Hidaka K

References (16)

Title : Microbial decomposition of biodegradable plastics on the deep-sea floor - Omura_2024_Nat.Commun_15_568
Author(s) : Omura T , Isobe N , Miura T , Ishii S , Mori M , Ishitani Y , Kimura S , Hidaka K , Komiyama K , Suzuki M , Kasuya KI , Nomaki H , Nakajima R , Tsuchiya M , Kawagucci S , Mori H , Nakayama A , Kunioka M , Kamino K , Iwata T
Ref : Nat Commun , 15 :568 , 2024
Abstract : Microbes can decompose biodegradable plastics on land, rivers and seashore. However, it is unclear whether deep-sea microbes can degrade biodegradable plastics in the extreme environmental conditions of the seafloor. Here, we report microbial decomposition of representative biodegradable plastics (polyhydroxyalkanoates, biodegradable polyesters, and polysaccharide esters) at diverse deep-sea floor locations ranging in depth from 757 to 5552 m. The degradation of samples was evaluated in terms of weight loss, reduction in material thickness, and surface morphological changes. Poly(L-lactic acid) did not degrade at either shore or deep-sea sites, while other biodegradable polyesters, polyhydroxyalkanoates, and polysaccharide esters were degraded. The rate of degradation slowed with water depth. We analysed the plastic-associated microbial communities by 16S rRNA gene amplicon sequencing and metagenomics. Several dominant microorganisms carried genes potentially encoding plastic-degrading enzymes such as polyhydroxyalkanoate depolymerases and cutinases/polyesterases. Analysis of available metagenomic datasets indicated that these microorganisms are present in other deep-sea locations. Our results confirm that biodegradable plastics can be degraded by the action of microorganisms on the deep-sea floor, although with much less efficiency than in coastal settings.
ESTHER : Omura_2024_Nat.Commun_15_568
PubMedSearch : Omura_2024_Nat.Commun_15_568
PubMedID: 38278791

Title : Identification of Missense Mutation (G365R) of the Butyrylcholinesterase (BCHE) Gene in a Japanese Patient with Familial Cholinesterasemia - Sakamoto_2001_Kobe.J.Med.Sci_47_153
Author(s) : Sakamoto N , Maeda T , Hidaka K , Teranishi T , Toyoda M , Onishi Y , Kuroda S , Sakaguchi K , Fujisawa T , Maeda M , Watanabe Y , Iuchi I
Ref : Kobe J Med Sci , 47 :153 , 2001
Abstract : A point mutation which caused a silent phenotype of human serum butyrylcholinesterase (BChE) was identified in the genomic DNA of a 57-year-old Japanese woman who visited our hospital because of pneumonia. The propositus exhibited an unusually low level of BChE activity, whereas her son and daughter had an intermediate level. Immunologically, there was an absence of BChE protein in the propositus's serum. DNA sequence analysis of the propositus demonstrated a point mutation at codon 365 (GGA-CGA), resulting in a Gly-Arg substitution. A family study showed her son and daughter to have the same mutation.
ESTHER : Sakamoto_2001_Kobe.J.Med.Sci_47_153
PubMedSearch : Sakamoto_2001_Kobe.J.Med.Sci_47_153
PubMedID: 11733654

Title : Gene analysis of genomic DNA from stored serum by polymerase chain reaction: identification of three missense mutations in patients with cholinesterasemia and ABO genotyping - Hidaka_2001_Clin.Chim.Acta_303_61
Author(s) : Hidaka K , Watanabe Y , Tomita M , Ueda N , Higashi M , Minatogawa Y , Iuchi I
Ref : Clinica Chimica Acta , 303 :61 , 2001
Abstract : We established a method to determine the butyrylcholinesterase genotype associated with a BCHE deficiency directly using multiple PCR from stored serum, which was stored at -70 degrees C for more than 30 years. PCR products from sera of six propositi were used for DNA sequence analysis. All of these BChE variants were characterized by a single nucleotide substitution. Four of them were homozygotes and demonstrated a C-->T single nucleotide point mutation at codon 100 from CCA (Pro) to TCA (Ser). The fifth case was a heterozygote of this mutation. The remaining one was a compound heterozygote showing a T-->C transition mutation at codon 203 from TCA (Ser) to CCA (Pro) and a G-->C transversion mutation at codon 365 from GGA (Gly) to CGA (Arg). Furthermore we developed a method to determine the ABO genotype from the same serum. These results indicated that serum is useful as a starting material for amplification of genomic DNA when fresh blood samples are not available.
ESTHER : Hidaka_2001_Clin.Chim.Acta_303_61
PubMedSearch : Hidaka_2001_Clin.Chim.Acta_303_61
PubMedID: 11163024

Title : [Missense mutations of the butyrylcholinesterase gene in six Japanese patients with low cholinesterasemia: genetic analysis using sera stored in a freezer] - Hidaka_1999_Rinsho.Byori_47_980
Author(s) : Hidaka K , Watanabe Y , Ueda N , Tomita M , Higashi M , Abe K , Minatogawa Y , Iuchi I
Ref : Rinsho Byori , 47 :980 , 1999
Abstract : Six serum samples with no detectable butyrylcholinesterase (BCHE) activity had been stored at -70 degrees C for more than 10 years. These sera were used for amplification of BCHE gene using polymerase chain reaction (PCR) and for nucleotide sequence analysis. Five of them demonstrated a C-->T transition at codon 100 (CCA-->TCA), resulting in a Pro-->Ser substitution. The other one was a compound heterozygote as revealed a T-->C transition mutation at codon 203 from TCA (Ser) to CCA (Pro) and G-->C transversion at codon 365 from GGA (Gly) to CGA (Arg). These results showed sera stored in a freezer could be used as a starting material for amplification of genomic DNA when it is not possible to obtain fresh blood samples.
ESTHER : Hidaka_1999_Rinsho.Byori_47_980
PubMedSearch : Hidaka_1999_Rinsho.Byori_47_980
PubMedID: 10590675

Title : Identification of a point mutation associated with a silent phenotype of human serum butyrylcholinesterase--a case of familial cholinesterasemia - Sakamoto_1998_Clin.Chim.Acta_274_159
Author(s) : Sakamoto N , Hidaka K , Fujisawa T , Maeda M , Iuchi I
Ref : Clinica Chimica Acta , 274 :159 , 1998
Abstract : A point mutation which caused a silent phenotype of human serum butyrylcholinesterase (BChE) was identified in the DNA of a 47-year-old Japanese woman who visited our hospital complaining of hypertension. The propositus exhibited an unusually low level of BChE activity, whereas her younger sister and her daughter had intermediate levels of BChE activity and her elder sister a normal level. Immunologically, the amount of BChE protein in the serum of the propositus was normal. DNA sequence analysis of the propositus identified a point mutation at codon 199 (GCA --> GTA), resulting in a Ala --> Val substitution. This alteration is one downstream codon from the catalytic active site (Ser, 198). A family study showed her younger sister and her daughter to have the same mutation.
ESTHER : Sakamoto_1998_Clin.Chim.Acta_274_159
PubMedSearch : Sakamoto_1998_Clin.Chim.Acta_274_159
PubMedID: 9694584

Title : Genetic analysis of a Japanese patient with butyrylcholinesterase deficiency - Hidaka_1997_Ann.Hum.Genet_61_491
Author(s) : Hidaka K , Iuchi I , Tomita M , Watanabe Y , Minatogawa Y , Iwasaki K , Gotoh K , Shimizu C
Ref : Ann Hum Genet , 61 :491 , 1997
Abstract : A patient (64-year-old, male) with familial cholinesterasemia caused by BChE deficiency was studied. DNA sequence analysis of all exons identified a point mutation, an A-->G transition at codon 128, resulting in a Tyr-->Cys substitution. The propositus showed extremely low BChE activity, but his other family members (three individuals) showed from intermediate to normal BChE activity. An immunological method revealed the absence of BChE protein in serum of the propositus. Both PCR primer introduced restriction analysis (PCR-PIRA) and sequence analysis revealed all three family members to be heterozygotes for this mutation.
ESTHER : Hidaka_1997_Ann.Hum.Genet_61_491
PubMedSearch : Hidaka_1997_Ann.Hum.Genet_61_491
PubMedID: 9543549

Title : Nonsense mutation in exon 2 of the butyrylcholinesterase gene: a case of familial cholinesterasemia - Hidaka_1997_Clin.Chim.Acta_261_27
Author(s) : Hidaka K , Iuchi I , Yamasaki T , Ueda N , Hukano K
Ref : Clinica Chimica Acta , 261 :27 , 1997
Abstract : A point mutation that causes a silent phenotype for human serum butyrylcholinesterase (BChE) was proved by DNA analyses of a 64-year-old Japanese female who visited the hospital because of a common cold. The propositus and her two siblings showed extremely low BChE activity, but other family members (six individuals) manifested from intermediate to normal values of BChE activity. An immunological method revealed that the propositus and her two siblings showed absence of the BChE protein in serum. DNA sequence analysis of the propositus identified a point mutation at codon 400 (TGC-->TGA), resulting in the production of a stop codon. This alteration exists upstream of the Cys571 of the subunit, which forms a disulfide bridge with the Cys571 of another partner subunit.
ESTHER : Hidaka_1997_Clin.Chim.Acta_261_27
PubMedSearch : Hidaka_1997_Clin.Chim.Acta_261_27
PubMedID: 9187502

Title : [Determination of gene mutation of silent serum cholinesterase and its epidemiologic characters in the Japanese]. [Japanese] - Hidaka_1995_Rinsho.Byori.Japanese.J.ClinPathol_43_786
Author(s) : Hidaka K , Iuchi I
Ref : Rinsho Byori Japanese Journal of Clinical Pathology , 43 :786 , 1995
Abstract : We detected 121 individuals with silent type of serum cholinesterase from 36 families in Japan. DNA analysis totaling 37 members of eleven blood unrelated families were carried out by four useful methods, namely, 1) PCR-SSCP analysis, 2) dot blot hybridization (DBH) with the use of synthetic oligonucleotide probe, 3) restriction endonuclease analysis (REA) and 4) direct sequencing analysis. Their mutations were classified into four groups, namely, 1) a G-->C transversion at codon 365, 2) a frameshift mutation with insertion of an extra A at codon 315, 3) an A-->G transition at codon 128 and 4) a C-->A transition at codon 400. The three procedures including (PCR-SSCP, DBH, REA) without the use of radio labeled materials (non-RI) are recommendable for the analyses. However, the direct sequencing analysis of bases with RI might be, at present, necessary for the final identification.
ESTHER : Hidaka_1995_Rinsho.Byori.Japanese.J.ClinPathol_43_786
PubMedSearch : Hidaka_1995_Rinsho.Byori.Japanese.J.ClinPathol_43_786
PubMedID: 7474437

Title : Synthesis and structure-activity studies of a series of 1-oxa-8-azaspiro[4.5]decanes as M1 muscarinic agonists - Tsukamoto_1995_Chem.Pharm.Bull.(Tokyo)_43_842
Author(s) : Tsukamoto S , Fujii M , Yasunaga T , Matsuda K , Wanibuchi F , Hidaka K , Furuya T , Tamura T
Ref : Chem Pharm Bull (Tokyo) , 43 :842 , 1995
Abstract : 2,8-Dimethyl-1-oxa-8-azaspiro[4,5]decan-3-one (17), designed by incorporating the tetrahydrofuran ring moiety of muscarone into an 8-azaspiro[4,5]decane skeleton, and related 1-oxa-8-azaspiro[4.5]decanes were synthesized and assessed as M1 muscarinic agonists for the symptomatic treatment of dementia of Alzheimer's type. The compounds were tested for central muscarinic M1 and M2 receptor affinity and in vivo muscarinic activities: namely, amelioration of scopolamine-induced impairment in rat passive avoidance tasks, and induction of hypothermia, tremor, and salivary secretion. Compound 17 exhibited potent muscarinic activities in vitro and in vivo with no selectivity. Systematic modifications of 17 were conducted, and a number of compounds, including the 2-ethyl analogue (18), 3-methylene analogue (29), 3-dithioketal analogues (26, 28), and 3-oxime analogue (37) were found to display preferential affinity for M1 receptors over M2 receptors and, in addition, to exhibit potent antiamnesic activity sufficiently separated from hypothermia-inducing activity, taken as an index of cholinergic side effects, compared with the reference compound RS86 (1). Structure-activity relationships are discussed in comparison with those for muscarone analogues. Of these compounds only two, 2-ethyl-8-methyl-1-oxa-8-azaspiro[4.5]decan-3-one (18) and 2,8-dimethyl-3-methylene-1-oxa-8-azaspiro[4.5]decane (29), stimulated phosphoinositide hydrolysis in rat hippocampal slices, indicating partial agonistic activity for M1 muscarinic receptors. The optical resolution of 18 and 29 was performed. Eudismic ratios of both compounds in binding affinity were low, but M1 agonist activity resided preferentially in the (-)-isomers. The absolute configuration of (-)-29 was determined by X-ray crystal structure analysis to be S, being the same as that of muscarone. Based on the in vivo selectivity, (-)-29 was selected for clinical studies.
ESTHER : Tsukamoto_1995_Chem.Pharm.Bull.(Tokyo)_43_842
PubMedSearch : Tsukamoto_1995_Chem.Pharm.Bull.(Tokyo)_43_842
PubMedID: 7553970

Title : Synthesis and structure-activity studies of a series of 1-oxa-2,8-diazaspiro[4.5]decan-3-ones and related compounds as M1 muscarinic agonists - Tsukamoto_1995_Chem.Pharm.Bull.(Tokyo)_43_1523
Author(s) : Tsukamoto S , Nagaoka H , Igarashi S , Wanibuchi F , Hidaka K , Tamura T
Ref : Chem Pharm Bull (Tokyo) , 43 :1523 , 1995
Abstract : A series of novel 2,8-dialkyl-1-oxa-2,8-diazaspiro[4.5]decan-3-ones and 2,8-dimethyl-1,2,8-triazaspiro[4.5]-decan-3-one (13), related to M1 muscarinic agonists YM796 and RS86, were synthesized by using Michael addition reaction of hydroxyurea or methylhydrazine to alpha, beta-unsaturated esters followed by cyclization reaction. These compounds were assessed for binding affinities for M1 and M2 receptors and in vivo muscarinic activity: namely, amelioration of scopolamine-induced impairment in rat passive avoidance tasks and induction of hypothermia, tremor, and salivation. 2,8-Dimethyl-1-oxa-2,8-diazaspiro[4.5]decan-3-one (6a) exhibited high affinities for both M1 and M2 receptors, showed antiamnesic activity (0.1 mg/kg, s.c.) and induced hypothermia (3 mg/kg, s.c.). In addition, 6a stimulated phosphoinositide hydrolysis in rat hippocampal slices, indicating partial agonistic activity for M1 muscarinic receptors. The alteration of the methyl group at N2 of 6a increased the selectivity in binding affinities for M1 over M2 receptors, but resulted in loss of M1 agonistic activity or antiamnesic activity. Compound 13 exhibited only low affinity for M1 receptors, suggesting that a basic nitrogen atom is not tolerated in M1 receptor binding as a substitute for an oxygen atom or a carbonyl group at the 1-position of 6a or RS86. None of these derivatives exhibited high selectivity for antiamnesic effect over induction of hypothermia compared to YM796.
ESTHER : Tsukamoto_1995_Chem.Pharm.Bull.(Tokyo)_43_1523
PubMedSearch : Tsukamoto_1995_Chem.Pharm.Bull.(Tokyo)_43_1523
PubMedID: 7586076

Title : Characterization of a novel muscarinic receptor agonist, YM796: comparison with cholinesterase inhibitors in in vivo pharmacological studies - Wanibuchi_1994_Eur.J.Pharmacol_265_151
Author(s) : Wanibuchi F , Nishida T , Yamashita H , Hidaka K , Koshiya K , Tsukamoto S , Usuda S
Ref : European Journal of Pharmacology , 265 :151 , 1994
Abstract : Previous reports have shown that (+/-)-YM796 (2,8-dimethyl-3-methylene-1-oxa-8-azaspiro[4.5]decane) exhibits M1 agonistic activity and ameliorates cognitive impairment, and that the (-)-S isomer is active in in vitro studies. We report here the characterization of the (-)-S isomer, YM796 ((-)-(S)-2,8-dimethyl-3-methylene-1-oxa-8-azaspiro[4.5]decane L-tartrate monohydrate), and its (+)-R isomer in in vivo pharmacological studies in comparison with the cholinesterase inhibitors tacrine, amiridine and E-2020. YM796 (0.031-0.5 mg/kg p.o.), like the racemate, reversed the cognitive impairment in passive avoidance tasks of rats with nucleus basalis magnocellularis lesions, whereas (+)-R-YM796 was ineffective in this experimental amnesia. YM796 exhibited only weak effects on mouse salivation and hypothermia, a peripheral cholinergic response and a central cholinergic response, respectively. The (+)-R isomer, however, failed to induce these cholinergic responses. YM796 also ameliorated the memory deficits induced by scopolamine in rats and electroconvulsive shock in mice. The potency of YM796 in these experimental amnesia models was over a 100 times greater than that of tacrine, over 10 times greater than that of E-2020, and 6 times greater than that of amiridine. In salivary secretion and hypothermia, YM796 was 2-4 times weaker than tacrine and E-2020, and 1-2 times stronger than amiridine. Thus, YM796's ratio of anti-amnesic effects to salivary secretion and hypothermia was much greater than that of the cholinesterase inhibitors tested.(ABSTRACT TRUNCATED AT 250 WORDS)
ESTHER : Wanibuchi_1994_Eur.J.Pharmacol_265_151
PubMedSearch : Wanibuchi_1994_Eur.J.Pharmacol_265_151
PubMedID: 7875230

Title : Poster: Anti-amnesic effects of a novel muscarinic agonist, YM796 -
Author(s) : Wanibuchi F , Nishida T , Yamashita H , Hidaka K , Tsukamoto S , Koshiya K , Usuda S
Ref : Life Sciences , 52(5-6) :589 , 1993
PubMedID:

Title : Synthesis and structure-activity studies of a series of spirooxazolidine-2,4-diones: 4-oxa analogues of the muscarinic agonist 2-ethyl-8-methyl-2,8-diazaspiro[4.5]decane-1,3-dione - Tsukamoto_1993_J.Med.Chem_36_2292
Author(s) : Tsukamoto S , Ichihara M , Wanibuchi F , Usuda S , Hidaka K , Harada M , Tamura T
Ref : Journal of Medicinal Chemistry , 36 :2292 , 1993
Abstract : A series of spirooxazolidine-2,4-dione derivatives related to the putative M1 agonist 2-ethyl-8-methyl-2,8-diazaspiro[4.5]decane-1,3-dione (RS86; 1) were synthesized. The compounds were evaluated as cholinergic agents in in vitro binding assays and in in vivo pharmacological tests including antiamnesic effects using scopolamine-treated mice, hypothermia, and salivation in mice. Four compounds (5a,c,f and 17a) exhibited affinity for cortical M1 receptors and reversed scopolamine-induced impairment of mouse passive avoidance tasks, as did 1. Among these compounds, only 5a exhibited M1-receptor stimulating activity in pithed rats. Structural requirements for muscarinic activity in this series of spirooxazolidine-2,4-dione derivatives were as strict as those reported for spirosuccinimide derivatives including 1. The antiamnesic dose of 3-ethyl-8-methyl-1-oxa-3,8-diazaspiro[4.5]decane-2,4-dione (5a) was 2 orders of magnitude lower than the doses inducing hypothermia and salivation, in contrast to 1 for which the former dose was only 5-10-fold lower than the latter. These results suggest that the 8-azaspiro[4.5]decane skeleton represents a useful template for designing new muscarinic agonists as antidementia drugs.
ESTHER : Tsukamoto_1993_J.Med.Chem_36_2292
PubMedSearch : Tsukamoto_1993_J.Med.Chem_36_2292
PubMedID: 8360873

Title : [Identification of two different genetic mutation associated with silent phenotypes for human serum cholinesterase in Japanese] - Hidaka_1992_Rinsho.Byori_40_535
Author(s) : Hidaka K , Iuchi I , Yamasaki T , Ohhara M , Shoda T , Primo-Parmo SL , La Du BN
Ref : Rinsho Byori , 40 :535 , 1992
Abstract : Two different gene mutations associated with the silent phenotype for human serum cholinesterase were demonstrated. DNA from five individuals with silent gene phenotype of three unrelated Japanese families was amplified by the polymerase chain reaction (PCR) and analyzed by direct sequencing. The first instance demonstrated a G----C transversion at codon 365 from GGA (Gly) to CGA (Arg), which was seen in three individuals of the two families. This mutation was resulted to create a new Taq 1 restriction site (TCGA). The second mutation was shown by a double heterozygous condition with two different silent gene mutations in two members of remaining one family. These mutations were as follows: 1) one type was a frameshift mutation, in which an extra A was inserted in codon 315 (ACC----AACC) to create a new stop codon at position 322 and 2) the other was the same point mutation at codon 365 as seen in the first instance. These results indicated that many silent variants can be distinguished by direct sequence analyses of genomic DNA.
ESTHER : Hidaka_1992_Rinsho.Byori_40_535
PubMedSearch : Hidaka_1992_Rinsho.Byori_40_535
PubMedID: 1507480

Title : Pharmacological characterization of a novel muscarinic partial agonist, YM796, in transfected cells expressing the m1 or m2 muscarinic receptor gene - Wei_1992_Life.Sci_50_355
Author(s) : Wei HB , Roeske WR , Lai J , Wanibuchi F , Hidaka K , Usuda S , Yamamura HI
Ref : Life Sciences , 50 :355 , 1992
Abstract : To investigate the pharmacological effect of a novel compound YM796, we performed radioligand binding experiments and correlative biochemical experiments using the transfected murine fibroblast B82 cells which expressed the m1 and m2 muscarinic receptor genes (cloned cell lines designated as LK3-3 and M2LKB2-2, respectively). [3H](-)methyl-3-quinuclidinyl benzilate [( 3H](-)MQNB) binding in these transfected cell lines was inhibited by different optical isomers of YM796 and other muscarinic drugs, atropine, pirenzepine, AF-DX 116, as well as selected agonists. (-)YM796, (+)YM796 and (+/-)YM796 inhibited [3H](-)MQNB binding in LK3-3 cells with Ki values of 16.4 microM, 30.1 microM and 21.8 microM and in M2LKB2-2 cells with Ki values of 52.0 microM, 108 microM and 77.1 microM, respectively. From functional assays we found the two isomers, (-)YM796 and (+)YM796 had different intrinsic activities for the M1 and M2 muscarinic receptors. (-)YM796 revealed agonistic activity: stimulation of [3H]IP1 accumulation in LK3-3 cells with an EC50 value of 26.5 microM, which was less efficacious (the Emax value was 5.6 times basal) than carbachol, a full agonist (the Emax value was 17.2 times basal). Interestingly, (-)YM796 did not show significant inhibition of cAMP formation in M2LKB2-2 cells except at extremely high concentrations (greater than 1mM). (+)YM796 exhibited no significant efficacy for the M1 and M2 muscarinic receptors. These results suggest that (-)YM796 represents a muscarinic partial agonist with functional selectivity for the M1 muscarinic receptors whereas (+)YM796 shows no efficacy for either M1 or M2 muscarinic receptors in these transfected cells.
ESTHER : Wei_1992_Life.Sci_50_355
PubMedSearch : Wei_1992_Life.Sci_50_355
PubMedID: 1310135

Title : Pharmacological studies on novel muscarinic agonists, 1-oxa-8-azaspiro[4.5]decane derivatives, YM796 and YM954 - Wanibuchi_1990_Eur.J.Pharmacol_187_479
Author(s) : Wanibuchi F , Konishi T , Harada M , Terai M , Hidaka K , Tamura T , Tsukamoto S , Usuda S
Ref : European Journal of Pharmacology , 187 :479 , 1990
Abstract : We have investigated the pharmacological profiles of the novel muscarinic agonists, 1-oxa-8-azaspiro[4.5]decane derivatives, YM796 (2,8-dimethyl-3-methylene) and YM954 (2-ethyl-8-methyl-3-oxo). These compounds, like the putative M1 agonists, RS86 and AF102B, inhibited [3H]pirenzepine binding to cerebral cortical membranes in the micromolar range and weakly inhibited [3H]quinuclidinyl benzylate binding to cerebellar membranes. Their (-) isomers had Hill coefficients lower than 1.0. (+/-)-YM796, (+/-)-YM954 and RS86, but not AF102B, stimulated phosphoinositide hydrolysis in hippocampal slices, an effect which is mainly linked to M1 receptors. (+/-)-YM796 (0.031 mg/kg p.o.) and (+/-)-YM954 (0.016 mg/kg p.o.) reversed the cognitive impairment in nucleus basalis magnocellularis-lesioned rats in a passive avoidance task more effectively than did RS86 and AF102B. Similar results were obtained in scopolamine-treated rats. Finally, (+/-)-YM796 was weaker than (+/-)-YM954 and RS86 in the induction of tremor, hypothermia and contraction of isolated ileum, which are mainly mediated by M2 and/or M3 receptors. These results suggest that (+/-)-YM796, (+/-)-YM954 and RS86 have M1 agonistic activity in central nervous system and that (+/-)-YM796 has relatively weak M2 and/or M3 agonistic activity.
ESTHER : Wanibuchi_1990_Eur.J.Pharmacol_187_479
PubMedSearch : Wanibuchi_1990_Eur.J.Pharmacol_187_479
PubMedID: 1963596