Muramatsu M

References (6)

Title : Functional polymorphisms in carboxylesterase1A2 (CES1A2) gene involves specific protein 1 (Sp1) binding sites - Yoshimura_2008_Biochem.Biophys.Res.Commun_369_939
Author(s) : Yoshimura M , Kimura T , Ishii M , Ishii K , Matsuura T , Geshi E , Hosokawa M , Muramatsu M
Ref : Biochemical & Biophysical Research Communications , 369 :939 , 2008
Abstract : Carboxylesterase 1 (CES1) is involved in metabolic activation of a variety of prodrugs into active derivatives and plays an important role in pharmacokinetics. We previously reported that a single nucleotide polymorphism (SNP), -816A/C of the CES1A2 gene associates with the responsiveness to an angiotensin-converting enzyme (ACE) inhibitor, imidapril, whose activity is achieved by CES1. To identify relevant functional polymorphisms, we re-sequenced the CES1A2 promoter region ( approximately 1kb) in 100 Japanese hypertensive patients. Altogether 10 SNPs and one insertion/deletion (I/D) were identified, among which seven SNPs and one I/D residing between -62 and -32 were in almost complete linkage disequilibrium (D'=1.00, r2=0.97). They consisted a minor and a major haplotype, the allele frequencies of which were 22% and 74%, respectively. The minor haplotype possessed two putative Sp1 binding sites while the major haplotype did not have any Sp1 binding site. The minor haplotype had a higher transcription and Sp1 binding activities than the major haplotype, invitro. The original -816A/C was in high linkage disequilibrium with these haplotypes (D'=0.92, r2=0.85), and well agreed with the efficacy of imidapril medication. These results suggest that the Sp1 binding site variation in the CES1A2 promoter is functional, and are good candidates for the pharmacogenetic studies of CES1-activated drugs.
ESTHER : Yoshimura_2008_Biochem.Biophys.Res.Commun_369_939
PubMedSearch : Yoshimura_2008_Biochem.Biophys.Res.Commun_369_939
PubMedID: 18328811
Gene_locus related to this paper: human-CES1

Title : A single nucleotide polymorphism in the carboxylesterase gene is associated with the responsiveness to imidapril medication and the promoter activity - Geshi_2005_Hypertens.Res_28_719
Author(s) : Geshi E , Kimura T , Yoshimura M , Suzuki H , Koba S , Sakai T , Saito T , Koga A , Muramatsu M , Katagiri T
Ref : Hypertens Res , 28 :719 , 2005
Abstract : Imidapril is an angiotensin-converting enzyme inhibitor that is widely used in treating hypertension, although the responses vary among individuals. We investigated whether a single nucleotide polymorphism at position -816 of the carboxylesterase 1 (CES1) gene, which activates imidapril in the liver, is involved in the responsiveness to imidapril medication. A total of 105 Japanese hypertensives with systolic/diastolic blood pressures (SBP/DBP) of 140/90 mmHg or higher were prescribed 5-10 mg/day of imidapril. At baseline, blood pressure levels were not different between patients with and those without the -816C allele (AA vs. AC+ CC groups). After 8 weeks of treatment, we classified the responders and non-responders based on the decline in their blood pressures, and found that the responder rate was significantly higher in the AC+CC group than in the AA group (p=0.0331). Also, the reduction in SBP was significantly greater in the AC+CC group than in the AA group (24.7+/-11.8 vs. 17.6+/-16.8 mmHg, p=0.0184). Furthermore, an in vitro reporter assay revealed that the -816C construct had significantly higher promoter activity (p<0.0001). These findings suggest that the A(-816)C polymorphism affects the transcriptional activity, and that this may account for the responsiveness to imidapril.
ESTHER : Geshi_2005_Hypertens.Res_28_719
PubMedSearch : Geshi_2005_Hypertens.Res_28_719
PubMedID: 16419644
Gene_locus related to this paper: human-CES1

Title : Functional annotation of a full-length Arabidopsis cDNA collection - Seki_2002_Science_296_141
Author(s) : Seki M , Narusaka M , Kamiya A , Ishida J , Satou M , Sakurai T , Nakajima M , Enju A , Akiyama K , Oono Y , Muramatsu M , Hayashizaki Y , Kawai J , Carninci P , Itoh M , Ishii Y , Arakawa T , Shibata K , Shinagawa A , Shinozaki K
Ref : Science , 296 :141 , 2002
Abstract : Full-length complementary DNAs (cDNAs) are essential for the correct annotation of genomic sequences and for the functional analysis of genes and their products. We isolated 155,144 RIKEN Arabidopsis full-length (RAFL) cDNA clones. The 3'-end expressed sequence tags (ESTs) of 155,144 RAFL cDNAs were clustered into 14,668 nonredundant cDNA groups, about 60% of predicted genes. We also obtained 5' ESTs from 14,034 nonredundant cDNA groups and constructed a promoter database. The sequence database of the RAFL cDNAs is useful for promoter analysis and correct annotation of predicted transcription units and gene products. Furthermore, the full-length cDNAs are useful resources for analyses of the expression profiles, functions, and structures of plant proteins.
ESTHER : Seki_2002_Science_296_141
PubMedSearch : Seki_2002_Science_296_141
PubMedID: 11910074
Gene_locus related to this paper: arath-CXE15

Title : Normalization and subtraction of cap-trapper-selected cDNAs to prepare full-length cDNA libraries for rapid discovery of new genes - Carninci_2000_Genome.Res_10_1617
Author(s) : Carninci P , Shibata Y , Hayatsu N , Sugahara Y , Shibata K , Itoh M , Konno H , Okazaki Y , Muramatsu M , Hayashizaki Y
Ref : Genome Res , 10 :1617 , 2000
Abstract : In the effort to prepare the mouse full-length cDNA encyclopedia, we previously developed several techniques to prepare and select full-length cDNAs. To increase the number of different cDNAs, we introduce here a strategy to prepare normalized and subtracted cDNA libraries in a single step. The method is based on hybridization of the first-strand, full-length cDNA with several RNA drivers, including starting mRNA as the normalizing driver and run-off transcripts from minilibraries containing highly expressed genes, rearrayed clones, and previously sequenced cDNAs as subtracting drivers. Our method keeps the proportion of full-length cDNAs in the subtracted/normalized library high. Moreover, our method dramatically enhances the discovery of new genes as compared to results obtained by using standard, full-length cDNA libraries. This procedure can be extended to the preparation of full-length cDNA encyclopedias from other organisms.
ESTHER : Carninci_2000_Genome.Res_10_1617
PubMedSearch : Carninci_2000_Genome.Res_10_1617
PubMedID: 11042159
Gene_locus related to this paper: mouse-1plip , mouse-1plrp , mouse-abhd5 , mouse-Abhd8 , mouse-cauxin , mouse-Ces1g , mouse-CPMac , mouse-dpp8 , mouse-hslip , mouse-hyes , mouse-lipli , mouse-LIPN , mouse-pafa , mouse-Ppgb , mouse-q3uuq7 , mouse-Q9DAI6 , mouse-RISC

Title : Blockade of voltage-dependent 42K efflux from rat brain synaptosome by minaprine and tetrahydroaminoacridine - Chaki_1991_Life.Sci_48_2383
Author(s) : Chaki S , Muramatsu M , Otomo S
Ref : Life Sciences , 48 :2383 , 1991
Abstract : The effect of minaprine (3-(2-morpholinoethylamino)-4-methyl-6-phenylpyridazine) on the K+ channels was studied by means of 42K efflux from rat brain synaptosomes, comparing the effects of 4-aminopyridine and 9-amino-1,2,3,4-tetrahydroacridine (THA). 42K efflux from rat brain synaptosomes was classified into five components: a resting component (R), a rapidly inactivating, voltage-dependent component (T), a slowly inactivating, voltage-dependent component (S) and a voltage-dependent, Ca(2+)-dependent component which is divided into a fast phase (CT) and a slower phase (CS). 4-Aminopyridine selectively inhibited 42K efflux of component T. THA blocked both S and T components. The inhibitory effect of THA on the 42K efflux of component S was quite pronounced compared with that of component T. Minaprine inhibited the 42K efflux of components S and T but the inhibitory effect on component S was observed with a lower dose of minaprine than that needed for the effect on component T. Minaprine had no effect on the Ca(2+)-dependent component while THA blocked component CT. 42K efflux of the resting component was not changed by minaprine, THA or 4-aminopyridine. These results suggest that minaprine blocks Ca2+ independent voltage-dependent K+ channel is involved in the pharmacological actions of minaprine.
ESTHER : Chaki_1991_Life.Sci_48_2383
PubMedSearch : Chaki_1991_Life.Sci_48_2383
PubMedID: 2046464

Title : Attenuation of serotonin-suppressed [3H]acetylcholine release by tetrahydroaminoacridine and dendrotoxin: interaction with minaprine binding site - Muramatsu_1990_Res.Commun.Chem.Pathol.Pharmacol_68_131
Author(s) : Muramatsu M , Chaki S , Usuki-ito C , Otomo S
Ref : Res Commun Chem Pathol Pharmacol , 68 :131 , 1990
Abstract : 5-Hydroxytryptamine (5-HT) inhibited K(+)-induced [3H]acetylcholine ([3H]ACh) release from rat hippocampal slices dose-dependently. Minaprine [3-(2-morpholino-ethylamino)-4-methyl-6-phenylpyridazine] and 9-amino-1,2,3,4-tetrahydroacridine (THA) attenuated the inhibition of [3H]ACh release by 5-HT. A neurotoxin isolated from the venom of Dendroaspis snake, dendrotoxin (DTX), also attenuated the 5-HT inhibited [3H]ACh release from hippocampal slices dose-dependently at doses of more than 3 x 10(-7) g/ml (about 42 nM). Specific binding of [3H]minaprine to hippocampal membrane was dose-dependently inhibited by THA and DTX. The IC50 of THA and DTX for the [3H]minaprine binding were about 32 and 0.7 mu M, respectively. Scatchard plot analyses showed that the inhibitory effects of THA and DTX were noncompetitive for [3H]minaprine binding. THA and DTX inhibited [3H]ketanserin binding with IC50 of 28.8 and 26.2 mu M, respectively. These results suggest that THA and DTX attenuate the 5-HT-inhibited [3H]ACh release by blocking a voltage-dependent K+ current, and that they interact with the binding site of minaprine in the hippcampus.
ESTHER : Muramatsu_1990_Res.Commun.Chem.Pathol.Pharmacol_68_131
PubMedSearch : Muramatsu_1990_Res.Commun.Chem.Pathol.Pharmacol_68_131
PubMedID: 2353129