Saito T

References (48)

Title : Synthetic Studies on Tetracyclic Diquinane Lycopodium Alkaloids Magellanine, Magellaninone and Paniculatine - Saito_2023_Molecules_28_
Author(s) : Saito T , Awad JM , Zhang W
Ref : Molecules , 28 : , 2023
Abstract : (-)-Magellanine, (+)-magellaninone, and (+)-paniculatine are three natural products isolated from the Lycopodium family that share a unique 6-5-5-6-fused tetracyclic diquinane core skeleton. Several members of this family have potent s anti-inflammatory and acetylcholinesterase-inhibitory properties and are under development for the treatment of Alzheimer's and other neurodegenerative diseases. Several research groups have undertaken the formal and total syntheses of this class of natural products. This review highlights over 20 reported total syntheses of these three alkaloids and the development of synthetic methods for the assembly of their core skeletons.
ESTHER : Saito_2023_Molecules_28_
PubMedSearch : Saito_2023_Molecules_28_
PubMedID: 36771167

Title : Synthesis of Carlactone Derivatives to Develop a Novel Inhibitor of Strigolactone Biosynthesis - Kawada_2023_ACS.Omega_8_13855
Author(s) : Kawada K , Saito T , Onoda S , Inayama T , Takahashi I , Seto Y , Nomura T , Sasaki Y , Asami T , Yajima S , Ito S
Ref : ACS Omega , 8 :13855 , 2023
Abstract : Strigolactones (SLs), phytohormones that inhibit shoot branching in plants, promote the germination of root-parasitic plants, such as Striga spp. and Orobanche spp., which drastically reduces the crop yield. Therefore, reducing SL production via chemical treatment may increase the crop yield. To design specific inhibitors, it is valid to utilize the substrate structure of the target proteins as lead compounds. In this study, we focused on Os900, a rice enzyme that oxidizes the SL precursor carlactone (CL) to 4-deoxyorobanchol (4DO), and synthesized 10 CL derivatives. The effects of the synthesized CL derivatives on SL biosynthesis were evaluated by the Os900 enzyme assay in vitro and by measuring 4DO levels in rice root exudates. We identified some CL derivatives that inhibited SL biosynthesis in vitro and in vivo.
ESTHER : Kawada_2023_ACS.Omega_8_13855
PubMedSearch : Kawada_2023_ACS.Omega_8_13855
PubMedID: 37091382

Title : Molecular Interactions between an Enzyme and Its Inhibitor for Selective Detection of Limonene - Saito_2022_Anal.Chem__
Author(s) : Saito T , Nishida Y , Tabata M , Isobayashi A , Tomizawa H , Miyahara Y , Sugizaki Y
Ref : Analytical Chemistry , : , 2022
Abstract : Researchers widely apply enzyme inhibition to chemicals such as pesticides, nerve gases, and anti-Alzheimer's drugs. However, application of enzyme inhibition to odorant sensors is less common because the corresponding reaction mechanisms have not yet been clarified in detail. In this study, we propose a new strategy for highly selective detection of odorant molecules by using an inhibitor-specific enzyme. As an example, we analyzed the selective interactions between acetylcholinesterase (AChE) and limonenethe major odorant of citrus and an AChE inhibitorusing molecular dynamics simulations. In these simulations, limonene was found to be captured at specific binding sites of AChE by modifying the binding site of acetylcholine (ACh), which induced inhibition of the catalytic activity of AChE toward ACh hydrolysis. We confirmed the simulation results by experiments using an ion-sensitive field-effect transistor, and the degree of inhibition of ACh hydrolysis depended on the limonene concentration. Accordingly, we quantitatively detected limonene at a detection limit of 5.7 microM. We furthermore distinguished the response signals to limonene from those to other odorants, such as pinene and perillic acid. Researchers will use our proposed odorant detection method for other odorant-enzyme combinations and applications of miniaturized odorant-sensing systems based on rapid testing.
ESTHER : Saito_2022_Anal.Chem__
PubMedSearch : Saito_2022_Anal.Chem__
PubMedID: 35543317

Title : Early administration of galantamine from preplaque phase suppresses oxidative stress and improves cognitive behavior in APPswe\/PS1dE9 mouse model of Alzheimer's disease - Saito_2019_Free.Radic.Biol.Med_145_20
Author(s) : Saito T , Hisahara S , Iwahara N , Emoto MC , Yokokawa K , Suzuki H , Manabe T , Matsumura A , Suzuki S , Matsushita T , Kawamata J , Sato-Akaba H , Fujii HG , Shimohama S
Ref : Free Radic Biol Med , 145 :20 , 2019
Abstract : Alzheimer's disease (AD) is a common neurodegenerative disease that progressively impairs memory and cognition. Deposition of amyloid-beta (Abeta) peptides is the most important pathophysiological hallmark of AD. Oxidative stress induced by generation of reactive oxygen species (ROS) is a prominent phenomenon in AD and known to occur early in the course of AD. Several reports suggest a relationship between change in redox status and AD pathology including progressive Abeta deposition, glial cell activation, and inflammation. Galantamine is an acetylcholinesterase inhibitor and has been reported to have an oxidative stress inhibitory function. In the present study, galantamine was administered orally to AD model mice from before the appearance of Abeta plaques (preplaque phase), and in vivo change in redox status of the brain was measured using electron paramagnetic resonance (EPR) imaging. Administration of galantamine from the preplaque phase ameliorated memory decline in Morris water maze test and novel object recognition test. Monitoring of the redox status of the brain using EPR imaging showed that galantamine treatment improved the unbalanced redox state. Additionally, galantamine administration enhanced microglial function to promote Abeta clearance, reducing the Abeta-positive area in the cortex and amount of insoluble Abeta in the brain. In contrast, galantamine treatment from the preplaque phase suppressed the production of proinflammatory cytokines through neurotoxic microglial activity. Therefore, galantamine administration from the preplaque phase may have the potential of clinical application for the prevention of AD. In addition, our results demonstrate the usefulness of EPR imaging for speedy and quantitative evaluation of the efficacy of disease-modifying drugs for AD.
ESTHER : Saito_2019_Free.Radic.Biol.Med_145_20
PubMedSearch : Saito_2019_Free.Radic.Biol.Med_145_20
PubMedID: 31536772

Title : The prediction of response to Galantamine treatment in Patients with mild to moderate Alzheimer's Disease - Ohnishi_2014_Curr.Alzheimer.Res_11_110
Author(s) : Ohnishi T , Sakiyama Y , Okuri Y , Kimura Y , Sugiyama N , Saito T , Takahashi M , Kobayashi T
Ref : Curr Alzheimer Res , 11 :110 , 2014
Abstract : The prediction of efficacy in long-term treatment of acetylcholinesterase inhibitors (AChEIs) is a major clinical issue, although no consistently strong predictive factors have emerged thus far. The present analyses aimed to identify factors for predicting long-term outcome of galantamine treatment. Analyses were conducted with data from a 24 weeks randomized, double-blind, placebo controlled trial to evaluate the efficacy and the safety of galantamine in the treatment of 303 patients with mild to moderate AD. Patients were divided into responders (4 or more point improvement of ADAScog scores at 24 weeks of treatment) and non-responders. We explored whether patients' background (e.g. sex, age, and duration of disease) and scores of cognitive scales at early stage, are relevant to the long-term response to AChEIs. Predictive values were estimated by the logistic regression model. The responder rate was 31.7%. We found that changes in scores of ADAS-J cog subscales between week 4 and baseline, especially word recognition, can be a good variable to predict subsequent response to galantamine, with approximately 75% of predictive performance. Characteristics of patients, including demographic characteristics, severity of disease and neuropsychological features before treatment were poorly predictive. The present study indicate that initial response to galantamine administration in patients with mild to moderate AD seems to be a reliable predictor of response of consequent galantamine treatment. Patients who show improvement of episodic memory function during the first 4 weeks of galantamine administration may be likely to particularly benefit from galantamine treatment.
ESTHER : Ohnishi_2014_Curr.Alzheimer.Res_11_110
PubMedSearch : Ohnishi_2014_Curr.Alzheimer.Res_11_110
PubMedID: 24156269

Title : Total cholesterol level for assessing pancreatic insufficiency due to chronic pancreatitis - Hirano_2014_Gut.Liver_8_563
Author(s) : Hirano K , Saito T , Mizuno S , Tada M , Sasahira N , Isayama H , Matsukawa M , Umefune G , Akiyama D , Saito K , Kawahata S , Takahara N , Uchino R , Hamada T , Miyabayashi K , Mohri D , Sasaki T , Kogure H , Yamamoto N , Nakai Y , Koike K
Ref : Gut Liver , 8 :563 , 2014
Abstract : BACKGROUND/AIMS: To determine the nutritional markers important for assessing the degree of pancreatic insufficiency due to chronic pancreatitis in routine clinical practice.
METHODS: A total of 137 patients with chronic pancreatitis were followed up for more than 1 year. They were divided into two groups: a pancreatic diabetes mellitus (DM) group, consisting of 47 patients undergoing medical treatment for DM of pancreatic origin, and a nonpancreatic DM group, consisting of 90 other patients (including 86 patients without DM). Serum albumin, prealbumin, total cholesterol, cholinesterase, magnesium, and hemoglobin were compared between the two groups.
RESULTS: The total cholesterol was significantly lower in the pancreatic than the nonpancreatic DM group (164 mg/dL vs 183 mg/dL, respectively; p=0.0028). Cholinesterase was significantly lower in the former group (263 U/L vs 291 U/L, respectively; p=0.016). Among the 37 patients with nonalcoholic pancreatitis, there was no difference in the cholinesterase levels between the pancreatic and nonpancreatic (296 U/L vs 304 U/L, respectively; p=0.752) DM groups, although cholesterol levels remained lower in the former (165 mg/dL vs 187 mg/dL, respectively; p=0.052).
CONCLUSIONS: Cholinesterase levels are possibly affected by concomitant alcoholic liver injury. The total cholesterol level should be considered when assessing pancreatic insufficiency due to chronic pancreatitis.
ESTHER : Hirano_2014_Gut.Liver_8_563
PubMedSearch : Hirano_2014_Gut.Liver_8_563
PubMedID: 25228979

Title : Chemical analysis and acetylcholinesterase inhibitory effect of anthocyanin-rich red leaf tea (cv. Sunrouge) - Maeda-Yamamoto_2012_J.Sci.Food.Agric_92_2379
Author(s) : Maeda-Yamamoto M , Saito T , Nesumi A , Tokuda Y , Ema K , Honma D , Ogino A , Monobe M , Murakami A , Tachibana H
Ref : J Sci Food Agric , 92 :2379 , 2012
Abstract : BACKGROUND: The purpose of this study was to evaluate the effects of leaf order or crop season on anthocyanins and other chemicals in the anthocyanin-rich tea cultivar 'Sunrouge' (Camellia sinensis x C. taliensis) by using high-performance liquid chromatography, and to study the effect of 'Sunrouge' extract on acetylcholinesterase (AChE) activity in human neuroblastoma SK-N-SH cells. RESULTS: The total anthocyanin content was higher in the third (3.09 mg g(-)(1)) than in the second (2.24 mg g(-)(1)) or first crop season (1.79 mg g(-)(1)). The amount of anthocyanins contained in the stem was high (1.61 mg g(-)(1)). In the third crop season, the concentrations of delphinidin-3-O-beta-D-(6-(E)-p-coumaroyl)galactopyranoside (DCGa), cyanidin-3-O-beta-D-(6-(E)-p-coumaroyl)galactopyranoside, delphinidin-3-O-beta-D-galactopyranoside, delphinidin-3-O-beta-D-(6-O-(Z)-p-coumaroyl)galactopyranoside, cyanidin-3-O-beta-D-galactoside, and delphinidin-3-O-beta-D-glucoside were 1.57 mg g(-)(1), 0.52 mg g(-)(1), 0.40 mg g(-)(1), 0.22 mg g(-)(1), 0.14 mg g(-)(1), and 0.11 mg g(-)(1), respectively. DCGa accounted for about 50% of the anthocyanins present. The suppressive effect of 'Sunrouge' water extract on AChE activity in human neuroblastoma SK-N-SH cells was the strongest among the three tea cultivars ('Sunrouge', 'Yabukita' and 'Benifuuki'). CONCLUSION: These results suggested that 'Sunrouge' might protect humans from humans from AChE-related diseases by suppressing AChE activity. To obtain sufficient amounts of anthocyanins, catechins and/or caffeine for a functional food material, 'Sunrouge' from the third crop season should be used.
ESTHER : Maeda-Yamamoto_2012_J.Sci.Food.Agric_92_2379
PubMedSearch : Maeda-Yamamoto_2012_J.Sci.Food.Agric_92_2379
PubMedID: 22419270

Title : Comparative genomics of the social amoebae Dictyostelium discoideum and Dictyostelium purpureum - Sucgang_2011_Genome.Biol_12_R20.1
Author(s) : Sucgang R , Kuo A , Tian X , Salerno W , Parikh A , Feasley CL , Dalin E , Tu H , Huang E , Barry K , Lindquist E , Shapiro H , Bruce D , Schmutz J , Salamov A , Fey P , Gaudet P , Anjard C , Babu MM , Basu S , Bushmanova Y , van der Wel H , Katoh-Kurasawa M , Dinh C , Coutinho PM , Saito T , Elias M , Schaap P , Kay RR , Henrissat B , Eichinger L , Rivero F , Putnam NH , West CM , Loomis WF , Chisholm RL , Shaulsky G , Strassmann JE , Queller DC , Kuspa A , Grigoriev IV
Ref : Genome Biol , 12 :R20 , 2011
Abstract : BACKGROUND: The social amoebae (Dictyostelia) are a diverse group of Amoebozoa that achieve multicellularity by aggregation and undergo morphogenesis into fruiting bodies with terminally differentiated spores and stalk cells. There are four groups of dictyostelids, with the most derived being a group that contains the model species Dictyostelium discoideum.
RESULTS: We have produced a draft genome sequence of another group dictyostelid, Dictyostelium purpureum, and compare it to the D. discoideum genome. The assembly (8.41 x coverage) comprises 799 scaffolds totaling 33.0 Mb, comparable to the D. discoideum genome size. Sequence comparisons suggest that these two dictyostelids shared a common ancestor approximately 400 million years ago. In spite of this divergence, most orthologs reside in small clusters of conserved synteny. Comparative analyses revealed a core set of orthologous genes that illuminate dictyostelid physiology, as well as differences in gene family content. Interesting patterns of gene conservation and divergence are also evident, suggesting function differences; some protein families, such as the histidine kinases, have undergone little functional change, whereas others, such as the polyketide synthases, have undergone extensive diversification. The abundant amino acid homopolymers encoded in both genomes are generally not found in homologous positions within proteins, so they are unlikely to derive from ancestral DNA triplet repeats. Genes involved in the social stage evolved more rapidly than others, consistent with either relaxed selection or accelerated evolution due to social conflict.
CONCLUSIONS: The findings from this new genome sequence and comparative analysis shed light on the biology and evolution of the Dictyostelia.
ESTHER : Sucgang_2011_Genome.Biol_12_R20.1
PubMedSearch : Sucgang_2011_Genome.Biol_12_R20.1
PubMedID: 21356102
Gene_locus related to this paper: dicpu-f0z7q0 , dicpu-f0z822 , dicpu-f0zfi0 , dicpu-f0zjs1 , dicpu-f0zks4 , dicpu-f0zmm3 , dicpu-f0zmm8 , dicpu-f0zmm9 , dicpu-f0zni7 , dicpu-f0znl3 , dicpu-f0zq90 , dicpu-f0zvn5 , dicpu-f0zxa4 , dicpu-f0zyf9 , dicpu-f1a3n5 , dicpu-f1a5b4 , dicpu-f1a269 , dicpu-f1a615 , dicpu-f0ztw9 , dicpu-f0zri3 , dicpu-f0zys7

Title : Enzymatic hydrolysis of structurally diverse phthalic acid esters by porcine and bovine pancreatic cholesterol esterases - Saito_2010_Chemosphere_81_1544
Author(s) : Saito T , Hong P , Tanabe R , Nagai K , Kato K
Ref : Chemosphere , 81 :1544 , 2010
Abstract : A weak hydrolyzing activity against bis (2-ethylhexyl) phthalate (DEHP) was discovered in a commercial crude lipase (EC preparation from porcine pancreas. DEHP was hydrolyzed to mono (2-ethylhexyl) phthalate (MEHP) not by a pancreatic lipase but by a cholesterol esterase (CEase, EC, a trace contaminant in the crude lipase preparation. Enzymatic hydrolysis of phthalic acid esters (PAEs), suspected to be endocrine-disrupting chemicals, was investigated using CEases from two species of mammals and a microorganism. Eight structurally diverse PAEs, namely diethyl phthalate (DEP), di-n-propyl phthalate (DPrP), di-n-butyl phthalate (DBP), di-n-pentyl phthalate (DPeP), di-n-hexyl phthalate (DHP), DEHP, n-butyl benzyl phthalate (BBP), and dicyclohexyl phthalate (DCHP), were hydrolyzed to their corresponding monoesters by both porcine and bovine pancreatic CEases, while a microbial CEase from Pseudomonas sp. had no hydrolyzing activity against these PAEs. The hydrolysis experiments with bovine pancreatic CEase (50 U) indicated complete hydrolysis of every PAE (5 mumole) except for BBP and DCHP within 15 min; BBP and DCHP were hydrolyzed within 30 min and 6h, respectively. The rates of PAE hydrolysis could be affected by the bulkiness of alkyl side chains in the PAEs. This study provides important evidence that mammalian pancreatic CEases, such as those from porcine and bovine sources, are potential enzymes for nonspecific degradation of structurally diverse PAEs.
ESTHER : Saito_2010_Chemosphere_81_1544
PubMedSearch : Saito_2010_Chemosphere_81_1544
PubMedID: 20822795
Gene_locus related to this paper: bovin-balip , pig-i3ltk9

Title : Risk factors for early death due to recurrence after resection of large hepatocellular carcinomas - Kaibori_2008_Hepatogastroenterology_55_2151
Author(s) : Kaibori M , Matsui K , Saito T , Kamiyama Y
Ref : Hepato-Gastroenterology , 55 :2151 , 2008
Abstract : BACKGROUND/AIM: Long-term survival after resection of hepatocellular carcinomas larger than 5 cm in diameter is worse than after resection of smaller tumors. The risk factors for early death due to recurrence after resection of large tumors have not been clearly elucidated. METHODOLOGY: Among 377 patients who underwent curative resection of hepatocellular carcinoma between 1992 and 2004, 115 patients with tumors larger than 5 cm in diameter were enrolled. They were divided into two groups, i.e., 35 patients who died of recurrent cancer within 2 years after surgery and 80 patients who survived for more than 2 years. RESULTS: The preoperative serum alpha-fetoprotein level, positive surgical margins, number of tumors, the serum levels of albumin and alpha-fetoprotein at 1 and 3 months after surgery, as well as the prothrombin time, cholinesterase and protein induced by vitamin K antagonism-II levels at 3 months, respectively, were significant determinants of survival by univariate analysis. Multivariate analysis showed that an albumin level <3.5 g/dl at 1 month and a cholinesterase level <100 U/L at 3 months after surgery were associated with an increased risk of early death due to recurrence. CONCLUSIONS: The hepatic functional reserve in the early postoperative period significantly influences early recurrence and early death after resection of large hepatocellular carcinomas. It is important to maintain a good perioperative nutritional status and early postoperative adjuvant therapy is required for patients with large tumors.
ESTHER : Kaibori_2008_Hepatogastroenterology_55_2151
PubMedSearch : Kaibori_2008_Hepatogastroenterology_55_2151
PubMedID: 19260495

Title : Common null variant, Arg192Stop, in a G-protein coupled receptor, olfactory receptor 1B1, associated with decreased serum cholinesterase activity - Koyano_2008_Hepatol.Res_38_696
Author(s) : Koyano S , Emi M , Saito T , Makino N , Toriyama S , Ishii M , Kubota I , Kato T , Kawata S
Ref : Hepatol Res , 38 :696 , 2008
Abstract : AIM: Non-functioning single nucleotide polymorphisms (nSNPs) that result in premature termination codons, that is null-alleles of the respective genes, may have phenotypic effects on clinical parameters. We conducted association studies involving several G-protein coupled receptors (GPCRs) that harbor nSNPs, using clinical parameters of liver function in a general population consisting of 2969 Japanese adults. METHODS: SNP typings were performed with TaqMan and Invader assays. Quantitative associations between genotypes and clinical parameters were analyzed by analysis of variance. Linkage disequilibrium (LD) was tested by Haploview Version 3.3. Haplotype-based association was performed using the haplo.stats program. RESULTS: A significant correlation (P = 0.0057) was identified between serum cholinesterase activity (CHE) and an nSNP (Arg192Stop) in the olfactory receptor (OR) 1B1 gene, a member of the GPCR gene family. This nSNP was associated with decreased serum CHE (P = 0.0013). LD analysis based on eight selected SNPs at the locus revealed three LD blocks. The Arg192Stop nSNP was located on the second LD block, which covered one-third of the 3'-portion of the gene. CONCLUSION: These results suggested that the null-allele of OR1B1 might affect metabolism of serum cholinesterase in carriers of this nSNP.
ESTHER : Koyano_2008_Hepatol.Res_38_696
PubMedSearch : Koyano_2008_Hepatol.Res_38_696
PubMedID: 18328065

Title : Prognostic factors and toxicokinetics in acute fenitrothion self-poisoning requiring intensive care - Inoue_2008_Clin.Toxicol.(Phila)_46_528
Author(s) : Inoue S , Saito T , Suzuki Y , Iizuka S , Takazawa K , Akieda K , Yamamoto I , Inokuchi S
Ref : Clinical Toxicology (Phila) , 46 :528 , 2008
Abstract : OBJECTIVE: We aimed to evaluate prognostic factors and toxicokinetics in acute fenitrothion self-poisoning.
METHODS: We reviewed 12 patients with fenitrothion self-poisoning admitted to the intensive care unit between 2003 and 2006. We compared the characteristics, initial vital signs, physiological scores, corrected QT interval on electrocardiogram and laboratory data (serum fenitrothion concentration and cholinesterase activity) of non-survivors and survivors. Furthermore, we evaluated the correlation between the prognostic factors and severity of poisoning (lengths of intensive care unit and hospital stays), and the toxicokinetics of the patients.
RESULTS: In the 2 non-survivors, the estimated fenitrothion ingestion dose and the serum fenitrothion concentration at the emergency department and at 24 h after ingestion were significantly higher than those in the 10 survivors. (P = 0.008, 0.003, and 0.04, respectively). In the 10 survivors, the serum fenitrothion concentration at 24 h after ingestion was significantly correlated with the lengths of intensive care unit and hospital stays (P = 0.004 and 0.04, respectively); however, the initial vital signs, physiological scores, corrected QT interval on electrocardiogram at the emergency department, and serum cholinesterase activity did not show any correlation. In five patients successfully fitted to a two-compartment model, the distribution and elimination half-lives were 2.5 and 49.8 h, respectively, which is compatible with the slow and prolonged clinical course of fenitrothion poisoning. CONCLUSION. Estimated fenitrothion ingestion dose and serum fenitrothion concentration at the emergency department and at 24 h after ingestion may be useful prognostic factors in acute fenitrothion self-poisoning. Furthermore, we should take care for the patients whose serum fenitrothion concentration is high.
ESTHER : Inoue_2008_Clin.Toxicol.(Phila)_46_528
PubMedSearch : Inoue_2008_Clin.Toxicol.(Phila)_46_528
PubMedID: 18584365

Title : Rapid simultaneous determination for organophosphorus pesticides in human serum by LC-MS - Inoue_2007_J.Pharm.Biomed.Anal_44_258
Author(s) : Inoue S , Saito T , Mase H , Suzuki Y , Takazawa K , Yamamoto I , Inokuchi S
Ref : J Pharm Biomed Anal , 44 :258 , 2007
Abstract : A simple and rapid method was developed for measuring 10 organophosphorus pesticides (acephate, methidathion, dichlorvos, fenthion, EPN, diazinon, phenthoate, malathion, fenitrothion, and cyanophos) in the serum of acute poisoning patients by LC/MS. Following deproteinization by acetonitrile, an aliquot of the biological sample was injected into a C(18) column using 10mM ammonium formate-methanol as the mobile phase. Extraction recoveries were satisfactory and ranged between 60.0 and 108.1% in serum. The limits of detection (LODs) in serum ranged from 0.125 to 1 microg/ml, and the limits of quantitation (LOQs) ranged from 0.25 to 1.25 microg/ml. An excellent linearity was observed for these LOQs up to 8 microg/ml. Intra- and interassay precision and accuracy were satisfactory for most of the pesticides analyzed. In terms of temperature stability, of all the organophosphorus compounds analyzed, dichlorvos and malathion exhibited the most rapid degradations over 24h at room temperature. Methidathion and diazinon remained relatively stable at all temperatures during the entire 4-week testing period. The present method was successfully applied to one actual case of acute poisoning. In conclusion, this method is simple, accurate, and useful for the determination of organophosphorus pesticides and should benefit both clinical and forensic toxicology.
ESTHER : Inoue_2007_J.Pharm.Biomed.Anal_44_258
PubMedSearch : Inoue_2007_J.Pharm.Biomed.Anal_44_258
PubMedID: 17337150

Title : Purification and molecular cloning of an intracellular 3-hydroxybutyrate-oligomer hydrolase from Paucimonas lemoignei - Uchino_2007_J.Biosci.Bioeng_104_224
Author(s) : Uchino K , Katsumata Y , Takeda T , Arai H , Shiraki M , Saito T
Ref : J Biosci Bioeng , 104 :224 , 2007
Abstract : An intracellular 3-hydroxybutyrate-oligomer hydrolase was purified from a poly(3-hydroxybutyrate)-degrading bacterium, Paucimonas lemoignei. It hydrolyzed the 3-hydroxybutyrate dimer with the highest specific activity of any of the enzymes reported so far. The gene was cloned and sequenced. The deduced amino acid sequence showed that the enzyme is a homolog of the PhaZc of Ralstonia eutropha H16.
ESTHER : Uchino_2007_J.Biosci.Bioeng_104_224
PubMedSearch : Uchino_2007_J.Biosci.Bioeng_104_224
PubMedID: 17964488

Title : Successful pediatric living donor liver transplantation from carrier to carrier of hereditary butyrylcholinesterase variant - Kawano_2007_Pediatr.Transplant_11_694
Author(s) : Kawano Y , Mizuta K , Hisikawa S , Saito T , Egami S , Takatsuka Y , Sanada Y , Fujiwara T , Yasuda Y , Ohmori M , Sakamoto K , Liu W , Nishiguchi S , Hada T , Kawarasaki H
Ref : Pediatr Transplant , 11 :694 , 2007
Abstract : Hypocholinesterasemia is often observed clinically, especially in various liver diseases. Not well known, however, is the fact that some patients have a hereditary BChE variant. Little has been reported on liver transplants associated with this hereditary BChE variant. Furthermore, no cases have been reported of a LDLT involving hereditary BChE variant that had been diagnosed preoperatively. A 23-month-old girl who had had a failed Kasai operation for biliary atresia underwent a liver transplant using as a graft her father's lateral segment. Preoperatively, she had been diagnosed with hypocholinesterasemia. As the donor, her father had undergone a preoperative examination, during which he was found to also have hypocholinesterasemia. DNA sequencing revealed that both had the hereditary BChE variant. The unique mutation caused a frame-shift mutation. Variant K was also detected. The patient was discharged 143 days after the operation and has had no problems with immunosuppression since. In conclusion, we report that the hereditary BChE variant is not a contraindication for either transplantation or living liver donation.
ESTHER : Kawano_2007_Pediatr.Transplant_11_694
PubMedSearch : Kawano_2007_Pediatr.Transplant_11_694
PubMedID: 17663697

Title : Relationship between periodontitis and hepatic condition in Japanese women - Saito_2006_J.Int.Acad.Periodontol_8_89
Author(s) : Saito T , Shimazaki Y , Koga T , Tsuzuki M , Ohshima A
Ref : J Int Acad Periodontol , 8 :89 , 2006
Abstract : The liver is an important organ closely associated with lipid and glucose metabolism. This study was performed to clarify the relationship between periodontitis and hepatic condition in apparently healthy Japanese women. A cross-sectional study was performed on 172 apparently healthy, dentulous Japanese women (20-59 years old) who attended a health promotion program at Fukuoka Health Promotion Center. After multivariate adjustment for age, smoking history and oral hygiene, which were known risk factors for periodontitis, the incidence of periodontitis (deepest probing depth > or =4 mm) in females was significantly increased with elevated serum levels of aspartate aminotransferase (AST, p < 0.01), alanine aminotransferase (ALT, p < 0.01) and cholinesterase (p < 0.001), and an AST-to-ALT ratio of less than one (p = 0.02). Further adjustment for either body mass index (BMI) or percent body fat did not attenuate these relationships. These results suggest that hepatic steatosis is associated with periodontitis in Japanese women.
ESTHER : Saito_2006_J.Int.Acad.Periodontol_8_89
PubMedSearch : Saito_2006_J.Int.Acad.Periodontol_8_89
PubMedID: 16865998

Title : The crystal structure of polyhydroxybutyrate depolymerase from Penicillium funiculosum provides insights into the recognition and degradation of biopolyesters - Hisano_2006_J.Mol.Biol_356_993
Author(s) : Hisano T , Kasuya K , Tezuka Y , Ishii N , Kobayashi T , Shiraki M , Oroudjev E , Hansma H , Iwata T , Doi Y , Saito T , Miki K
Ref : Journal of Molecular Biology , 356 :993 , 2006
Abstract : Polyhydroxybutyrate is a microbial polyester that can be produced from renewable resources, and is degraded by the enzyme polyhydroxybutyrate depolymerase. The crystal structures of polyhydroxybutyrate depolymerase from Penicillium funiculosum and its S39 A mutant complexed with the methyl ester of a trimer substrate of (R)-3-hydroxybutyrate have been determined at resolutions of 1.71 A and 1.66 A, respectively. The enzyme is comprised of a single domain, which represents a circularly permuted variant of the alpha/beta hydrolase fold. The catalytic residues Ser39, Asp121, and His155 are located at topologically conserved positions. The main chain amide groups of Ser40 and Cys250 form an oxyanion hole. A crevice is formed on the surface of the enzyme, to which a single polymer chain can be bound by predominantly hydrophobic interactions with several hydrophobic residues. The structure of the S39A mutant-trimeric substrate complex reveals that Trp307 is responsible for the recognition of the ester group adjacent to the scissile group. It is also revealed that the substrate-binding site includes at least three, and possibly four, subsites for binding monomer units of polyester substrates. Thirteen hydrophobic residues, which are exposed to solvent, are aligned around the mouth of the crevice, forming a putative adsorption site for the polymer surface. These residues may contribute to the sufficient binding affinity of the enzyme for PHB granules without a distinct substrate-binding domain.
ESTHER : Hisano_2006_J.Mol.Biol_356_993
PubMedSearch : Hisano_2006_J.Mol.Biol_356_993
PubMedID: 16405909
Gene_locus related to this paper: penfu-PHAZ

Title : Characterization of two 3-hydroxybutyrate dehydrogenases in poly(3-hydroxybutyrate)-degradable bacterium, Ralstonia pickettii T1 - Takanashi_2006_J.Biosci.Bioeng_101_501
Author(s) : Takanashi M , Saito T
Ref : J Biosci Bioeng , 101 :501 , 2006
Abstract : Two D-(-)-3-hydroxybutyrate (3HB) dehydrogenases, BDH1 and BDH2, were isolated and purified from a poly(3-hydroxybutyrate) (PHB)-degradable bacterium, Ralstonia pickettii T1. BDH1 activity increased in R. pickettii T1 cells grown on several organic acids as a carbon source but not on 3HB, whereas BDH2 activity markedly increased in the same cells grown on 3HB or PHB. To examine their biochemical properties, bdh1 and bdh2 were cloned and overexpressed in Escherichia coli, and their purified products were characterized. The kinetic parameters indicate that BDH1 is more suitable for converting acetoacetate to 3HB than BDH2, whereas BDH2 is more efficient for the reverse reaction than BDH1. Thus, R. pickettii T1 contains two BDHs with different biochemical properties and physiological roles: BDH1 for cell growth on organic acids other than 3HB and BDH2 for cell growth on 3HB or PHB.
ESTHER : Takanashi_2006_J.Biosci.Bioeng_101_501
PubMedSearch : Takanashi_2006_J.Biosci.Bioeng_101_501
PubMedID: 16935252

Title : Novel intracellular 3-hydroxybutyrate-oligomer hydrolase in Wautersia eutropha H16 - Kobayashi_2005_J.Bacteriol_187_5129
Author(s) : Kobayashi T , Uchino K , Abe T , Yamazaki Y , Saito T
Ref : Journal of Bacteriology , 187 :5129 , 2005
Abstract : Wautersia eutropha H16 (formerly Ralstonia eutropha) mobilizes intracellularly accumulated poly(3-hydroxybutyrate) (PHB) with intracellular poly(3-hydroxybutyrate) depolymerases. In this study, a novel intracellular 3-hydroxybutyrate-oligomer hydrolase (PhaZc) gene was cloned and overexpressed in Escherichia coli. Then PhaZc was purified and characterized. Immunoblot analysis with polyclonal antiserum against PhaZc revealed that most PhaZc is present in the cytosolic fraction and a small amount is present in the poly(3-hydroxybutyrate) inclusion bodies of W. eutropha. PhaZc degraded various 3-hydroxybutyrate oligomers at a high specific activity and artificial amorphous poly(3-hydroxybutyrate) at a lower specific activity. Native PHB granules and semicrystalline PHB were not degraded by PhaZc. A PhaZ deletion mutation enhanced the deposition of PHB in the logarithmic phase in nutrient-rich medium. PhaZc differs from the hydrolases of W. eutropha previously reported and is a novel type of intracellular 3-hydroxybutyrate-oligomer hydrolase, and it participates in the mobilization of PHB along with other hydrolases.
ESTHER : Kobayashi_2005_J.Bacteriol_187_5129
PubMedSearch : Kobayashi_2005_J.Bacteriol_187_5129
PubMedID: 16030206
Gene_locus related to this paper: alceu-q4w8c9

Title : The genome of the social amoeba Dictyostelium discoideum - Eichinger_2005_Nature_435_43
Author(s) : Eichinger L , Pachebat JA , Glockner G , Rajandream MA , Sucgang R , Berriman M , Song J , Olsen R , Szafranski K , Xu Q , Tunggal B , Kummerfeld S , Madera M , Konfortov BA , Rivero F , Bankier AT , Lehmann R , Hamlin N , Davies R , Gaudet P , Fey P , Pilcher K , Chen G , Saunders D , Sodergren E , Davis P , Kerhornou A , Nie X , Hall N , Anjard C , Hemphill L , Bason N , Farbrother P , Desany B , Just E , Morio T , Rost R , Churcher C , Cooper J , Haydock S , van Driessche N , Cronin A , Goodhead I , Muzny D , Mourier T , Pain A , Lu M , Harper D , Lindsay R , Hauser H , James K , Quiles M , Madan Babu M , Saito T , Buchrieser C , Wardroper A , Felder M , Thangavelu M , Johnson D , Knights A , Loulseged H , Mungall K , Oliver K , Price C , Quail MA , Urushihara H , Hernandez J , Rabbinowitsch E , Steffen D , Sanders M , Ma J , Kohara Y , Sharp S , Simmonds M , Spiegler S , Tivey A , Sugano S , White B , Walker D , Woodward J , Winckler T , Tanaka Y , Shaulsky G , Schleicher M , Weinstock G , Rosenthal A , Cox EC , Chisholm RL , Gibbs R , Loomis WF , Platzer M , Kay RR , Williams J , Dear PH , Noegel AA , Barrell B , Kuspa A
Ref : Nature , 435 :43 , 2005
Abstract : The social amoebae are exceptional in their ability to alternate between unicellular and multicellular forms. Here we describe the genome of the best-studied member of this group, Dictyostelium discoideum. The gene-dense chromosomes of this organism encode approximately 12,500 predicted proteins, a high proportion of which have long, repetitive amino acid tracts. There are many genes for polyketide synthases and ABC transporters, suggesting an extensive secondary metabolism for producing and exporting small molecules. The genome is rich in complex repeats, one class of which is clustered and may serve as centromeres. Partial copies of the extrachromosomal ribosomal DNA (rDNA) element are found at the ends of each chromosome, suggesting a novel telomere structure and the use of a common mechanism to maintain both the rDNA and chromosomal termini. A proteome-based phylogeny shows that the amoebozoa diverged from the animal-fungal lineage after the plant-animal split, but Dictyostelium seems to have retained more of the diversity of the ancestral genome than have plants, animals or fungi.
ESTHER : Eichinger_2005_Nature_435_43
PubMedSearch : Eichinger_2005_Nature_435_43
PubMedID: 15875012
Gene_locus related to this paper: dicdi-abhd , dicdi-ACHE , dicdi-apra , dicdi-cinbp , dicdi-CMBL , dicdi-crysp , dicdi-DPOA , dicdi-P90528 , dicdi-ppme1 , dicdi-Q8MYE7 , dicdi-q54cf7 , dicdi-q54cl7 , dicdi-q54cm0 , dicdi-q54ct5 , dicdi-q54cu1 , dicdi-q54d54 , dicdi-q54d66 , dicdi-q54dj5 , dicdi-q54dy7 , dicdi-q54ek1 , dicdi-q54eq6 , dicdi-q54et1 , dicdi-q54et7 , dicdi-q54f01 , dicdi-q54g24 , dicdi-q54g47 , dicdi-q54gi7 , dicdi-q54gw5 , dicdi-q54gx3 , dicdi-q54h23 , dicdi-q54h73 , dicdi-q54i38 , dicdi-q54ie5 , dicdi-q54in4 , dicdi-q54kz1 , dicdi-q54l36 , dicdi-q54li1 , dicdi-q54m29 , dicdi-q54n21 , dicdi-q54n35 , dicdi-q54n85 , dicdi-q54qe7 , dicdi-q54qi3 , dicdi-q54qk2 , dicdi-q54rl3 , dicdi-q54rl8 , dicdi-q54sy6 , dicdi-q54sz3 , dicdi-q54t49 , dicdi-q54t91 , dicdi-q54th2 , dicdi-q54u01 , dicdi-q54vc2 , dicdi-q54vw1 , dicdi-q54xe3 , dicdi-q54xl3 , dicdi-q54xu1 , dicdi-q54xu2 , dicdi-q54y48 , dicdi-q54yd0 , dicdi-q54ye0 , dicdi-q54yl1 , dicdi-q54yr8 , dicdi-q54z90 , dicdi-q55bx3 , dicdi-q55d01 , dicdi-q55d81 , dicdi-q55du6 , dicdi-q55eu1 , dicdi-q55eu8 , dicdi-q55fk4 , dicdi-q55gk7 , dicdi-Q54ZA6 , dicdi-q86h82 , dicdi-Q86HC9 , dicdi-Q86HM5 , dicdi-Q86HM6 , dicdi-q86iz7 , dicdi-q86jb6 , dicdi-Q86KU7 , dicdi-q550s3 , dicdi-q552c0 , dicdi-q553t5 , dicdi-q555e5 , dicdi-q555h0 , dicdi-q555h1 , dicdi-q557k5 , dicdi-q558u2 , dicdi-Q869Q8 , dicdi-u554 , dicdi-y9086 , dicdi-q54r44 , dicdi-f172a

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 : Properties of a novel intracellular poly(3-hydroxybutyrate) depolymerase with high specific activity (PhaZd) in Wautersia eutropha H16 - Abe_2005_J.Bacteriol_187_6982
Author(s) : Abe T , Kobayashi T , Saito T
Ref : Journal of Bacteriology , 187 :6982 , 2005
Abstract : A novel intracellular poly(3-hydroxybutyrate) (PHB) depolymerase (PhaZd) of Wautersia eutropha (formerly Ralstonia eutropha) H16 which shows similarity with the catalytic domain of the extracellular PHB depolymerase in Ralstonia pickettii T1 was identified. The positions of the catalytic triad (Ser190-Asp266-His330) and oxyanion hole (His108) in the amino acid sequence of PhaZd deduced from the nucleotide sequence roughly accorded with those of the extracellular PHB depolymerase of R. pickettii T1, but a signal peptide, a linker domain, and a substrate binding domain were missing. The PhaZd gene was cloned and the gene product was purified from Escherichia coli. The specific activity of PhaZd toward artificial amorphous PHB granules was significantly greater than that of other known intracellular PHB depolymerase or 3-hydroxybutyrate (3HB) oligomer hydrolases of W. eutropha H16. The enzyme degraded artificial amorphous PHB granules and mainly released various 3-hydroxybutyrate oligomers. PhaZd distributed nearly equally between PHB inclusion bodies and the cytosolic fraction. The amount of PHB was greater in phaZd deletion mutant cells than the wild-type cells under various culture conditions. These results indicate that PhaZd is a novel intracellular PHB depolymerase which participates in the mobilization of PHB in W. eutropha H16 along with other PHB depolymerases.
ESTHER : Abe_2005_J.Bacteriol_187_6982
PubMedSearch : Abe_2005_J.Bacteriol_187_6982
PubMedID: 16199568

Title : Roles of poly(3-hydroxybutyrate) depolymerase and 3HB-oligomer hydrolase in bacterial PHB metabolism - Sugiyama_2004_Curr.Microbiol_48_424
Author(s) : Sugiyama A , Kobayashi T , Shiraki M , Saito T
Ref : Curr Microbiol , 48 :424 , 2004
Abstract : Many poly-3-hydroxybutyrate (PHB)-degrading enzymes have been studied. But biological roles of 3HB-oligomer hydrolases (3HBOHs) and how PHB depolymerases (PHBDPs) and 3HBOHs cooperate in PHB metabolism are not fully elucidated. In this study, several PHBDPs and 3HBOHs from three types of bacteria were purified, and their substrate specificity, kinetic properties, and degradation products were investigated. From the results, PHBDP and 3HBOH seemed to play a role in PHB metabolism in three types of bacteria, as follows: (A) In Ralstonia pickettii T1, an extracellular PHBDP degrades extracellular PHB to various-sized 3HB-oligomers, which an extracellular 3HBOH hydrolyzes to 3HB-monomers. (B) In Acidovorax sp. SA1, an extracellular PHBDP hydrolyzes extracellular PHB to small 3HB-oligomers (dimer and trimer), which an intracellular 3HBOH efficiently degrades to 3HB in the cell. (C) In Ralstonia eutropha H16, an intracellular 3HBOH helps in the degradation of intracellular PHB inclusions by PHBDP.
ESTHER : Sugiyama_2004_Curr.Microbiol_48_424
PubMedSearch : Sugiyama_2004_Curr.Microbiol_48_424
PubMedID: 15170237
Gene_locus related to this paper: ralpi-hboh2 , cupnh-hboh

Title : Purification and properties of an intracellular 3-hydroxybutyrate-oligomer hydrolase (PhaZ2) in Ralstonia eutropha H16 and its identification as a novel intracellular poly(3-hydroxybutyrate) depolymerase - Kobayashi_2003_J.Bacteriol_185_3485
Author(s) : Kobayashi T , Shiraki M , Abe T , Sugiyama A , Saito T
Ref : Journal of Bacteriology , 185 :3485 , 2003
Abstract : An intracellular 3-hydroxybutyrate (3HB)-oligomer hydrolase (PhaZ2(Reu)) of Ralstonia eutropha was purified from Escherichia coli harboring a plasmid containing phaZ2(Reu). The purified enzyme hydrolyzed linear and cyclic 3HB-oligomers. Although it did not degrade crystalline poly(3-hydroxybutyrate) (PHB), the purified enzyme degraded artificial amorphous PHB at a rate similar to that of the previously identified intracellular PHB (iPHB) depolymerase (PhaZ1(Reu)). The enzyme appeared to be an endo-type hydrolase, since it actively hydrolyzed cyclic 3HB-oligomers. However, it degraded various linear 3HB-oligomers and amorphous PHB in the fashion of an exo-type hydrolase, releasing one monomer unit at a time. PhaZ2 was found to bind to PHB inclusion bodies and as a soluble enzyme to cell-free supernatant fractions in R. eutropha; in contrast, PhaZ1 bound exclusively to the inclusion bodies. When R. eutropha H16 was cultivated in a nutrient-rich medium, the transient deposition of PHB was observed: the content of PHB was maximized in the log growth phase (12 h, ca. 14% PHB of dry cell weight) and decreased to a very low level in the stationary phase (ca. 1% of dry cell weight). In each phaZ1-null mutant and phaZ2-null mutant, the PHB content in the cell increased to ca. 5% in the stationary phase. A double mutant lacking both phaZ1 and phaZ2 showed increased PHB content in the log phase (ca. 20%) and also an elevated PHB level (ca. 8%) in the stationary phase. These results indicate that PhaZ2 is a novel iPHB depolymerase, which participates in the mobilization of PHB in R. eutropha along with PhaZ1.
ESTHER : Kobayashi_2003_J.Bacteriol_185_3485
PubMedSearch : Kobayashi_2003_J.Bacteriol_185_3485
PubMedID: 12775684
Gene_locus related to this paper: cupnh-hboh

Title : Immunomodulation of human natural killer cell cytotoxic function by triazine and carbamate pesticides - Whalen_2003_Chem.Biol.Interact_145_311
Author(s) : Whalen MM , Loganathan BG , Yamashita N , Saito T
Ref : Chemico-Biological Interactions , 145 :311 , 2003
Abstract : Triazine (atrazine) and carbamates (maneb, metiram, and ziram) are used as pesticides on a variety of crops around the world. To our knowledge, there have been no studies dealing with the effects of these compounds on human natural killer (NK) cells cytotoxic function. NK cells play a central role in immune defense against tumor development and viral infections. Thus, any agent that interferes with the ability of NK cells to lyse their targets could increase the risk of tumor incidence and/or viral infections. In this study, we examined the effects of atrazine, maneb, metiram, zineb, and ziram on the ability of human NK cells to lyse tumor cells. The compounds were tested in both purified NK cells as well as a cell preparation that contained both T and NK lymphocytes (T/NK cells). Lymphocytes were exposed to the compounds for periods of time ranging from 1 h to 6 days. Exposure of highly purified NK cells to 10 microM atrazine, maneb, or metiram inhibited K562 tumor cell lysis by 63+/-25, 95+/-4, and 50+/-6%, respectively, after a 24 h exposure and by 83+/-21, 70+/-39, and 48+/-41% after a 6-day exposure. Exposure to 2.5 microM ziram for 24 h caused a 99+/-2% decrease in lytic function and at 1 microM for 6 days caused a 96+/-4% decrease. However, when T/NK cells were exposed to atrazine, maneb, or metiram for 24 h only 10 microM atrazine and maneb caused a significant decreases in lytic function (61+/-13 and 38+/-18%) and after 6 days only atrazine was inhibitory (54+/-12%). A 24-h exposure to 2.5-microM ziram caused a 41+/-51% decrease in function, but a 6-day exposure to 1 microM ziram caused no inhibition of lytic function. The results provide evidence of relative toxic potential for the five compounds and the immunomodulatory effects on both T and NK lymphocyte function.
ESTHER : Whalen_2003_Chem.Biol.Interact_145_311
PubMedSearch : Whalen_2003_Chem.Biol.Interact_145_311
PubMedID: 12732457

Title : Identification of NDRG1 as an early inducible gene during in vitro maturation of cultured mast cells - Taketomi_2003_Biochem.Biophys.Res.Commun_306_339
Author(s) : Taketomi Y , Sugiki T , Saito T , Ishii S , Hisada M , Suzuki-Nishimura T , Uchida MK , Moon TC , Chang HW , Natori Y , Miyazawa S , Kikuchi-Yanoshita R , Murakami M , Kudo I
Ref : Biochemical & Biophysical Research Communications , 306 :339 , 2003
Abstract : Coculture of mouse bone marrow-derived mast cells (BMMC) with fibroblasts in the presence of stem cell factor (SCF) facilitates morphological and functional maturation toward a connective tissue mast cell (CTMC)-like phenotype. By means of cDNA subtraction, we identified several inducible genes during this mast cell maturation process. Of approximately 100 sequenced clones induced, nearly 50% were chromosome 14-associated serine proteases. Approximately 14% encoded NDRG1, a 43-kDa cytosolic protein that has been implicated in cell differentiation. NDRG1 was distributed in the cytosol of cultured mast cells and CTMC in rat skin. Overexpression of NDRG1 in RBL-2H3 cells resulted in enhanced degranulation in response to various stimuli. Thus, NDRG1 may be a mast cell maturation-associated inducible protein that allows the cells to be susceptible to extracellular stimuli leading to degranulation. Additionally, several unique maturation-associated inducible genes were identified, molecular and functional characterization of which will provide new insights into mast cell biology.
ESTHER : Taketomi_2003_Biochem.Biophys.Res.Commun_306_339
PubMedSearch : Taketomi_2003_Biochem.Biophys.Res.Commun_306_339
PubMedID: 12804568
Gene_locus related to this paper: human-NDRG1

Title : Contraction of isolated guinea-pig ileum by urotensin II via activation of ganglionic cholinergic neurons and acetylcholine release - Horie_2003_Neuropharmacol_45_1019
Author(s) : Horie S , Yasuda S , Tsurumaki Y , Someya A , Saito T , Okuma Y , Nomura Y , Hirabayashi T , Murayama T
Ref : Neuropharmacology , 45 :1019 , 2003
Abstract : Urotensin II and its receptor are expressed in the gastrointestinal tract of mice, but the effects of urotensin II on the gastrointestinal functions have not been established. In the present study, we investigated the effects of human urotensin II on a segment of the guinea-pig ileum. The addition of urotensin II induced contraction of the ileum in concentration-manner (-log EC(50) value was 8.13+/-0.21). The response by urotensin II was extracellular CaCl(2)-dependent and easily desensitized. Like nicotine, the contraction induced by 100 nM urotensin II was inhibited by treatment with atropine, hexamethonium, D-tubocurarine, tetrodotoxin or hemicholinium-3, and enhanced by physostigmine. Treatment with omega-conotoxin GVIA (an inhibitor of N-type Ca(2+) channels, 300 nM) inhibited 100 nM urotensin II- and 4 microM nicotine-, but not 3 microM acetylcholine-, induced contraction. Both urotensin II and nicotine stimulated [(3)H]choline release in a tetrodotoxin-sensitive manner from the prelabeled slices of the ileum. These findings suggest that urotensin II stimulated acetylcholine release from the ganglionic cholinergic neurons and thus stimulated contraction via muscarinic acetylcholine receptors in the guinea-pig ileum. Urotensin II receptor system in the myenteric neurons may regulate the gastrointestinal functions.
ESTHER : Horie_2003_Neuropharmacol_45_1019
PubMedSearch : Horie_2003_Neuropharmacol_45_1019
PubMedID: 14573394

Title : Cloning of an intracellular D(-)-3-hydroxybutyrate-oligomer hydrolase gene from Ralstonia eutropha H16 and identification of the active site serine residue by site-directed mutagenesis - Saegusa_2002_J.Biosci.Bioeng_94_106
Author(s) : Saegusa H , Shiraki M , Saito T
Ref : J Biosci Bioeng , 94 :106 , 2002
Abstract : An intracellular D(-)-3-hydroxybutyrate (3HB)-oligomer hydrolase gene from Ralstonia eutropha (formerly Alcaligenes eutrophus) H16 was cloned, sequenced, and characterized. As a hybridization probe to screen restriction digests of chromosomal DNA, an extracellular 3HB-oligomer hydrolase gene from Ralstonia pickettii strain (formerly Pseudomonas sp. strain) A1 was used. A specific hybridization signal was obtained and a 6.5-kbp SmaI fragment was cloned in an Escherichia coli phagemid vector. The crude extract from E. coli with this plasmid showed 3HB-trimer hydrolase activity. The subcloned 3.2-kbp fragment still showed 3HB-trimer hydrolase activity in E. coli and expressed an approximately 78-kDa protein in an in vitro transcription-translation system. Nucleotide sequence analysis of the 3.2-kbp fragment showed an open reading frame that encodes a polypeptide with a deduced molecular weight of 78,510. The putative amino acid sequence showed 54% identity with that of the oligomer hydrolase from R. pickettii A1. By site-directed mutagenesis, a novel amino acid sequence (S-V-S*-N-G) containing an essential serine residue in the catalytic center of the enzyme was determined. The gene product was found in PHB-rich cells of R. eutropha by immunodetection. The expressed 3HB-oligomer hydrolase localized both in the supernatant fraction and the PHB granules of the cells.
ESTHER : Saegusa_2002_J.Biosci.Bioeng_94_106
PubMedSearch : Saegusa_2002_J.Biosci.Bioeng_94_106
PubMedID: 16233278
Gene_locus related to this paper: cupnh-hboh

Title : Association of a G994 -->T missense mutation in the plasma platelet-activating factor acetylhydrolase gene with risk of abdominal aortic aneurysm in Japanese - Unno_2002_Ann.Surg_235_297
Author(s) : Unno N , Nakamura T , Mitsuoka H , Uchiyama T , Yamamoto N , Saito T , Sugatani J , Miwa M , Nakamura S
Ref : Annals of Surgery , 235 :297 , 2002
Abstract : OBJECTIVE: To investigate a possible association with plasma platelet activating factor acetylhydrolase (PAF-AH) gene mutation with the risk of abdominal aortic aneurysm (AAA). SUMMARY BACKGROUND DATA: Plasma platelet activating factor acetylhydrolase is known to catalyze platelet activating factor (PAF), thereby inactivating its inflammatory function. Deficiency of this enzyme is caused by a missense mutation (G994 -->T) in exon 9 of the plasma PAF-AH gene.
METHODS: We did a case-control study including 131 patients (median age 73.4 [range 50-84] years) and 106 controls matched for age and sex. Genomic DNA was analyzed for the mutant allele by a specific polymerase-chain reaction. Plasma PAF-AH activity was measured in both groups.
RESULTS: The frequency of the mutant allele (T allele) in the plasma PAF-AH gene in AAA patients was significantly higher than in control subjects. The association of the missense mutation with AAA was statistically significant and independent of other risk factors. Among AAA patients with normal genomic type, plasma PAF-AH activity was strongly correlated to the plasma concentration of low density lipoprotein cholesterol (LDL-C), while the correlation was not observed among AAA patients with heterozygotes genotype. Patients having AAA with both T allele and hyperlipidemia were more likely to have other atherosclerotic diseases such as ischemic heart disease, stroke and peripheral arterial occlusive diseases than patients with the normal genomic type and normal lipid level.
CONCLUSIONS: The genetic mutation of plasma PAF-AH gene appear to be an independent risk factor for AAA. Our findings need to be confirmed in a larger, prospective study including patients from different populations.
ESTHER : Unno_2002_Ann.Surg_235_297
PubMedSearch : Unno_2002_Ann.Surg_235_297
PubMedID: 11807372

Title : Cloning and sequencing of an intracellular D(-)-3-hydroxybutyrate oligomer hydrolase from Acidovorax sp. strain SA1 and purification of the enzyme - Sugiyama_2002_Curr.Microbiol_45_123
Author(s) : Sugiyama A , Shiraki M , Kobayashi T , Morikawa G , Yamamoto M , Yamaoka M , Saito T
Ref : Curr Microbiol , 45 :123 , 2002
Abstract : The gene of an intracellular D(-)-3-hydroxybutyrate oligomer hydrolase (i3HBOH) was cloned and sequenced from a poly(3-hydroxybutyrate) (PHB)-degrading bacterium, Acidovorax sp. strain SA1. The i3HBOH gene has 876 nucleotides corresponding to the deduced sequence of 292 amino acids. In this amino acid sequence, the general lipase box sequence (G-X(1)-S-X(2)-G) was found, whose serine residue was determined to the active sites serine by site-directed mutagenesis. An i3HBOH was purified to electrophoretical homogeneity from SA1. The molecular mass of the purified enzyme was estimated to be 32 kDa by SDS-PAGE. The N-terminal amino acid sequence of the purified enzyme corresponded to the deduced N-terminal amino acid sequence in the cloned i3HBOH gene. This is the first cloning and sequencing of an intracellular D(-)-3-hydroxybutyrate oligomer hydrolase gene to date.
ESTHER : Sugiyama_2002_Curr.Microbiol_45_123
PubMedSearch : Sugiyama_2002_Curr.Microbiol_45_123
PubMedID: 12070691

Title : Cloning of an intracellular Poly[D(-)-3-Hydroxybutyrate] depolymerase gene from Ralstonia eutropha H16 and characterization of the gene product - Saegusa_2001_J.Bacteriol_183_94
Author(s) : Saegusa H , Shiraki M , Kanai C , Saito T
Ref : Journal of Bacteriology , 183 :94 , 2001
Abstract : An intracellular poly[D(-)-3-hydroxybutyrate] (PHB) depolymerase gene (phaZ) has been cloned from Ralstonia eutropha H16 by the shotgun method, sequenced, and characterized. Nucleotide sequence analysis of a 2.3-kbp DNA fragment revealed an open reading frame of 1,260 bp, encoding a protein of 419 amino acids with a predicted molecular mass of 47,316 Da. The crude extract of Escherichia coli containing the PHB depolymerase gene digested artificial amorphous PHB granules and released mainly oligomeric D(-)-3-hydroxybutyrate, with some monomer. The gene product did not hydrolyze crystalline PHB or freeze-dried artificial amorphous PHB granules. The deduced amino acid sequence lacked sequence corresponding to a classical lipase box, Gly-X-Ser-X-Gly. The gene product was expressed in R. eutropha cells concomitant with the synthesis of PHB and localized in PHB granules. Although a mutant of R. eutropha whose phaZ gene was disrupted showed a higher PHB content compared to the wild type in a nutrient-rich medium, it accumulated PHB as much as the wild type did in a nitrogen-free, carbon-rich medium. These results indicate that the cloned phaZ gene encodes an intracellular PHB depolymerase in R. eutropha.
ESTHER : Saegusa_2001_J.Bacteriol_183_94
PubMedSearch : Saegusa_2001_J.Bacteriol_183_94
PubMedID: 11114905
Gene_locus related to this paper: alceu-PHAZRE

Title : The neuronal form of adaptor protein-3 is required for synaptic vesicle formation from endosomes - Blumstein_2001_J.Neurosci_21_8034
Author(s) : Blumstein J , Faundez V , Nakatsu F , Saito T , Ohno H , Kelly RB
Ref : Journal of Neuroscience , 21 :8034 , 2001
Abstract : Heterotetrameric adaptor complexes vesiculate donor membranes. One of the adaptor protein complexes, AP-3, is present in two forms; one form is expressed in all tissues of the body, whereas the other is restricted to brain. Mice lacking both the ubiquitous and neuronal forms of AP-3 exhibit neurological disorders that are not observed in mice that are mutant only in the ubiquitous form. To begin to understand the role of neuronal AP-3 in neurological disease, we investigated its function in in vitro assays as well as its localization in neural tissue. In the presence of GTPgammaS both ubiquitous and neuronal forms of AP-3 can bind to purified synaptic vesicles. However, only the neuronal form of AP-3 can produce synaptic vesicles from endosomes in vitro. We also identified that the expression of neuronal AP-3 is limited to varicosities of neuronal-like processes and is expressed in most axons of the brain. Although the AP-2/clathrin pathway is the major route of vesicle production and the relatively minor neuronal AP-3 pathway is not necessary for viability, the absence of the latter could lead to the neurological abnormalities seen in mice lacking the expression of AP-3 in brain. In this study we have identified the first brain-specific function for a neuronal adaptor complex.
ESTHER : Blumstein_2001_J.Neurosci_21_8034
PubMedSearch : Blumstein_2001_J.Neurosci_21_8034
PubMedID: 11588176

Title : Muscarinic acetylcholine receptors in the normal, developing and regenerating newt retinas - Cheon_2001_Brain.Res.Dev.Brain.Res_127_9
Author(s) : Cheon EW , Kuwata O , Saito T
Ref : Brain Research Developmental Brain Research , 127 :9 , 2001
Abstract : Immunoreactivity for m2 and m4 muscarinic acetylcholine receptors (mAChRs) was demonstrated in the adult newt retina. The m2 mAChR was localized to somata on either side of the inner plexiform layer (IPL), especially ganglion cells, and also distributed into two bands within the IPL. The distal band at a depth of 0-15% IPL co-localized with one of two choline acetyltransferase (ChAT) immunoreactive bands, while the proximal band at 85-100% depth did not overlap with either of the ChAT-ir bands. The m4 mAChR was localized to somata closely apposed to either side of the IPL, probably amacrine cell somata, and no immunoreactivity was detectable throughout the IPL. The time course of appearance of the m2 and m4 mAChRs was examined in both developing and regenerating retinas. Like acetylcholinesterase (AChE), the m2 was first detected in somata located at the most proximal level of the retina well before ChAT-ir cholinergic neurons appeared, while the m4 was detected at the time of appearance of ChAT, in both developing and regenerating retinas. When the outer plexiform layer (OPL) began to form, somata in the horizontal cell layer became transiently immunoreactive to the m2. The discrepancy in distribution of the m2 and ChAT in the IPL suggests that mAChR may play a role other than cholinergic neurotransmission. Furthermore, the similarity in time course of appearance of the m2 and m4, as well as other cholinergic system components [4], in both developing and regenerating retinas would suggest that the mechanisms that control neuronal differentiation during retinal development and regeneration are similar.
ESTHER : Cheon_2001_Brain.Res.Dev.Brain.Res_127_9
PubMedSearch : Cheon_2001_Brain.Res.Dev.Brain.Res_127_9
PubMedID: 11287060

Title : Functional annotation of a full-length mouse cDNA collection - Kawai_2001_Nature_409_685
Author(s) : Kawai J , Shinagawa A , Shibata K , Yoshino M , Itoh M , Ishii Y , Arakawa T , Hara A , Fukunishi Y , Konno H , Adachi J , Fukuda S , Aizawa K , Izawa M , Nishi K , Kiyosawa H , Kondo S , Yamanaka I , Saito T , Okazaki Y , Gojobori T , Bono H , Kasukawa T , Saito R , Kadota K , Matsuda H , Ashburner M , Batalov S , Casavant T , Fleischmann W , Gaasterland T , Gissi C , King B , Kochiwa H , Kuehl P , Lewis S , Matsuo Y , Nikaido I , Pesole G , Quackenbush J , Schriml LM , Staubli F , Suzuki R , Tomita M , Wagner L , Washio T , Sakai K , Okido T , Furuno M , Aono H , Baldarelli R , Barsh G , Blake J , Boffelli D , Bojunga N , Carninci P , de Bonaldo MF , Brownstein MJ , Bult C , Fletcher C , Fujita M , Gariboldi M , Gustincich S , Hill D , Hofmann M , Hume DA , Kamiya M , Lee NH , Lyons P , Marchionni L , Mashima J , Mazzarelli J , Mombaerts P , Nordone P , Ring B , Ringwald M , Rodriguez I , Sakamoto N , Sasaki H , Sato K , Schonbach C , Seya T , Shibata Y , Storch KF , Suzuki H , Toyo-oka K , Wang KH , Weitz C , Whittaker C , Wilming L , Wynshaw-Boris A , Yoshida K , Hasegawa Y , Kawaji H , Kohtsuki S , Hayashizaki Y
Ref : Nature , 409 :685 , 2001
Abstract : The RIKEN Mouse Gene Encyclopaedia Project, a systematic approach to determining the full coding potential of the mouse genome, involves collection and sequencing of full-length complementary DNAs and physical mapping of the corresponding genes to the mouse genome. We organized an international functional annotation meeting (FANTOM) to annotate the first 21,076 cDNAs to be analysed in this project. Here we describe the first RIKEN clone collection, which is one of the largest described for any organism. Analysis of these cDNAs extends known gene families and identifies new ones.
ESTHER : Kawai_2001_Nature_409_685
PubMedSearch : Kawai_2001_Nature_409_685
PubMedID: 11217851
Gene_locus related to this paper: mouse-1lipg , mouse-1plip , mouse-1plrp , mouse-ABH15 , mouse-abhd5 , mouse-ABHD6 , mouse-Abhd8 , mouse-aryla , mouse-bphl , mouse-cauxin , mouse-Ces1g , mouse-CPMac , mouse-dpp8 , mouse-EPHX1 , mouse-ES10 , mouse-hslip , mouse-hyes , mouse-ABHD2 , mouse-lcat , mouse-lipli , mouse-LIPN , mouse-lypla1 , mouse-lypla2 , mouse-OVCA2 , mouse-pafa , mouse-pcp , mouse-Ppgb , mouse-PPME1 , mouse-ppt , mouse-q3uuq7 , mouse-Q9DAI6 , mouse-Q80UX8 , mouse-RISC , mouse-SERHL , mouse-SPG21 , mouse-Tex30

Title : Efficient preparation of optically active ketoprofen by Mucor javanicus lipase immobilized on an inorganic support - Kato_2000_J.Biosci.Bioeng_90_332
Author(s) : Kato K , Gong Y , Saito T , Kimoto H
Ref : J Biosci Bioeng , 90 :332 , 2000
Abstract : Lipase M from Mucor javanicus, one of nine commercially available hydrolytic enzymes, showed good enantioselectivity (E=50) for racemic ketoprofen trifluoroethyl ester in phosphate buffer (pH 7.0) containing 30% acetone. Lipase M immobilized on Toyonite 200-A showed the best selectivity (E=55) and reactivity. Moreover, the lipase could be recycled at least 5 times.
ESTHER : Kato_2000_J.Biosci.Bioeng_90_332
PubMedSearch : Kato_2000_J.Biosci.Bioeng_90_332
PubMedID: 16232865

Title : Properties of a Poly(3-hydroxybutyrate) Depolymerase from Penicillium funiculosum - Miyazaki_2000_J.Polym.Environ_8_175
Author(s) : Miyazaki S , Takahashi K , Shiraki M , Saito T , Tezuka Y , Kasuya KI
Ref : J. Polym. Environ , 8 :175 , 2000
Abstract : A poly(3-hydroxybutyrate) (PHB) depolymerase was purified from a fungus, Penicillium funiculosum(IFO6345), with phenyl-Toyopearl and its properties were compared with those of other PHB depolymerases. The molecular mass of the purified enzyme was estimated at about 33 kDa by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The pH optimum and pI were 6.5 and 6.5, respectively. The purified protein showed affinity to Con A-Sepharose, indicating that it is a glycoprotein. Diisopropylfluorophosphate and dithiothreitol inhibited the depolymerase activity completely. The N-terminal amino acid sequence of the purified enzyme was TALPAFNVNPNSVS-VSGLSSGGYMAAQL, which contained a 'lipase box' sequence. This purified enzyme is one of the extracellular PHB depolymerase which belong to serine esterase. The purified enzyme showed relatively strong hydrolytic activity against 3-hydroxybutyrate oligomers compared with its PHB-degrading activity. PHB-binding experiments showed that P. funiculosum depolymerase has the weakest affinity for PHB of all the depolymerases examined.
ESTHER : Miyazaki_2000_J.Polym.Environ_8_175
PubMedSearch : Miyazaki_2000_J.Polym.Environ_8_175
Gene_locus related to this paper: penfu-PHAZ

Title : Biochemical and genetic characterization of an extracellular poly(3-hydroxybutyrate) depolymerase from Acidovorax sp strain TP4 - Kobayashi_1999_J.Environ.Polym.Degr_7_281
Author(s) : Kobayashi T , Sugiyama A , Kawase Y , Saito T , Mergaert J , Swings J
Ref : J Environ Polym Degr , 7 :9 , 1999
Abstract : To determine the properties of enzymes from bacteria that degrade polypropiolactone (PPL), we isolated 13 PPL-degrading bacteria from pond water, river water, and soil. Nine of these strains were identified as Acidovorax sp., three as Variovorax paradoxus, and one as Sphingomonas paucimobilis. All the isolates also degraded poly(3-hydroxybutyrate) (PHB). A PPL-degrading enzyme was purified to electrophoretical homogeneity from one of these bacteria, designated Acidovorax sp. TP4. The purified enzyme also degraded PHB. The molecular weight of the enzyme was estimated as about 50,000. The enzyme activity was inhibited by diisopropylfluorophosphate, dithiothreitol, and Triton X-100. The structural gene of the depolymerase was cloned in Escherichia coli. The nucleotide sequence of the cloned DNA fragment contained an open reading frame (1476 bp) specifying a protein with a deduced molecular weight of 50,961 (491 amino acids). The deduced overall sequence was very similar to that of a PHB depolymerase of Comamonas acidovorans YM1609. From these results it was concluded that the isolated PPL-degrading enzyme belongs to the class of PHB depolymerases. A conserved amino acid sequence, Gly-X1-Ser-X2-Gly (lipase box), was found at the N-terminal side of the amino acid sequence. Site-directed mutagenesis of the TP4 enzyme confirmed that 20Ser in the lipase box was essential for the enzyme activity. This is the first report of the isolation a PHB depolymerase from Acidovorax.
ESTHER : Kobayashi_1999_J.Environ.Polym.Degr_7_281
PubMedSearch : Kobayashi_1999_J.Environ.Polym.Degr_7_281
Gene_locus related to this paper: acisp-Q9ZNH8

Title : Choline acetyltransferase and acetylcholinesterase in the normal, developing and regenerating newt retinas - Cheon_1999_Brain.Res.Dev.Brain.Res_116_97
Author(s) : Cheon EW , Saito T
Ref : Brain Research Developmental Brain Research , 116 :97 , 1999
Abstract : The presence of the choline acetyltransferase (ChAT) and acetylcholinesterase (AChE) was demonstrated in the adult newt retina using immunocytochemical and histochemical techniques. Within the inner plexiform layer (IPL), two ChAT-positive bands were detected at relative depths of 0-15% and 45-60% of the total thickness (100%) of the IPL. AChE-positive band occupied approximately 0-60% of the IPL width with an intensive AChE-positive band at a depth of 20-40% within the IPL. Localizations of maximum ChAT and AChE activity were not exactly the same in the IPL of the mature retina. To elucidate whether retinal regeneration follows the same sequence of cellular differentiation steps that occur in retinal development, we examined the time course of appearance of the cholinergic neurons and AChE activity in both developing and regenerating retinas. The ChAT-positive cells were first detected in the retina just before or at the beginning of the morphological development of the IPL in both developing and regenerating retinas. AChE activity first became detectable in somata located at the most proximal layer of the retina before the ChAT-positive cells could be detected and well before the IPL developed in both developing and regenerating retinas. During subsequent development and regeneration, the outer plexiform layer, the IPL, and somata close to either side of the IPL became AChE-positive. The fact that the time course of the appearance of ChAT and AChE molecules during regeneration was similar to that observed during development suggests that common mechanisms may control both the development and the regeneration of the newt retina.
ESTHER : Cheon_1999_Brain.Res.Dev.Brain.Res_116_97
PubMedSearch : Cheon_1999_Brain.Res.Dev.Brain.Res_116_97
PubMedID: 10446351

Title : Structure and function of poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis T1 - Nojiri_1997_J.Bacteriol_179_6965
Author(s) : Nojiri M , Saito T
Ref : Journal of Bacteriology , 179 :6965 , 1997
Abstract : Poly(3-hydroxybutyrate) (PHB) depolymerase from Alcaligenes faecalis T1 is composed of three domains: the catalytic (C) domain, the fibronectin type III-like (F) domain, and the substrate-binding (S) domain. We constructed domain deletion, inversion, chimera, and extra-F-domain mutants and examined their enzyme activity and PHB-binding ability. In addition, we performed substitution of 214Asp and 273His with glycine and aspartate, respectively, to examine their participation in a catalytic triad together with 139Ser. The mutant with both the F and S domains deleted and the trypsin-digested enzyme showed no PHB-hydrolyzing activity and less PHB-binding ability than that of the wild-type enzyme but retained D-(-)-3-hydroxybutyrate trimer-hydrolyzing activity at a level similar to that of the wild-type enzyme. The mutant with the F domain deleted and the mutant which had the order of the F and S domains inverted retained PHB-binding ability and trimer-hydrolyzing activity at levels similar to those of the wild-type enzyme but lost PHB-hydrolyzing activity. The chimera mutant, in which the F domain was substituted with a Thr-rich domain of PHB depolymerase A from Pseudomonas lemoignei, and the extra-F-domain mutant, with an additional F domain, retained trimer- and PHB-hydrolyzing activities and PHB-binding ability at levels similar to those of the wild-type enzyme. Two mutants (D214G and H273D) showed no enzymatic activity toward trimer and PHB, and they were not labeled with [3H]diisopropylfluorophosphate.
ESTHER : Nojiri_1997_J.Bacteriol_179_6965
PubMedSearch : Nojiri_1997_J.Bacteriol_179_6965
PubMedID: 9371441

Title : Purification of an extracellular D-(-)-3-hydroxybutyrate oligomer hydrolase from Pseudomonas sp. strain A1 and cloning and sequencing of its gene - Zhang_1997_J.Bacteriol_179_72
Author(s) : Zhang K , Shiraki M , Saito T
Ref : Journal of Bacteriology , 179 :72 , 1997
Abstract : An extracellular D-(-)-3-hydroxybutyrate oligomer hydrolase was purified from a poly(3-hydroxybutyrate)-degrading bacterium, Pseudomonas sp. strain A1. The purified enzyme hydrolyzed the D-(-)-3-hydroxybutyrate dimer and trimer at similar rates. The enzyme activity was inhibited by a low concentration of diisopropylfluorophosphate. The molecular weight of the hydrolase was estimated to be about 70,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A 10-kbp DNA fragment of A1 was detected by hybridization with the gene (2 kbp) of an extracellular poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis. Subsequent subcloning showed that a SmaI-KpnI fragment (2.8 kbp) was responsible for expression of the hydrolase in Escherichia coli and an in vitro transcription-translation system. The expressed protein detected by immunostaining had the same molecular weight as the purified enzyme from A1. The protein band detected in the in vitro transcription-translation system had a molecular size of 72 kDa. The nucleotide sequence of the SmaI-KpnI fragment was determined, and one open reading frame (2,112 nucleotides) was found. It specifies a protein with a deduced molecular weight of 72,876 (704 amino acids). In this sequence, the consensus sequence of serine-dependent hydrolysis, G-X-S-X-G, did not exist.
ESTHER : Zhang_1997_J.Bacteriol_179_72
PubMedSearch : Zhang_1997_J.Bacteriol_179_72
PubMedID: 8981982

Title : Determination of the active sites serine of the poly (3-hydroxybutyrate) depolymerases of Pseudomonas lemoignei (PhaZ5) and of Alcaligenes faecalis - Shinohe_1996_FEMS.Microbiol.Lett_141_103
Author(s) : Shinohe T , Nojiri M , Saito T , Stanislawski T , Jendrossek D
Ref : FEMS Microbiology Letters , 141 :103 , 1996
Abstract : Mutational analysis of the poly(3-hydroxybutyrate) (PHB) depolymerase A of Pseudomonas lemoignei and of the poly(3-hydroxybutyrate) depolymerase of Alcaligenes faecalis revealed that S138 (P. lemoignei) and S139 (A. faecalis) are essential for activity. Both serines are part of a strictly conserved pentapeptide sequence which is present in all poly(3-hydroxybutyrate) depolymerases analyzed so far (G-L-S-S(A)-G) and which resembles the lipase box of lipases and other serine hydrolases (G-X-S-X-G). Mutation of another conserved serine, namely S195 (P. lemoignei) and S196 (A. faecalis), resulted in mutant proteins with almost full activity and proved that S195 and S196 are not essential for activity. The results indicate the structural and functional relationship of poly(3-hydroxybutyrate) depolymerases to the family of serine hydrolases.
ESTHER : Shinohe_1996_FEMS.Microbiol.Lett_141_103
PubMedSearch : Shinohe_1996_FEMS.Microbiol.Lett_141_103
PubMedID: 8764515

Title : Intracellular degradation of poly(3-hydroxybutyrate) granules of Zoogloea ramigera I-16-M - Saito_1992_FEMS.Microbiol.Rev_9_333
Author(s) : Saito T , Saegusa H , Miyata Y , Fukui T
Ref : FEMS Microbiology Reviews , 9 :333 , 1992
Abstract : Intracellular degradation of poly(3-hydroxybutyrate) (PHB) in bacteria is not yet clear. The properties of the autodigestion of native PHB granules from Zoogloea ramigera I-16-M were examined. The release of D(-)-3-hydroxybutyrate was observed only at pH values higher than about 8.5 and at relatively high ionic strength (optimal concentration 200 mM NaCl). Triton X-100 and diisopropylfluorophosphate inhibited this reaction. Addition of the supernatant fraction of Z. ramigera did not increase the release of D(-)-3-hydroxybutyrate from the native PHB granules. On the other hand, using the protease-treated PHB granules from Alcaligenes eutrophus as a substrate, PHB depolymerase activity was detected in the supernatant fraction of Z. ramigera cells. The soluble PHB depolymerase showed similar properties to the enzyme in the PHB granules. Since PHB depolymerase activity was found in fractions containing D(-)-3-hydroxybutyrate oligomer hydrolase activity, which were separated by DEAE-Toyopearl or by Sephacryl S-100, it is possible that the intracellular PHB depolymerase is identical to the oligomer hydrolase which has been purified already.
ESTHER : Saito_1992_FEMS.Microbiol.Rev_9_333
PubMedSearch : Saito_1992_FEMS.Microbiol.Rev_9_333
PubMedID: 1476778

Title : Cloning, nucleotide sequence, and expression in Escherichia coli of the gene for poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis - Saito_1989_J.Bacteriol_171_184
Author(s) : Saito T , Suzuki K , Yamamoto J , Fukui T , Miwa K , Tomita K , Nakanishi S , Odani S , Suzuki J , Ishikawa K
Ref : Journal of Bacteriology , 171 :184 , 1989
Abstract : The extracellular poly(3-hydroxybutyrate) depolymerase gene from Alcaligenes faecalis T1 was cloned into Escherichia coli DH1 by using the plasmid pUC8. An A. faecalis T1 genomic library was prepared in E. coli from a partial Sau3AI digest and screened with antibody against the depolymerase. Of the 29 antibody-positive clones, 1 (pDP14), containing about 4 kilobase pairs of A. faecalis T1 DNA, caused expression of a high level of depolymerase activity in E. coli. The enzyme purified from E. coli was not significantly different from the depolymerase of A. faecalis in molecular weight, immunological properties, peptide map, specific activity, or substrate specificity. Most of the expressed enzyme was found to be localized in the periplasmic space of E. coli, although about 10% of the total activity was found in the culture medium. Results of a deletion experiment with pDP14 showed that a large SalI fragment of about 2 kilobase pairs was responsible for expression of the enzyme in E. coli. The nucleotide sequence of the large SalI fragment has been determined. Comparison of the deduced amino terminus with that obtained from sequence analysis of the purified protein indicated that poly(3-hydroxybutyrate) depolymerase exists as a 488-amino-acid precursor with a signal peptide of 27 amino acids.
ESTHER : Saito_1989_J.Bacteriol_171_184
PubMedSearch : Saito_1989_J.Bacteriol_171_184
PubMedID: 2644188
Gene_locus related to this paper: alcfa-phb

Title : Differential effects of ethanol on the striatal and cortical adenylate cyclase system - Saito_1987_Jpn.J.Pharmacol_43_133
Author(s) : Saito T , Luthin GR , Lee JM , Hoffman PL , Tabakoff B
Ref : Japanese Journal of Pharmacology , 43 :133 , 1987
Abstract : In the present study, effects of ethanol (EtOH) on C57/BL mouse cortical beta-adrenergic receptor coupled adenylate cyclase (AC) were shown to be different from the effects of EtOH on striatal dopaminergic-stimulated AC activity. The addition of EtOH (500 mM) increased the AC activity by 60% in cortical membrane and by less than 10% in striatal membrane preparations in the absence of guanine nucleotide. The dose-response relationship for EtOH stimulation of cortical AC activity in the presence of guanylylimidodiphosphate (Gpp(NH)p) was biphasic, whereas, in the striatum, a linear dose-response relationship for EtOH was found for stimulation of AC in the presence of Gpp(NH)p. Activation of AC by Gpp(NH)p occurred as an apparent pseudo-first order process. EtOH increased the pseudo-first order rate constant for activation of AC by Gpp(NH)p in the cortex, but not in the striatum. Following 10 min preincubation with Gpp(NH)p, catecholamines and Gpp(NH)p were not able to stimulate further the AC activities in either tissue. Nevertheless, EtOH increased AC activity in both cortex and striatum following the preincubation with Gpp(NH)p. These data suggest that one effect of EtOH in striatal tissue is to promote the interaction of an activated guanine nucleotide-binding regulatory protein (G-protein) with the catalytic unit of AC. In cortical tissue, the effects of EtOH may be attributable to direct actions on the catalytic activity of the enzyme, effects on the rate of activation of the G-protein, and an altered interaction of G-protein with the catalytic unit.
ESTHER : Saito_1987_Jpn.J.Pharmacol_43_133
PubMedSearch : Saito_1987_Jpn.J.Pharmacol_43_133
PubMedID: 3573421

Title : Purification and properties of extracellular poly(3-hydroxybutyrate) depolymerases from Pseudomonas lemoignei - Nakayama_1985_Biochim.Biophys.Acta_827_63
Author(s) : Nakayama K , Saito T , Fukui T , Shirakura Y , Tomita K
Ref : Biochimica & Biophysica Acta , 827 :63 , 1985
Abstract : Extracellular poly(3-hydroxybutyrate) depolymerase was purified from the culture medium of Peudomonas lemoignei and separated into four isozymes (A1, A2, B1 and B2) by CM-Sepharose CL-6B chromatography. The molecular weights of A1 and A2 and those of B1 and B2 were estimated to be 54 000 and 58 000, respectively, by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The isoelectric points of A1, A2, B1 and B2 were found to be approximately pH 9.7, 10.0, 10.0 and 10.6, respectively, by isoelectric focusing. All four enzymes hydrolyzed poly(3-hydroxybutyrate) and oligomeric esters of D-(-)-3-hydroxybutyrate, but showed no activity toward the dimeric ester. Analysis of hydrolytic products of the oligomeric esters with A1 and B2 suggested that the enzymes hydrolyzed mainly the second and third ester bonds from the free hydroxy terminus at different frequencies, depending upon the chain length of the substrates.
ESTHER : Nakayama_1985_Biochim.Biophys.Acta_827_63
PubMedSearch : Nakayama_1985_Biochim.Biophys.Acta_827_63
PubMedID: 3967030

Title : Differential effects of ethanol on striatal and cortical adenylate cyclase -
Author(s) : Tabakoff B , Luthin GR , Saito T , Lee JM
Ref : Psychopharmacol Bull , 20 :481 , 1984
PubMedID: 6473652

Title : Purification and properties of D(-)-3-hydroxybutyrate-dimer hydrolase from Zoogloea ramigera I-16-M - Tanaka_1981_Eur.J.Biochem_118_177
Author(s) : Tanaka Y , Saito T , Fukui T , Tanio T , Tomita K
Ref : European Journal of Biochemistry , 118 :177 , 1981
Abstract : D(-)-3-Hydroxybutyrate-dimer hydrolase from Zoogloea ramigera I-16-M was purified 7000-fold to electrophoretic homogeneity. The molecular weight of the purified enzyme was 28 000 as determined by Sephadex G-100 gel filtration, and 30 000 as estimated by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The isoelectric point was at pH 5.7. The pH optimum for the enzyme reaction was 8.0. The dimer hydrolase was stereospecific for D(-)-3-[D(-)-3-hydroxybutyryloxy]butyric acid (DD-dimer) but also hydrolyzed D(-)-3-[L(+)-3-hydroxybutyryloxy]butyric acid (DL-dimmer) and L(+)-3-[D(-)-3-hydroxybutyryloxy]butyric acid (LD-dimer) at reduced rates. However, the enzyme did not attack L(+)-3-[L(+)-3-hydroxybutyryloxy]butyric acid (LL-dimer) at all. In addition, the purified hydrolase hydrolyzed several oligomeric esters of D(-)-3-hydroxybutyric acid (DDD-dimer, DDDD-tetramer and DDDDD-pentamer) faster than DD-dimer. Time course experiments with these oligomers and analysis of hydrolytic products of DDD-tetramer methyl ester with the hydrolase indicated that the enzyme attached these substrates from the free hydroxyl terminus releasing monomer units one at a time.
ESTHER : Tanaka_1981_Eur.J.Biochem_118_177
PubMedSearch : Tanaka_1981_Eur.J.Biochem_118_177
PubMedID: 7285912

Title : Substrate specificity of cholinesterases in mites -
Author(s) : Motoyama N , Saito T
Ref : Bochu-Kagaku , 33 :77 , 1968