase activity. Among them, g.13651G > A (V281I) and g.14008T > C (X400Q) were nonsynonymous. The latter would be predicted to cause a C-terminal one-amino acid (glutamine) extension. The AADAC*2 allele (g.13651G > A) was found in all populations investigated in this study (European American, African American, Korean, and Japanese), at allelic frequencies of 52.6 to 63.5%, whereas the AADAC*3 allele (g.13651G > A/g.14008T > C) was found in European American (1.3%) and African American (2.0%) samples. COS7 cells expressing AADAC.1 (wild-type) exhibited flutamide, phenacetin, and rifampicin hydrolase activities with intrinsic clearance (CLint) values of 1.31 +/- 0.06, 1.00 +/- 0.02, and 0.39 +/- 0.02 mul x min(-1) x unit(-1), respectively. AADAC.2, which is a protein produced from the AADAC*2 allele, showed moderately lower or similar CLint values, compared with AADAC.1, but AADAC.3 showed substantially lower CLint values (flutamide hydrolase, 0.21 +/- 0.02 mul x min(-1) x unit(-1); phenacetin hydrolase, 0.12 +/- 0.00 mul x min(-1) x unit(-1); rifampicin hydrolase, 0.03 +/- 0.01 mul x min(-1) x unit(-1), respectively). Microsomes from a liver sample genotyped as AADAC*3/AADAC*3 showed decreased enzyme activities, compared with those genotyped as AADAC*1/AADAC*1, AADAC*1/AADAC*2, and AADAC*2/AADAC*2. In conclusion, we found an AADAC allele that yielded decreased enzyme activity. This study should provide useful information on interindividual variations in AADAC enzyme activity.
ESTHER : Shimizu_2012_Drug.Metab.Dispos_40_1183
PubMedSearch : Shimizu_2012_Drug.Metab.Dispos_40_1183
PubMedID: 22415931
Gene_locus related to this paper: human-AADAC

Title : Genome sequences of two stress-tolerant Campylobacter jejuni poultry strains, 305 and DFVF1099 - Takamiya_2011_J.Bacteriol_193_5546
Author(s) : Takamiya M , Ozen A , Rasmussen M , Alter T , Gilbert T , Ussery DW , Knochel S
Ref : Journal of Bacteriology , 193 :5546 , 2011
Abstract : Campylobacter jejuni is a food-borne pathogen with a high prevalence in poultry meat, which in fresh unfrozen condition is the major source of campylobacteriosis. C. jejuni strains DFVF1099 and 305 are considered tolerant to several environmental stresses (T. Birk et al., J. Food Prot. 73:258-265, 2010; S. L. On et al., Int. J. Med. Microbiol. 296:353-363, 2006). Here, we report the genome sequences of C. jejuni 305 and DFVF1099, a turkey and a chicken isolate, respectively.
ESTHER : Takamiya_2011_J.Bacteriol_193_5546
PubMedSearch : Takamiya_2011_J.Bacteriol_193_5546
PubMedID: 21914871
Gene_locus related to this paper: camco-e0qbj3 , camco-q4hhu5 , camjr-q5ht69 , camju-a3yll6 , camju-Q9ZF63

Title : Genome Sequence of Campylobacter jejuni strain 327, a strain isolated from a turkey slaughterhouse - Takamiya_2011_Stand.Genomic.Sci_4_113
Author(s) : Takamiya M , Ozen A , Rasmussen M , Alter T , Gilbert T , Ussery DW , Knochel S
Ref : Stand Genomic Sci , 4 :113 , 2011
Abstract : Campylobacter is one of the leading causes of food-borne gastroenteritis and has a high prevalence in poultry. Campylobacter jejuni subsp. jejuni 327 is a subspecies of the genus Campylobacter of the family Campylobacteraceae in the phylum Proteobacteria. The microaerophilic, spiral shaped, catalase positive bacterium obtains energy from the metabolism of amino acids and Krebs cycle intermediates. Strain 327 was isolated from a turkey slaughter production line and is considered environmentally sensitive to food processing (cold, heat, drying) and storage conditions. The 327 whole genome shotgun sequence of 1,618,613 bp long consists of 1,740 protein-coding genes, 46 tRNA genes and 3 rRNA operons. A protein based BLAST analysis places the turkey isolate 327 close to the human clinical strain 81116 (NCTC 11828).
ESTHER : Takamiya_2011_Stand.Genomic.Sci_4_113
PubMedSearch : Takamiya_2011_Stand.Genomic.Sci_4_113
PubMedID: 21677848
Gene_locus related to this paper: camjr-q5ht69

Title : Human arylacetamide deacetylase is a principal enzyme in flutamide hydrolysis - Watanabe_2009_Drug.Metab.Dispos_37_1513
Author(s) : Watanabe A , Fukami T , Nakajima M , Takamiya M , Aoki Y , Yokoi T
Ref : Drug Metabolism & Disposition: The Biological Fate of Chemicals , 37 :1513 , 2009
Abstract : Flutamide, an antiandrogen drug, is widely used for the treatment of prostate cancer. The initial metabolic pathways of flutamide are hydroxylation and hydrolysis. It was recently reported that the hydrolyzed product, 4-nitro-3-(trifluoromethyl)phenylamine (FLU-1), is further metabolized to N-hydroxy FLU-1, an assumed hepatotoxicant. However, the esterase responsible for the flutamide hydrolysis has not been characterized. In the present study, we found that human arylacetamide deacetylase (AADAC) efficiently hydrolyzed flutamide using recombinant AADAC expressed in COS7 cells. In contrast, carboxylesterase1 (CES1) and CES2, which are responsible for the hydrolysis of many drugs, could not hydrolyze flutamide. AADAC is specifically expressed in the endoplasmic reticulum. Flutamide hydrolase activity was highly detected in human liver microsomes (K(m), 794 +/- 83 microM; V(max), 1.1 +/- 0.0 nmol/min/mg protein), whereas the activity was extremely low in human liver cytosol. The flutamide hydrolase activity in human liver microsomes was strongly inhibited by bis-(p-nitrophenyl)phosphate [corrected], diisopropylphosphorofluoride, and physostigmine sulfate (eserine) but moderately inhibited by sodium fluoride, phenylmethylsulfonyl fluoride, and disulfiram. The same inhibition pattern was obtained with the recombinant AADAC. Moreover, human liver and jejunum microsomes showing AADAC expression could hydrolyze flutamide, but human pulmonary and renal microsomes, which do not express AADAC, showed slight activity. In human liver microsomal samples (n = 50), the flutamide hydrolase activities were significantly correlated with the expression levels of AADAC protein (r = 0.66, p < 0.001). In conclusion, these results clearly showed that flutamide is exclusively hydrolyzed by AADAC. AADAC would be an important enzyme responsible for flutamide-induced hepatotoxicity.
ESTHER : Watanabe_2009_Drug.Metab.Dispos_37_1513
PubMedSearch : Watanabe_2009_Drug.Metab.Dispos_37_1513
PubMedID: 19339378
Gene_locus related to this paper: human-AADAC

Title : Structure and characterization of human carboxylesterase 1A1, 1A2, and 1A3 genes - Fukami_2008_Pharmacogenet.Genomics_18_911
Author(s) : Fukami T , Nakajima M , Maruichi T , Takahashi S , Takamiya M , Aoki Y , McLeod HL , Yokoi T
Ref : Pharmacogenet Genomics , 18 :911 , 2008
Abstract : OBJECTIVE: Human carboxylesterase (CES) 1A1 gene (14 exons) and CES1A3 pseudogene (six exons) are inverted and duplicated genes in a reference sequence (NT_010498). In contrast, earlier studies reported the CES1A2 gene (14 exons) instead of the CES1A3 pseudogene. The sequences of the CES1A2 gene downstream and upstream of intron 1 are identical with those of the CES1A1 and CES1A3 genes, respectively. A CES1A1 variant of which exon 1 is converted with that of the CES1A3 gene (the transcript is CES1A2) has recently been identified. We sought to clarify the confusing gene structure of human CES1A.
METHODS: A panel of 55 human liver as well as 318 blood samples (104 Caucasians, 107 African-Americans, and 107 Japanese) was used to clarify the gene structures of CES1A1, CES1A2, and CES1A3. Real-time reverse transcription-PCR and western blot analysis were carried out. Imidapril hydrolase activity in human liver microsomes and cytosol was determined by liquid chromatography-mass spectrometry (LC-MS)/MS.
RESULTS: By PCR analyses, we found that the CES1A2 gene is a variant of the CES1A3 gene. Four haplotypes, A (CES1A1 wild type and CES1A3), B (CES1A1 wild type and CES1A2), C (CES1A1 variant and CES1A3), and D (CES1A1 variant and CES1A2), were demonstrated. Ethnic differences were observed in allele frequencies of CES1A1 variant (17.3% in Caucasians and African-Americans and 25.2% in Japanese) and CES1A2 gene (14.4% in Caucasians, 5.1% in African-Americans, and 31.3% in Japanese). In human livers whose diplotype was A/A and C/C or C/D, no CES1A2 and CES1A1 mRNA was detected, respectively. In the other participants, the CES1A1 mRNA levels were higher than the CES1A2 mRNA levels. The CES1A proteins translated from CES1A1 mRNA and CES1A2 mRNA were detected in both human liver microsomes and cytosol fractions suggesting that the differences in exon 1 encoding a signal peptide did not affect the subcellular localization. Imidapril hydrolase activities reflected the CES1A protein levels. CONCLUSION: We found that the CES1A2 gene is a variant of the CES1A3 pseudogene. The findings presented here significantly increase our understanding about the gene structure and expression properties of human CES1A.
ESTHER : Fukami_2008_Pharmacogenet.Genomics_18_911
PubMedSearch : Fukami_2008_Pharmacogenet.Genomics_18_911
PubMedID: 18794728
Gene_locus related to this paper: human-CES1

Title : Complete genome sequence of an aerobic thermoacidophilic crenarchaeon, Sulfolobus tokodaii strain7 - Kawarabayasi_2001_DNA.Res_8_123
Author(s) : Kawarabayasi Y , Hino Y , Horikawa H , Jin-no K , Takahashi M , Sekine M , Baba S , Ankai A , Kosugi H , Hosoyama A , Fukui S , Nagai Y , Nishijima K , Otsuka R , Nakazawa H , Takamiya M , Kato Y , Yoshizawa T , Tanaka T , Kudoh Y , Yamazaki J , Kushida N , Oguchi A , Aoki K , Masuda S , Yanagii M , Nishimura M , Yamagishi A , Oshima T , Kikuchi H
Ref : DNA Research , 8 :123 , 2001
Abstract : The complete genomic sequence of an aerobic thermoacidophilic crenarchaeon, Sulfolobus tokodaii strain7 which optimally grows at 80 degrees C, at low pH, and under aerobic conditions, has been determined by the whole genome shotgun method with slight modifications. The genomic size was 2,694,756 bp long and the G + C content was 32.8%. The following RNA-coding genes were identified: a single 16S-23S rRNA cluster, one 5S rRNA gene and 46 tRNA genes (including 24 intron-containing tRNA genes). The repetitive sequences identified were SR-type repetitive sequences, long dispersed-type repetitive sequences and Tn-like repetitive elements. The genome contained 2826 potential protein-coding regions (open reading frames, ORFs). By similarity search against public databases, 911 (32.2%) ORFs were related to functional assigned genes, 921 (32.6%) were related to conserved ORFs of unknown function, 145 (5.1%) contained some motifs, and remaining 849 (30.0%) did not show any significant similarity to the registered sequences. The ORFs with functional assignments included the candidate genes involved in sulfide metabolism, the TCA cycle and the respiratory chain. Sequence comparison provided evidence suggesting the integration of plasmid, rearrangement of genomic structure, and duplication of genomic regions that may be responsible for the larger genomic size of the S. tokodaii strain7 genome. The genome contained eukaryote-type genes which were not identified in other archaea and lacked the CCA sequence in the tRNA genes. The result suggests that this strain is closer to eukaryotes among the archaea strains so far sequenced. The data presented in this paper are also available on the internet homepage (http:\/\/www.bio.nite.go.jp\/E-home\/genome_list-e.html\/).
ESTHER : Kawarabayasi_2001_DNA.Res_8_123
PubMedSearch : Kawarabayasi_2001_DNA.Res_8_123
PubMedID: 11572479
Gene_locus related to this paper: sulto-ST0002 , sulto-ST0071 , sulto-ST0672 , sulto-ST0779 , sulto-ST1414 , sulto-ST1737 , sulto-ST1745 , sulto-ST2026 , sulto-ST2099 , sulto-ST2511

Title : Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1 - Kawarabayasi_1999_DNA.Res_6_83
Author(s) : Kawarabayasi Y , Hino Y , Horikawa H , Yamazaki S , Haikawa Y , Jin-no K , Takahashi M , Sekine M , Baba S , Ankai A , Kosugi H , Hosoyama A , Fukui S , Nagai Y , Nishijima K , Nakazawa H , Takamiya M , Masuda S , Funahashi T , Tanaka T , Kudoh Y , Yamazaki J , Kushida N , Oguchi A , Aoki KI , Kubota K , Nakamura Y , Nomura N , Sako Y , Kikuchi H
Ref : DNA Research , 6 :83 , 1999
Abstract : The complete sequence of the genome of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1, which optimally grows at 95 degrees C, has been determined by the whole genome shotgun method with some modifications. The entire length of the genome was 1,669,695 bp. The authenticity of the entire sequence was supported by restriction analysis of long PCR products, which were directly amplified from the genomic DNA. As the potential protein-coding regions, a total of 2,694 open reading frames (ORFs) were assigned. By similarity search against public databases, 633 (23.5%) of the ORFs were related to genes with putative function and 523 (19.4%) to the sequences registered but with unknown function. All the genes in the TCA cycle except for that of alpha-ketoglutarate dehydrogenase were included, and instead of the alpha-ketoglutarate dehydrogenase gene, the genes coding for the two subunits of 2-oxoacid:ferredoxin oxidoreductase were identified. The remaining 1,538 ORFs (57.1%) did not show any significant similarity to the sequences in the databases. Sequence comparison among the assigned ORFs suggested that a considerable member of ORFs were generated by sequence duplication. The RNA genes identified were a single 16S-23S rRNA operon, two 5S rRNA genes and 47 tRNA genes including 14 genes with intron structures. All the assigned ORFs and RNA coding regions occupied 89.12% of the whole genome. The data presented in this paper are available on the internet homepage (http:\/\/www.mild.nite.go.jp).
ESTHER : Kawarabayasi_1999_DNA.Res_6_83
PubMedSearch : Kawarabayasi_1999_DNA.Res_6_83
PubMedID: 10382966
Gene_locus related to this paper: aerpe-APE1244 , aerpe-APE1547 , aerpe-APE1832 , aerpe-APE2290 , aerpe-APE2361 , aerpe-APE2441

Title : Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3 - Kawarabayasi_1998_DNA.Res_5_55
Author(s) : Kawarabayasi Y , Sawada M , Horikawa H , Haikawa Y , Hino Y , Yamamoto S , Sekine M , Baba S , Kosugi H , Hosoyama A , Nagai Y , Sakai M , Ogura K , Otsuka R , Nakazawa H , Takamiya M , Ohfuku Y , Funahashi T , Tanaka T , Kudoh Y , Yamazaki J , Kushida N , Oguchi A , Aoki K , Kikuchi H
Ref : DNA Research , 5 :55 , 1998
Abstract : The complete sequence of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3, has been determined by assembling the sequences of the physical map-based contigs of fosmid clones and of long polymerase chain reaction (PCR) products which were used for gap-filling. The entire length of the genome was 1,738,505 bp. The authenticity of the entire genome sequence was supported by restriction analysis of long PCR products, which were directly amplified from the genomic DNA. As the potential protein-coding regions, a total of 2061 open reading frames (ORFs) were assigned, and by similarity search against public databases, 406 (19.7%) were related to genes with putative function and 453 (22.0%) to the sequences registered but with unknown function. The remaining 1202 ORFs (58.3%) did not show any significant similarity to the sequences in the databases. Sequence comparison among the assigned ORFs in the genome provided evidence that a considerable number of ORFs were generated by sequence duplication. By similarity search, 11 ORFs were assumed to contain the intein elements. The RNA genes identified were a single 16S-23S rRNA operon, two 5S rRNA genes and 46 tRNA genes including two with the intron structure. All the assigned ORFs and RNA coding regions occupied 91.25% of the whole genome. The data presented in this paper are available on the internet at http:@www.nite.go.jp.
ESTHER : Kawarabayasi_1998_DNA.Res_5_55
PubMedSearch : Kawarabayasi_1998_DNA.Res_5_55
PubMedID: 9679194
Gene_locus related to this paper: pyrho-PH0594 , pyrho-PH0863 , pyrho-PH1262