Maeda M

References (15)

Title : Anti-Dementia Drug Persistence Following Donepezil Initiation Among Alzheimer's Disease Patients in Japan: LIFE Study - Fukuda_2022_J.Alzheimers.Dis__
Author(s) : Fukuda H , Maeda M , Murata F , Murata Y
Ref : J Alzheimers Dis , : , 2022
Abstract : BACKGROUND: Donepezil is frequently used to treat Alzheimer's disease (AD) symptoms but is associated with early discontinuation. Determining the persistence rates of anti-dementia drug use after donepezil initiation may inform the development and improvement of treatment strategies, but there is little evidence from Japan. OBJECTIVE: To determine anti-dementia drug persistence following donepezil initiation among AD patients in Japan using insurance claims data. METHODS: Insurance claims data for AD patients with newly prescribed donepezil were obtained from 17 municipalities between April 2014 and October 2021. Anti-dementia drug persistence was defined as a gap of >=60 days between the last donepezil prescription and a subsequent prescription of donepezil, another cholinesterase inhibitor, or memantine. Cox proportional hazards models were used to analyze the association between care needs levels and discontinuation. RESULTS: We analyzed 20,474 AD patients (mean age+/-standard deviation: 82.2+/-6.3 years, women: 65.7%). The persistence rates were 89.1% at 30 days, 79.4% at 90 days, 72.6% at 180 days, 64.5% at 360 days, and 58.3% at 540 days after initiation. Among the care needs levels, the hazard ratio (95% confidence interval) for discontinuation was 1.01 (0.94-1.07) for patients with support needs, 1.12 (1.06-1.18) for patients with low long-term care needs, and 1.31 (1.21-1.40) for patients with moderate-to-high long-term care needs relative to independent patients. CONCLUSION: Japanese AD patients demonstrated low anti-dementia drug persistence rates that were similar to those of other countries. Higher long-term care needs were associated with discontinuation. Further measures are needed to improve drug persistence in AD patients.
ESTHER : Fukuda_2022_J.Alzheimers.Dis__
PubMedSearch : Fukuda_2022_J.Alzheimers.Dis__
PubMedID: 36213993

Title : Directed evolution of poly[(R)-3-hydroxybutyrate] depolymerase using cell surface display system: functional importance of asparagine at position 285 - Tan_2013_Appl.Microbiol.Biotechnol_97_4859
Author(s) : Tan LT , Hiraishi T , Sudesh K , Maeda M
Ref : Applied Microbiology & Biotechnology , 97 :4859 , 2013
Abstract : Poly[(R)-3-hydroxybutyrate] (PHB) depolymerase from Ralstonia pickettii T1 (PhaZRpiT1) consists of three functional domains to effectively degrade solid PHB materials, and its catalytic domain catalyzes the ester bond cleavage of the substrate. We performed the directed evolution of PhaZRpiT1 targeted at the catalytic domain in combination with the cell surface display method to effectively screen for mutants with improved p-nitrophenyl butyrate (pNPC4) activity. Mutated PhaZRpiT1 genes generated by error-prone PCR were fused to the oprI gene to display them as fusion proteins on Escherichia coli cell surface. Some cells displaying the mutant enzymes showed a two- to fourfold increase in pNPC4 hydrolysis activity relative to cells displaying wild-type enzyme. These mutant genes were recombined by a staggered extension process and the recombined enzymes were displayed to result in a five- to eightfold higher pNPC4 hydrolysis activity than the wild type. To further evaluate the mutation effects, unfused and undisplayed enzymes were prepared and applied to the hydrolysis of p-nitrophenyl esters having different chain lengths (pNPCn; n=2-6) and PHB degradation. One specific second-generation mutant showed an approximately tenfold increase in maximum rate for pNPC3 hydrolysis, although its PHB degradation efficiency at 1 microg/mL of enzyme concentration was approximately 3.5-fold lower than that of the wild type. Gene analysis showed that N285D or N285Y mutations were found in six of the seven improved second-generation mutants, indicating that Asn285 probably participates in the regulation of substrate recognition and may be more favorable for PHB degradation process than other amino acid residues.
ESTHER : Tan_2013_Appl.Microbiol.Biotechnol_97_4859
PubMedSearch : Tan_2013_Appl.Microbiol.Biotechnol_97_4859
PubMedID: 22940802
Gene_locus related to this paper: alcfa-phb

Title : Display of functionally active PHB depolymerase on Escherichia coli cell surface - Hiraishi_2012_Macromol.Biosci_12_218
Author(s) : Hiraishi T , Yamashita K , Sakono M , Nakanishi J , Tan LT , Sudesh K , Abe H , Maeda M
Ref : Macromol Biosci , 12 :218 , 2012
Abstract : The display of PHB depolymerase (PhaZ(RpiT1) ) from R. pickettii T1 on the surface of E. coli JM109 cells is realized using OprI of P. aeruginosa as the anchoring motif. The fusion protein is stably expressed and its surface localization is verified by immunofluorescence microscopy. The displayed PhaZ(RpiT1) retains its cleaving ability for soluble substrates as well as its ability to adsorb to the PHB surface, and also remains catalycically active in the degradation of insoluble polyester materials, in spite of the possible suppression of the enzyme movement on the polymer surface. The results demonstrate that PhaZ(RpiT1) -displaying E. coli shows potential for use as a whole-cell biocatalyst for the production of (R)-3-hydroxybutyrate monomers from insoluble PHB materials.
ESTHER : Hiraishi_2012_Macromol.Biosci_12_218
PubMedSearch : Hiraishi_2012_Macromol.Biosci_12_218
PubMedID: 22095689

Title : Poly(aspartate) hydrolases: biochemical properties and applications - Hiraishi_2011_Appl.Microbiol.Biotechnol_91_895
Author(s) : Hiraishi T , Maeda M
Ref : Applied Microbiology & Biotechnology , 91 :895 , 2011
Abstract : Thermally synthesized poly(aspartate) (tPAA) shows potential for use in a wide variety of products and applications as a biodegradable replacement for non-biodegradable polycarboxylates, such as poly(acrylate). The tPAA molecule has unnatural structures, and the relationship between its biodegradability and structures has been investigated. Two tPAA-degrading bacteria, Sphingomonas sp. KT-1 and Pedobacter sp. KP-2, were isolated from river water; from them, two PAA-hydrolyzing enzymes, PAA hydrolases-1 and -2, were purified and biologically and genetically characterized. Interestingly, not only are PAA hydrolases-1 from those two strains novel in terms of structural genes and substrate specificities (they specifically cleave the amide bond between beta-aspartate units in tPAA), they also probably play a central role in tPAA biodegradation by both strains. In green polymer chemistry, one active area of research is the use of purified enzymes for the enzyme-catalyzed synthesis of polypeptides by taking advantage of their substrate specificities. Recently, beta-peptides have attracted academic and industrial interest as functional materials as they possess both functions of alpha-peptides and excellent metabolic stability. As one of the attractive applications of PAA hydrolases, we report here the enzyme-catalyzed synthesis of poly(alpha-ethyl beta-aspartate), which is composed of only beta-linkages and belongs to beta-peptides, using the unique substrate specificity of the enzyme from Pedobacter sp. KP-2.
ESTHER : Hiraishi_2011_Appl.Microbiol.Biotechnol_91_895
PubMedSearch : Hiraishi_2011_Appl.Microbiol.Biotechnol_91_895
PubMedID: 21713512

Title : Cloning of poly(aspartic acid) (PAA) hydrolase-1 gene from Pedobacter sp. KP-2 and hydrolysis of thermally synthesized PAA by its gene product - Hiraishi_2009_Macromol.Biosci_9_10
Author(s) : Hiraishi T , Masuda E , Kanayama N , Nagata M , Doi Y , Abe H , Maeda M
Ref : Macromol Biosci , 9 :10 , 2009
Abstract : Pedobacter sp. KP-2 can degrade and metabolize thermally synthesized alpha,beta-poly(D,L-aspartic acid) (tPAA), which contains 70% of unnatural beta-amide units, with high-molecular-weight. In this study, gene cloning and molecular characterization of PAA hydrolase-1 from KP-2 was carried out. Gene analysis reveals that deduced amino acid sequence of the enzyme shows a similarity to only that of PAA hydrolase-1 from Sphingomonas sp. KT-1. GPC and NMR analyses of the hydrolyzed products of tPAA by PAA hydrolase-1 of KP-2 indicate that this enzyme cleaves the beta-beta amide linkage via endo-mode to yield oligo(aspartic acid) from tPAA. Taking the composition of tPAA and the substrate specificity of PAA hydrolase-1 into consideration, the enzyme possibly plays a crucial role in tPAA biodegradation by KP-2.
ESTHER : Hiraishi_2009_Macromol.Biosci_9_10
PubMedSearch : Hiraishi_2009_Macromol.Biosci_9_10
PubMedID: 18756460
Gene_locus related to this paper: 9sphi-b6vqa9

Title : Regulation of human extravillous trophoblast function by membrane-bound peptidases - Fujiwara_2005_Biochim.Biophys.Acta_1751_26
Author(s) : Fujiwara H , Higuchi T , Sato Y , Nishioka Y , Zeng BX , Yoshioka S , Tatsumi K , Ueda M , Maeda M
Ref : Biochimica & Biophysica Acta , 1751 :26 , 2005
Abstract : During human placentation, the invasion of extravillous trophoblasts (EVTs) into maternal decidual tissues, especially toward maternal spiral arteries, is considered an essential process for subsequent normal fetal development. However, the precise regulatory mechanisms to induce EVT invasion toward arteries and/or to protect EVTs from further invasion have not been well understood. Recently, we found that two cell surface peptidases, dipeptidyl peptidase IV (DPPIV) and carboxypeptidase-M (CP-M,) are differentially expressed on EVTs. DPPIV expression was mainly observed on EVTs that had already ceased invasion. CP-M was detected on migrating EVTs including endovascular trophoblasts in the maternal arteries. The enzymatic inhibition of these peptidases affected the invasive property of choriocarcinoma-derived cell lines, BeWo and JEG3 cells. In addition, a chemokine, RANTES, that is one of the substrates for DPPIV, enhanced invasion of EVTs isolated from primary villous explant culture and its receptor, CCR1, was specifically expressed on migrating EVTs toward maternal arteries. Furthermore, a novel membrane-bound cell surface peptidase, named laeverin, was found to be specifically expressed on EVTs that had almost ceased invasion. These findings suggest that membrane-bound peptidases are important factors regulating EVT invasion during early placentation in humans.
ESTHER : Fujiwara_2005_Biochim.Biophys.Acta_1751_26
PubMedSearch : Fujiwara_2005_Biochim.Biophys.Acta_1751_26
PubMedID: 15897020

Title : Vesicular acetylcholine transporter can be a morphological marker for the reinnervation to muscle of regenerating motor axons - Maeda_2004_Neurosci.Res_48_305
Author(s) : Maeda M , Ohba N , Nakagomi S , Suzuki Y , Kiryu-Seo S , Namikawa K , Kondoh W , Tanaka A , Kiyama H
Ref : Neurosci Res , 48 :305 , 2004
Abstract : This study was designed to evaluate whether the vesicular acetylcholine transporter (VAChT), which packages acetylcholine into synaptic vesicles, can be used as a marker for regenerating motor axon terminal. We examined motor axon regeneration in the tongue after hypoglossal nerve axotomy, using an anterograde tracer biotin-dextran (BD), retrograde tracer Fluoro-Gold (FG), electron microscopic (EM) observation, and VAChT immunocytochemistry. BD study demonstrated that outgrowth of thin regenerating axons into the frontal area of the tongue was firstly observed at 14 post-operative days, and presynaptic formation of neuromuscular junction (NMJ) was observed from 21 post-operative days. Under electron microscopic observation, reconstruction of new NMJs was observed within the interval between 21 and 28 days. VAChT-immunoreactive nerve terminals disappeared by 3 days after axotomy, slightly appeared at 14 post-operative days, and thereafter gradually increased in number from 21 to 28 post-operative days. The re-expression of VAChT positive presynaptic terminal was almost the same as those obtained in BD, FG and EM studies. Regenerating axons tip in the crush model of the hypoglossal nerve exhibited prominent VAChT immunoreactivity in growing tip of regenerating axons. These indicate that VAChT is an excellent morphological indicator for regenerating nerve terminals of motor neurons.
ESTHER : Maeda_2004_Neurosci.Res_48_305
PubMedSearch : Maeda_2004_Neurosci.Res_48_305
PubMedID: 15154676

Title : Skeletal muscle regeneration associated with the stroma reaction during tumor invasion in the rat tongue - Ohba_2002_J.Submicrosc.Cytol.Pathol_34_367
Author(s) : Ohba N , Maeda M , Sakamoto H , Kiyama H , Ishii M , Muraoka M , Kaneda K
Ref : J Submicrosc Cytol Pathol , 34 :367 , 2002
Abstract : This study was aimed to demonstrate the regeneration of skeletal muscle fibers in the stroma reaction during tumor invasion, using the rat model of tongue carcinoma. By oral administration of 4-nitroquinoline N-oxide, squamous cell carcinoma (SCC) appeared in the epithelium, and deeply invaded the muscular layer, inducing the stroma reaction around the tumor. Regenerating muscle fibers, characterized by the immature profiles of sparse myofibrils, centrally disposed multi-nuclei, and abundant mitochondria, were extended from the surrounding normal muscles into the stroma. By immunohistochemistry, some of them expressed BF-45, a marker for an early stage of myodifferentiation, similar to the regenerating muscle fibers in the bupivacaine hydrochloride-induced injury. They were closely associated with the stromal components such as ED-1-positive macrophages, alpha-smooth muscle actin-positive myofibroblasts, and factor VIII-related antigen-positive vascular endothelial cells, suggesting the roles of their interactions in muscle regeneration. Immature muscle fibers were usually devoid of acetylcholinesterase-positive endplates on them, but some were reinnervated by the terminal axons. The present results indicate that skeletal muscle regeneration is induced in association with the stroma reaction during SCC invasion in the tongue.
ESTHER : Ohba_2002_J.Submicrosc.Cytol.Pathol_34_367
PubMedSearch : Ohba_2002_J.Submicrosc.Cytol.Pathol_34_367
PubMedID: 12575835

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

Title : Pseudomonas putida CE2010 can degrade biphenyl by a mosaic pathway encoded by the tod operon and cmtE, which are identical to those of P. putida F1 except for a single base difference in the operator-promoter region of the cmt operon - Ohta_2001_Microbiology_147_31
Author(s) : Ohta Y , Maeda M , Kudo T
Ref : Microbiology , 147 :31 , 2001
Abstract : Psudomonas putida CE2010 can assimilate biphenyl despite its high similarity to P. putida F1. Biphenyl degradation in strain CE2010 was achieved using a mosaic of pathways consisting of the cmt and tod operons. CmtE hydrolysed 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, the meta-cleavage product of 2,3-dihydroxybiphenyl. This enzyme was expressed differently in strains CE2010 and F1. A cmtE disruption mutant, a tod operon disruption mutant and a cmt operon disruption mutant were unable to utilize biphenyl. The introduction of the cmtE gene enabled the cmt operon disruption mutant to grow on biphenyl. A single base difference was found in the cmt promoter-operator region in strain CE2010, compared with that of strain F1. CymR protein was purified from Escherichia coli and binding assays were performed, the results of which suggested that the protein bound less strongly to the CE2010 operator sequence than to the F1 operator sequence. Exchanging the F1 promoter-operator fragment into strain CE2010 resulted in a loss of biphenyl degradation capacity. These results indicate that cmtE is not effectively repressed by CymR in strain CE2010, leading to low constitutive expression and, therefore, low growth on biphenyl.
ESTHER : Ohta_2001_Microbiology_147_31
PubMedSearch : Ohta_2001_Microbiology_147_31
PubMedID: 11160798
Gene_locus related to this paper: psepu-todf

Title : Epoxide hydrolase affects estrogen production in the human ovary - Hattori_2000_Endocrinology_141_3353
Author(s) : Hattori N , Fujiwara H , Maeda M , Fujii S , Ueda M
Ref : Endocrinology , 141 :3353 , 2000
Abstract : To investigate the mechanisms of ovarian cell differentiation, we raised a new monoclonal antibody, HCL-3, which reacted with human luteal cells. It also reacted with human and porcine hepatocytes. The immunoaffinity-purified HCL-3 antigen from human corpora lutea (CL) was shown to be a 46-kDa protein. The N-terminal 22 amino acids of the 46-kDa protein from porcine liver exhibited high homology (82%) to human microsomal epoxide hydrolase (mEH). The purified HCL-3 antigen from human CL or porcine liver showed EH enzyme activity, confirming that HCL-3 antigen is identical to mEH, which is reported to detoxify the toxic substrates in the liver. In human follicles, mEH was immunohistochemically detected on granulosa and theca interna cells. In the menstrual and pregnant CL, mEH was also expressed on large and small luteal cells. A competitive inhibitor of EH, 1,2-epoxy-3,3,3-trichloropropane, inhibited the conversion of estradiol from testosterone by granulosa cells cultured in vitro, indicating the involvement of mEH in ovarian estrogen production. Because anticonvulsant sodium valproate and its analogues were reported to inhibit EH enzyme activity, these findings provide a new insight into the etiology of endocrine disorders that are frequently observed among epileptic patients taking anticonvulsant drugs.
ESTHER : Hattori_2000_Endocrinology_141_3353
PubMedSearch : Hattori_2000_Endocrinology_141_3353
PubMedID: 10965908

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

Title : Airway responsiveness to acetylcholine in congenitally bronchial- hypersensitive (BHS) and bronchial-hyposensitive (BHR) guinea pigs in vivo and in vitro - Yagi_1998_Exp.Anim_47_173
Author(s) : Yagi Y , Kuwahara M , Maeda M , Kadota H , Saegusa S , Birumachi J , Sugano S , Nishibata R , Mikami H , Tsubone H
Ref : Exp Anim , 47 :173 , 1998
Abstract : The characteristics of airway responsiveness to acetylcholine (ACh) in congenitally bronchial-hypersensitive (BHS) and bronchial-hyposensitive (BHR) guinea pigs were clarified in vivo and in vitro. We measured the change in ventilatory mechanics in response to ACh inhalation by means of the bodyplethysmograph and the contractile responses of isolated trachea to ACh and carbachol (CCh). Further, muscarinic receptor subtypes involved these responses were identified. The basal values for ventilatory mechanics in BHS were not significantly different from those in BHR. Respiratory resistance to ACh was progressively increased in a time- and dose-dependent manner in BHS. The contractile responses of tracheal smooth muscle to ACh in BHS were significantly greater than those in BHR, but CCh-induced responses in BHS and BHR were similar. ACh- and CCh-induced contractions were mediated via M3 receptors. These results suggested that the falling-down of BHS in response to ACh inhalation was caused by the strong constriction of the airway and the reduction in ventilation. Moreover, the airway hyperresponsiveness to ACh in BHS might be partly dependent on the change in acetylcholinesterase activity.
ESTHER : Yagi_1998_Exp.Anim_47_173
PubMedSearch : Yagi_1998_Exp.Anim_47_173
PubMedID: 9816493

Title : Three of the seven bphC genes of Rhodococcus erythropolis TA421, isolated from a termite ecosystem, are located on an indigenous plasmid associated with biphenyl degradation - Kosono_1997_Appl.Environ.Microbiol_63_3282
Author(s) : Kosono S , Maeda M , Fuji F , Arai H , Kudo T
Ref : Applied Environmental Microbiology , 63 :3282 , 1997
Abstract : Rhodococcus erythropolis TA421, a polychlorinated biphenyl and biphenyl degrader isolated from a termite ecosystem, has seven bphC genes expressing 2,3-dihydroxybiphenyl dioxygenase activity. R. erythropolis TA421 harbored a large and probably linear plasmid on which three (bphC2, bphC3, and bphC4) of the seven bphC genes were located. A non-biphenyl-degrading mutant, designated strain TA422, was obtained spontaneously from R. erythropolis TA421. TA422 lacked the plasmid, suggesting that the three bphC genes were involved in the degradation of biphenyl. Southern blot analyses showed that R. erythropolis TA421 and Rhodococcus globerulus P6 have a similar set of bphC genes and that the genes for biphenyl catabolism are located on plasmids of different sizes. These results indicated that the genes encoding the biphenyl catabolic pathway in Rhodococcus strains are borne on plasmids.
ESTHER : Kosono_1997_Appl.Environ.Microbiol_63_3282
PubMedSearch : Kosono_1997_Appl.Environ.Microbiol_63_3282
PubMedID: 9251216
Gene_locus related to this paper: rhoer-bphD2

Title : A novel recombinant tumor necrosis factor-alpha mutant with increased anti-tumor activity and lower toxicity - Nakamura_1991_Int.J.Cancer_48_744
Author(s) : Nakamura S , Kato A , Masegi T , Fukuoka M , Kitai K , Ogawa H , Ichikawa Y , Maeda M , Watanabe N , Kohgo Y , et al.
Ref : International Journal of Cancer , 48 :744 , 1991
Abstract : We prepared a novel recombinant tumor necrosis factor-alpha (TNF) mutant (mutant 471), in which 7 N-terminal amino-acids were deleted and Pro8Ser9Asp10 was replaced by ArgLysArg, and compared its biological activity with that of wild-type recombinant TNF. Mutant 471 had a 7-fold higher anti-tumor activity against murine L-M cells in vitro, and a higher binding activity to TNF receptors on L-M cells, than wild-type TNF. Furthermore, mutant 471 showed a higher anti-tumor effect on murine Meth A-HM tumors transplanted into BALB/c mice, with complete regression of the tumors being observed in the animals. The possible cachectin activity of mutant 471 was almost the same as that of wild-type TNF. The acute lethal toxicity of mutant 471 in beta-D-galactosamine-sensitized C3H/HeJ mice was 18 times lower than that of wild-type TNF. These results suggest that mutant 471 might be a more promising anti-cancer agent than wild-type TNF.
ESTHER : Nakamura_1991_Int.J.Cancer_48_744
PubMedSearch : Nakamura_1991_Int.J.Cancer_48_744
PubMedID: 1649139