Mori M

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 : Fluorescein diacetate (FDA) and its analogue as substrates for Pi-class glutathione S-transferase (GSTP1) and their biological application - Fujikawa_2018_Talanta_179_845
Author(s) : Fujikawa Y , Nampo T , Mori M , Kikkawa M , Inoue H
Ref : Talanta , 179 :845 , 2018
Abstract : Pi class glutathione S-transferase (GSTP1) is highly expressed in various cancerous cells and pre-neoplastic legions, where it is involved in apoptotic resistance or metabolism of several anti-tumour chemotherapeutics. Therefore, GSTP1 is a marker of malignant and pre-malignant cells and is a promising target for visualization and drug development. Here we demonstrate that fluorescein diacetate (FDA), a fluorescent probe used for vital staining, is a fluorescently activated by esterolytic activity of human GSTP1 (hGSTP1) selectively among various cytosolic GSTs. Fluorescence activation of FDA susceptible to GST inhibitors was observed in MCF7 cells exogenously overexpressing hGSTP1, but not in cells overexpressing hGSTA1 or hGSTM1. Inhibitor-sensitive fluorescence activation was also observed in several cancer cell lines endogenously expressing GSTP1, suggesting that GSTP1 is involved in FDA esterolysis in these cells. Among the FDA derivatives examined, FOMe-Ac, the acetyl ester of fluorescein O-methyl ether, was found to be a potential reporter for GSH-dependent GSTP1 activity as well as for carboxylesterase activity. Since GSTP1 is highly expressed in various types of cancer cells compared to their normal counterparts, improving the fluorogenic substrates to be more selective to the esterolysis activity of GSTP1 rather than carboxylesterases should lead to development of tools for detecting GSTP1-overexpressing cancer cells and investigating the biological functions of GSTP1.
ESTHER : Fujikawa_2018_Talanta_179_845
PubMedSearch : Fujikawa_2018_Talanta_179_845
PubMedID: 29310316

Title : Cholinesterase inhibitor rivastigmine enhances nerve growth factor-induced neurite outgrowth in PC12 cells via sigma-1 and sigma-2 receptors - Terada_2018_PLoS.One_13_e0209250
Author(s) : Terada K , Migita K , Matsushima Y , Sugimoto Y , Kamei C , Matsumoto T , Mori M , Matsunaga K , Takata J , Karube Y
Ref : PLoS ONE , 13 :e0209250 , 2018
Abstract : Rivastigmine (Riv) is a potent and selective cholinesterase (acetylcholinesterase, AChE and butyrylcholinesterase, BuChE) inhibitor developed for the treatment of Alzheimer's disease (AD). To elucidate whether Riv causes neuronal differentiation, we examined its effect on nerve growth factor (NGF)-induced neurite outgrowth in PC12 cells. At concentrations of 0-100 muM, Riv was non-toxic in PC12 cells. Riv caused dose-dependent (10-100 muM) enhancement of NGF-induced neurite outgrowth, which was completely inhibited by the TrkA antagonist GW-441756. By contrast, Riv-mediated enhancement of neurite outgrowth was not blocked by the acetylcholine receptor antagonists, scopolamine and hexamethonium. However, the sigma-1 receptor (Sig-1R) antagonist NE-100 and sigma-2 receptor (Sig-2R) antagonist SM-21 each blocked about half of the Riv-mediated enhancement of NGF-induced neurite outgrowth. Interestingly, the simultaneous application of NE-100 and SM-21 completely blocked the enhancement of NGF-induced neurite outgrowth by Riv. These findings suggest that both Sig-1R and Sig-2R play important roles in NGF-induced neurite outgrowth through TrkA and that Riv may contribute to neuronal repair via Sig-1R and Sig-2R in AD therapy.
ESTHER : Terada_2018_PLoS.One_13_e0209250
PubMedSearch : Terada_2018_PLoS.One_13_e0209250
PubMedID: 30557385

Title : A case of advanced systemic sclerosis with severe GERD successfully treated with acotiamide - Kato_2016_Surg.Case.Rep_2_36
Author(s) : Kato R , Nakajima K , Takahashi T , Miyazaki Y , Makino T , Kurokawa Y , Yamasaki M , Takiguchi S , Mori M , Doki Y
Ref : Surg Case Rep , 2 :36 , 2016
Abstract : The majority of systemic sclerosis (SSc) patients have gastrointestinal tract involvement, but therapies of prokinetic agents are usually unsatisfactory. Patients are often compromised by the use of steroid; therefore, a surgical indication including fundoplication has been controversial. There is no report that advanced SSc with severe gastroesophageal reflux disease (GERD) is successfully treated with acotiamide, which is the acetylcholinesterase (AChE) inhibitor designed for functional dyspepsia (FD). We report a 44-year-old woman of SSc with severe GERD successfully treated with acotiamide. She had received medical treatment in our hospital since 2003. She had been aware of the significant gastroesophageal reflux symptoms (e.g., heartburn, chest pain, and dysphagia) due to the development of esophageal hardening associated with SSc since 2014. As a result of upper gastrointestinal series, upper gastrointestinal endoscopy, and 24-h pH monitoring and frequency scale for the symptoms of the GERD (FSSG) scoring, she has been diagnosed with GERD associated with SSc. First of all, she started to take prokinetic agents Rikkunshito and mosapride and proton pump inhibitor; there was no change in reflux symptoms. So, we started to prescribe her the acotiamide.After oral administration started, reflux symptoms have been improved. Five months after oral administration, FSSG score, a questionnaire for evaluation of the symptoms of GERD, was improved. Since its introduction of acotiamide, the patient has kept free from symptoms for 6 months.
ESTHER : Kato_2016_Surg.Case.Rep_2_36
PubMedSearch : Kato_2016_Surg.Case.Rep_2_36
PubMedID: 27072944

Title : Perturbation of acyl ghrelin profile after liver transplantation - Murakami_2015_J.Surg.Res_199_450
Author(s) : Murakami K , Takiguchi S , Miyazaki Y , Kurokawa Y , Yamasaki M , Nagano H , Mori M , Doki Y
Ref : J Surg Res , 199 :450 , 2015
Abstract : BACKGROUND: A significant problem to be solved for patients after liver transplantation (LT) is malnutrition with anorexia in the early posttransplant period. We hypothesized that this problem was due to the change in ghrelin metabolism during LT. The aim of this study was to examine the balance of acyl ghrelin (AG) and desacyl ghrelin and the dependence of the regulation mechanism on hepatic-related enzymes in patients during LT. MATERIALS AND
METHODS: AG, desacyl ghrelin, and acyl/total ghrelin (A/T) concentrations in blood samples were measured in 15 patients with liver failure (LF), 15 patients after LT, and 10 controls. The correlations between the participants' ghrelin profiles and hepatic function-related data, including liver enzymes, were evaluated. In vitro assays using synthetic AG for assessment of deacylation activity in serum were performed.
RESULTS: AG and A/T ratio were significantly higher in the LF patients than the patients after LT and controls (AG: 25.9 +/- 12.6 versus 16.4 +/- 12.6 and 9.8 +/- 7.6 fmol/mL, P < 0.05; A/T ratio: 17.4 +/- 4.1 versus 12.2 +/- 5.5 and 11.8% +/- 5.9%, P < 0.05). The serum cholinesterase level was inversely correlated with AG and A/T ratio (P < 0.01). In vitro assays showed that deacylation activity was significantly lower in patients with LF than controls (10.5% versus 42.4%, 90 min; P < 0.01). Degradation of AG was partially suppressed by a cholinesterase inhibitor.
CONCLUSIONS: Deacylation activity was lower in LF patients, which could cause elevation of AG levels. Serum cholinesterase may be responsible for deacylation in humans.
ESTHER : Murakami_2015_J.Surg.Res_199_450
PubMedSearch : Murakami_2015_J.Surg.Res_199_450
PubMedID: 26205310

Title : The association of GPR85 with PSD-95-neuroligin complex and autism spectrum disorder: a molecular analysis - Fujita-Jimbo_2015_Mol.Autism_6_17
Author(s) : Fujita-Jimbo E , Tanabe Y , Yu Z , Kojima K , Mori M , Li H , Iwamoto S , Yamagata T , Momoi MY , Momoi T
Ref : Mol Autism , 6 :17 , 2015
Abstract : BACKGROUND: Autism spectrum disorder (ASD) has a complex genetic etiology. Some symptoms and mutated genes, including neuroligin (NLGN), neurexin (NRXN), and SH3 and multiple ankyrin repeat domains protein (SHANK), are shared by schizophrenia and ASD. Little is known about the molecular pathogenesis of ASD. One of the possible molecular pathogenesis is an imbalance of excitatory and inhibitory receptors linked with the NLGN-PSD-95-SHANK complex via postsynaptic density protein/Drosophila disc large tumor suppressor/zonula occludens-1 protein (PDZ) binding. In the present study, we focused on GPR85 as a candidate gene for ASD because the C-terminal amino acid sequence of GPR85 [Thr-Cys-Val-Ile (YCVI)] is classified as a type II PDZ-binding motif, and GPR85 is a risk factor for schizophrenia. GPR85 is an orphan receptor that regulates neural and synaptic plasticity and modulates diverse behaviors, including learning and memory. While searching for molecules that associate with GPR85, we found that GPR85 was associated with postsynaptic density protein (PSD)-95 linked with NLGN in the brain.
METHODS: We examined the proteins that associate with the C-terminal sequence of GPR85 by pull-down assay and immunoblot analysis and searched for a mutation of the GPR85 gene in patients with ASD. We used immunostaining to examine the intracellular localization of mutated GPR85 and its influence on the morphology of cells and neurons.
RESULTS: The C-terminal sequence of GPR85 interacted with PSD-95 at PDZ1, while NLGN interacted with PSD-95 at PDZ3. Two male patients with ASD from independent Japanese families possessed inherited missense mutations at conserved sites in GPR85: one had T1033C (M152T) and the other had G1239T (V221L). These mutations were located in a domain related to G protein interaction and signal transduction. In contrast to wild-type GPR85, mutated GPR85 was more preferentially accumulated, causing endoplasmic reticulum stress, and disturbed the dendrite formation of hippocampal neurons.
CONCLUSIONS: GPR85 associated with the PSD-95 linked with NLGN, which is related to ASD. GPR85 carrying the mutations detected in ASD patients disturbed dendrite formation that could be the candidate for molecular pathogenesis of ASD through the associated NLGN-PSD-95 receptor complex.
ESTHER : Fujita-Jimbo_2015_Mol.Autism_6_17
PubMedSearch : Fujita-Jimbo_2015_Mol.Autism_6_17
PubMedID: 25780553

Title : Characterization of a novel lipolytic enzyme from Aspergillus oryzae - Koseki_2013_Appl.Microbiol.Biotechnol_97_5351
Author(s) : Koseki T , Asai S , Saito N , Mori M , Sakaguchi Y , Ikeda K , Shiono Y
Ref : Applied Microbiology & Biotechnology , 97 :5351 , 2013
Abstract : In this study, we report the characterization of a protein from Aspergillus oryzae, exhibiting sequence identity with paraben esterase from the genus Aspergillus. The coding region of 1,586 bp, including a 77-bp intron, encoded a protein of 502 amino acids. The gene without the signal peptide of 19 amino acids was cloned into a vector, pPICZalphaC, and expressed successfully in Pichia pastoris as an active extracellular protein. The purified recombinant protein had pH and temperature optima of 7.0-8.0 and 30 degrees C, respectively, and was stable at the pH range of 7.0-10.0 and up to 40 degrees C. The optimal substrate for hydrolysis by the purified recombinant protein, among a panel of alpha-naphthyl esters (C2-C16), was alpha-naphthyl butyrate (C4), with activity of 0.16 units/mg protein. The considerable hydrolytic activity of the purified recombinant enzyme toward tributyrin was determined. However, no paraben esterase activity was detected toward the ethyl, propyl, and butyl esters of 4-hydroxybenzoic acid. In addition, no activity was detected toward the methyl esters of ferulic, p-coumaric, caffeic, and sinapic acids that would indicate feruloyl esterase activity.
ESTHER : Koseki_2013_Appl.Microbiol.Biotechnol_97_5351
PubMedSearch : Koseki_2013_Appl.Microbiol.Biotechnol_97_5351
PubMedID: 23001008
Gene_locus related to this paper: aspor-q2uf27

Title : Ectopic expression of an esterase, which is a candidate for the unidentified plant cutinase, causes cuticular defects in Arabidopsis thaliana - Takahashi_2010_Plant.Cell.Physiol_51_123
Author(s) : Takahashi K , Shimada T , Kondo M , Tamai A , Mori M , Nishimura M , Hara-Nishimura I
Ref : Plant Cell Physiol , 51 :123 , 2010
Abstract : Cutinase is an esterase that degrades the polyester cutin, a major component of the plant cuticle. Although cutinase activity has been detected in pollen, the genes encoding this enzyme have not been identified. Here, we report the identification and characterization of Arabidopsis CDEF1 (cuticle destructing factor 1), a novel candidate gene encoding cutinase. CDEF1 encodes a member of the GDSL lipase/esterase family of proteins, although fungal and bacterial cutinases belong to the alpha/beta hydrolase superfamily which is different from the GDSL lipase/esterase family. According to the AtGenExpress microarray data, CDEF1 is predominantly expressed in pollen. The ectopic expression of CDEF1 driven by the 35S promoter caused fusion of organs, including leaves, stems and flowers, and increased surface permeability. Ultrastructural analysis revealed that the cuticle of the transgenic plants was often disrupted and became discontinuous. Subcellular analysis with green fluorescent protein (GFP)-tagged CDEF1 showed that the protein is secreted to the extracellular space in leaves. The recombinant CDEF1 protein has esterase activity. These results are consistent with cutinase being secreted from cells and directly degrading the polyester in the cuticle. CDEF1 promoter activity was detected in mature pollen and pollen tubes, suggesting that CDEF1 is involved in the penetration of the stigma by pollen tubes. Additionally, we found CDEF1 expression at the zone of lateral root emergence, which suggests that CDEF1 degrades cell wall components to facilitate the emergence of the lateral roots. Our findings suggest that CDEF1 is a candidate gene for the unidentified plant cutinase.
ESTHER : Takahashi_2010_Plant.Cell.Physiol_51_123
PubMedSearch : Takahashi_2010_Plant.Cell.Physiol_51_123
PubMedID: 19996150

Title : Gene expression profiles of drug-metabolizing enzymes and transporters with an overexpression of hepatocyte growth factor - Kakizaki_2007_Liver.Int_27_109
Author(s) : Kakizaki S , Yamazaki Y , Kosone T , Horiguchi N , Sohara N , Sato K , Takagi H , Yoshinari K , Mori M
Ref : Liver Int , 27 :109 , 2007
Abstract : BACKGROUND: It is important to elucidate the precise mechanism of drug metabolism during hepatic regeneration. Although cytochromes P450 (CYPs) are well known to be down-regulated in growth-stimulated cells, the overall gene expression profile of drug metabolizing enzymes are still not fully understood during hepatic regeneration. In this study, we investigated the gene expression profiles of such enzymes with an overexpression of hepatocyte growth factor (HGF). METHODS: Gene expression profiles were obtained using the Affymetrix MOE430A GeneChip oligonucleotide microarray by comparing HGF transgenic mice and wild-type mice. RESULTS: HGF produced a general decrease in mice with the expression of CYP isoforms such as Cyp1a2, Cyp2b10, Cyp2c, Cyp2d9, Cyp3a11, Cyp4a10, and Cyp7a1. Some isoforms of alcohol dehydrogenase, aldehyde dehydrogenase, and carboxylesterase also decreased. In the phase II enzymes, some isoforms of glutathione S-transferase and UDP-glucuronosyl transferase showed a reduced expression, although the sulfotransferase did not. In phase III transporters, some organic anion transporter and organic cation transporters were down-regulated. Among the nuclear receptors that are known to regulate the drug-metabolizing enzymes, small heterodimer partner and constitutive androstane receptor were down-regulated with an HGF overexpression. The protein level and enzymatic activity of Cyp2c decreased with an HGF overexpression. We furthermore investigated the inducibility of Cyp2b10 with xenobiotic inducers. Although the basal expression of Cyp2b10 was repressed, the inducibility was not abolished with the HGF overexpression. CONCLUSIONS: HGF down-regulated not only CYPs but also some drug-metabolizing enzymes, transporters, and nuclear receptors. We thus have to take in our mind the low basal expression of drug metabolizing enzymes, when treating patients with a regenerative liver state.
ESTHER : Kakizaki_2007_Liver.Int_27_109
PubMedSearch : Kakizaki_2007_Liver.Int_27_109
PubMedID: 17241389

Title : Stargazin and other transmembrane AMPA receptor regulating proteins interact with synaptic scaffolding protein MAGI-2 in brain - Deng_2006_J.Neurosci_26_7875
Author(s) : Deng F , Price MG , Davis CF , Mori M , Burgess DL
Ref : Journal of Neuroscience , 26 :7875 , 2006
Abstract : The spatial coordination of neurotransmitter receptors with other postsynaptic signaling and structural molecules is regulated by a diverse array of cell-specific scaffolding proteins. The synaptic trafficking of AMPA receptors by the stargazin protein in some neurons, for example, depends on specific interactions between the C terminus of stargazin and the PDZ [postsynaptic density-95 (PSD-95)/Discs large/zona occludens-1] domains of membrane-associated guanylate kinase scaffolding proteins PSD-93 or PSD-95. Stargazin [Cacng2 (Ca2+ channel gamma2 subunit)] is one of four closely related proteins recently categorized as transmembrane AMPA receptor regulating proteins (TARPs) that appear to share similar functions but exhibit distinct expression patterns in the CNS. We used yeast two-hybrid screening to identify MAGI-2 (membrane associated guanylate kinase, WW and PDZ domain containing 2) as a novel candidate interactor with the cytoplasmic C termini of the TARPs. MAGI-2 [also known as S-SCAM (synaptic scaffolding molecule)] is a multi-PDZ domain scaffolding protein that interacts with several different ligands in brain, including PTEN (phosphatase and tensin homolog), dasm1 (dendrite arborization and synapse maturation 1), dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, and NMDA receptors. We confirmed that MAGI-2 coimmunoprecipitated with stargazin in vivo from mouse cerebral cortex and used in vitro assays to localize the interaction to the C-terminal -TTPV amino acid motif of stargazin and the PDZ1, PDZ3, and PDZ5 domains of MAGI-2. Expression of stargazin recruited MAGI-2 to cell membranes and cell-cell contact sites in transfected HEK-293T cells dependent on the presence of the stargazin -TTPV motif. These experiments identify MAGI-2 as a strong candidate for linking TARP/AMPA receptor complexes to a wide range of other postsynaptic molecules and pathways and advance our knowledge of protein interactions at mammalian CNS synapses.
ESTHER : Deng_2006_J.Neurosci_26_7875
PubMedSearch : Deng_2006_J.Neurosci_26_7875
PubMedID: 16870733

Title : Prognosis of elderly patients with acute myelogenous leukemia: analysis of 126 AML cases - Iwakiri_2002_Int.J.Hematol_75_45
Author(s) : Iwakiri R , Ohta M , Mikoshiba M , Tsutsumi H , Kumakawa T , Mori M
Ref : Int J Hematol , 75 :45 , 2002
Abstract : We retrospectively analyzed 126 acute myelogenous leukemia (AML) patients aged > or =60 years who had all been referred to the same hematological department between 1989 and 1999. In 76 de novo AML cases, 53 patients (median age, 72 years) were treated with combination chemotherapy (CT) for remission induction. Complete remission (CR) rate was 57.1%. The median overall survival (OS) was 16 months, and the rate of 3-year OS was 28%. The favorable prognostic factors were performance status < or =2, cholinesterase > or =100 IU, and intermediate or favorable karyotype (P < .01). Seventeen patients (median age, 78 years) with hypocellular bone marrow or poor general condition were treated with low-dose cytosine arabinoside (LDAraC). In these patients, the CR rate was 50% and the median OS was 11 months, with an OS estimate at 3 years of 14%. All patients with hypocellular bone marrow who received LDAraC for 21 days achieved CR. In 50 patients who developed AML following a myelodysplastic syndrome (MDS/AML), 22 patients (median age, 74 years) were treated with CT, and 14 (median age, 74 years) patients were treated with LDAraC. The CR rates were 22.7% and 21.4%, respectively, and the median OS durations were 8 months and 11 months, respectively. There were no significant factors that would indicate a good prognosis in MDS/AML patients.
ESTHER : Iwakiri_2002_Int.J.Hematol_75_45
PubMedSearch : Iwakiri_2002_Int.J.Hematol_75_45
PubMedID: 11843290

Title : Purification, molecular cloning, and functional expression of dog liver microsomal acyl-CoA hydrolase: a member of the carboxylesterase multigene family - Hosokawa_2001_Arch.Biochem.Biophys_389_245
Author(s) : Hosokawa M , Suzuki K , Takahashi D , Mori M , Satoh T , Chiba K
Ref : Archives of Biochemistry & Biophysics , 389 :245 , 2001
Abstract : To clarify the reason for the high acyl-CoA hydrolase (ACH) activity found in dog liver microsomes, the ACH was purified to homogeneity using column chromatography. The purified enzyme, named ACH D1, exhibited a subunit molecular weight of 60 KDa. The amino terminal amino acid sequence showed a striking homology with rat liver carboxylesterase (CES) isozymes. ACH D1 possessed hydrolytic activities toward esters containing xenobiotics in addition to acyl-CoA thioesters, and these activities were inhibited by a specific inhibitor of CES or by CES RH1 antibodies. These findings suggest that this protein is a member of the CES multigene family. Since ACH D1 appears to be a protein belonging to the CES family, we cloned the cDNA from a dog liver lambdagt10 library with a CES-specific probe. The clone obtained, designated CES D1, possessed several motifs characterizing CES isozymes, and the deduced amino acid sequences were 100% identical with those of ACH D1 in the first 18 amino acid residues. When it was expressed in V79 cells, it showed high catalytic activities toward acyl-CoA thioesters. In addition, the characteristics of the expressed protein were identical with those of ACH D1 in many cases, suggesting that CES D1 encodes liver microsomal ACH D1.
ESTHER : Hosokawa_2001_Arch.Biochem.Biophys_389_245
PubMedSearch : Hosokawa_2001_Arch.Biochem.Biophys_389_245
PubMedID: 11339814
Gene_locus related to this paper: canfa-CESDD1

Title : cDNA cloning, characterization and stable expression of novel human brain carboxylesterase - Mori_1999_FEBS.Lett_458_17
Author(s) : Mori M , Hosokawa M , Ogasawara Y , Tsukada E , Chiba K
Ref : FEBS Letters , 458 :17 , 1999
Abstract : The DNA sequence encoding a novel human brain carboxylesterase (CES) has been determined. The protein is predicted to have 567 amino acids, including conserved motifs, such as GESAGG, GXXXXEFG, and GDHGD which comprise a catalytic triad, and the endoplasmic reticulum retention motif (HXEL-COOH) observed in CES families. Their gene products exhibited hydrolase activity towards temocapril, p-nitrophenyl-acetate and long-chain acyl-CoA. Since the molecular masses of these gene products are similar to those that exist in capillary endothelial cells of the human brain [Yamamda et al. (1994) Brain Res. 658, 163-167], these CES isozymes may function as a blood-brain barrier to protect the central nervous system from ester or amide compounds.
ESTHER : Mori_1999_FEBS.Lett_458_17
PubMedSearch : Mori_1999_FEBS.Lett_458_17
PubMedID: 10518925
Gene_locus related to this paper: human-CES1 , mouse-Ces1d

Title : A new point mutation in cholinesterase: relationship between multiple mutation sites and enzyme activity - Takagi_1997_Internat.Hepat.Com_6_288
Author(s) : Takagi H , Narahara A , Takayama H , Shimoda R , Nagamine T , Mori M
Ref : International Hepatology Communications , 6 :288 , 1997
Abstract : A new mutation site has been found in a case of cholinesterase (ChE) deficiency diagnosed upon routine blood screening. Genomic DNA was sequenced and four point mutations were found: P1 (exon 2) nucleotide 298 (CCA-TCA), codon 100 (proline-serine), which is a novel mutation site; P4 (exon 2) nucleotide 1410 (CGT-CGG), codon 470 (arginine not changed); PS (exon 3) nucleotide 1543 (CGT-TGT), codon 515 (arginine-threonine); and P6 (exon 4) nucleotide 1615 (GCA-ACA), codon 539 (alanine-threonine). The patient had three (P1, P5, P6) heterozygous and one (P4) homozygous mutations. The three other family members studied had one (P1) or two (P5 and 6) heterozygous mutations in addition to a P4 homozygous mutation but their serum levels of ChE were normal or only slightly decreased. We concluded that three simultaneous mutations at codons 298, 1543 and 1615 are required to reduce serum ChE activity and that the single mutation at codon 298 or two mutations at codon 1543 and 1615 are not enough to reduce ChE activity.
ESTHER : Takagi_1997_Internat.Hepat.Com_6_288
PubMedSearch : Takagi_1997_Internat.Hepat.Com_6_288

Title : New mutation site of cholinesterase gene [editorial\; comment] -
Author(s) : Takagi H , Mori M
Ref : Intern Med , 36 :1 , 1997
PubMedID: 9058091

Title : Histochemical and cytochemical study of butyrylcholinesterase activity in rat hepatocellular carcinomas induced by 3'-methyl-4- dimethylaminoazobenzene - Yokoyama_1982_Cancer.Res_42_4158
Author(s) : Yokoyama S , Kaneko A , Dempo K , Chisaka N , Mori M , Onoe T
Ref : Cancer Research , 42 :4158 , 1982
Abstract : The activity of butyrylcholinesterase (BCHE), a liver fetal isozyme (Zone L-V) of a nonspecific esterase, was studied histochemically and cytochemically in rat hepatocellular carcinomas induced by 3'-methyl-4-dimethylaminoazobenzene (3'-Me-DAB). In normal adult rats, BCHE activity was very prominent in cells of the intestinal mucosa but was not detectable in the liver. On the other hand, in fetal rat liver, a few cells scattered throughout the organ were BCHE positive. 3'-Me-DAB induced poorly differentiated hepatocellular carcinomas showing an intense BCHE activity, especially in areas consisting of small tumoral cells proliferating in a sheet-like pattern. Surrounding noncancerous liver tissue was completely devoid of reaction products. Less-differentiated trabecular hepatocellular carcinomas also showed a positive reaction. On the other hand, well-differentiated hepatocellular carcinoma and hepatocellular carcinoma with an adenomatous pattern were barely stained, while areas of cholangiofibrosis were usually negative. Thus, in confirmation of a previous report, BCHE appears to be a positive marker of poorly differentiated hepatocellular carcinomas induced by 3'-Me-DAB. By electron microscopy, reaction products were demonstrated in the cisternae of the endoplasmic reticulum, in the nuclear envelopes, and sometimes on the cell surface of undifferentiated tumoral cells. The significance of the appearance of BCHE activity in hepatocellular carcinomas induced by 3'-Me-DAB is discussed.
ESTHER : Yokoyama_1982_Cancer.Res_42_4158
PubMedSearch : Yokoyama_1982_Cancer.Res_42_4158
PubMedID: 7105011