Tashiro K

References (8)

Title : In vitro deacetylation of N-acetylserotonin by arylacetamide deacetylase - Huang_2023_J.Pineal.Res_75_e12870
Author(s) : Huang Z , Li Y , Konishi K , Sakai Y , Tashiro K , Fukami T , Borjigin J
Ref : J Pineal Res , 75 :e12870 , 2023
Abstract : Arylacetamide deacetylase (AADAC) is a deacetylation enzyme present in the mammalian liver, gastrointestinal tract, and brain. During our search for mammalian enzymes capable of metabolizing N-acetylserotonin (NAS), AADAC was identified as having the ability to convert NAS to serotonin. Both human and rodent recombinant AADAC proteins can deacetylate NAS in vitro, although the human AADAC shows markedly higher activity compared with rodent enzyme. The AADAC-mediated deacetylation reaction can be potently inhibited by eserine in vitro. In addition to NAS, recombinant hAADAC can deacetylate melatonin (to form 5-methoxytryptamine) and N-acetyltryptamine (NAT) (to form tryptamine). In addition to the in vitro deacetylation of NAS by the recombinant AADAC proteins, liver (mouse and human) and brain (human) extracts were able to deacetylate NAS; these activities were sensitive to eserine. Taken together, these results demonstrate a new role for AADAC and suggest a novel pathway for the AADAC-mediated metabolism of pineal indoles in mammals.
ESTHER : Huang_2023_J.Pineal.Res_75_e12870
PubMedSearch : Huang_2023_J.Pineal.Res_75_e12870
PubMedID: 37002641

Title : Arylacetamide deacetylase knockout mice are sensitive to ketoconazole-induced hepatotoxicity and adrenal insufficiency - Nagaoka_2022_Biochem.Pharmacol_195_114842
Author(s) : Nagaoka M , Fukami T , Kisui F , Yamada T , Sakai Y , Tashiro K , Ogiso T , Konishi K , Honda S , Hirosawa K , Nakano M , Nakajima M
Ref : Biochemical Pharmacology , 195 :114842 , 2022
Abstract : Orally administered ketoconazole may rarely induce liver injury and adrenal insufficiency. A metabolite formed by arylacetamide deacetylase (AADAC)-mediated hydrolysis has been observed in cellulo studies, and it is relevant to ketoconazole-induced cytotoxicity. This study tried to examine the significance of AADAC in ketoconazole-induced toxicity in vivo using Aadac knockout mice. Oral administration of 150 mg/kg ketoconazole resulted in the area under the plasma concentration-time curve values of ketoconazole and N-deacetylketoconazole, a hydrolyzed metabolite of ketoconazole, in Aadac knockout mice being significantly higher and lower than those in wild-type mice, respectively. With the administration of ketoconazole (300 mg/kg/day) for 7 days, Aadac knockout mice showed higher mortality (100%) than wild-type mice (42.9%), and they also showed significantly higher plasma alanine transaminase and lower corticosterone levels, thus representing liver injury and steroidogenesis inhibition, respectively. It was suggested that a higher plasma ketoconazole concentration likely accounts for the inhibition of the synthesis of corticosterone, which has anti-inflammatory effects, in the adrenal gland in Aadac KO mice. In Aadac knockout mice, hepatic mRNA levels of immune- and inflammation-related factors were increased by the administration of 300 mg/kg ketoconazole, and the increase was restored by the replenishment of corticosterone (40 mg/kg, s.c.) along with recoveries of plasma alanine transaminase levels. In conclusion, Aadac defects exacerbate ketoconazole-induced liver injury by inhibiting glucocorticoid synthesis and enhancing the inflammatory response. This in vivo study revealed that the hydrolysis of ketoconazole by AADAC can mitigate ketoconazole-induced toxicities.
ESTHER : Nagaoka_2022_Biochem.Pharmacol_195_114842
PubMedSearch : Nagaoka_2022_Biochem.Pharmacol_195_114842
PubMedID: 34798123
Gene_locus related to this paper: mouse-aryla

Title : Role of human AADAC on hydrolysis of eslicarbazepine acetate and effects of AADAC genetic polymorphisms on hydrolase activity - Hirosawa_2021_Drug.Metab.Dispos__
Author(s) : Hirosawa K , Fukami T , Tashiro K , Sakai Y , Kisui F , Nakano M , Nakajima M
Ref : Drug Metabolism & Disposition: The Biological Fate of Chemicals , : , 2021
Abstract : Human arylacetamide deacetylase (AADAC) plays a role in the detoxification or activation of drugs and is sometimes involved in the incidence of toxicity by catalyzing hydrolysis reactions. AADAC prefers compounds with relatively small acyl groups, such as acetyl groups. Eslicarbazepine acetate, an antiepileptic drug, is a prodrug rapidly hydrolyzed to eslicarbazepine. We sought to clarify whether AADAC might be responsible for the hydrolysis of eslicarbazepine acetate. Eslicarbazepine acetate was efficiently hydrolyzed by human intestinal and liver microsomes and recombinant human AADAC. The hydrolase activities in human intestinal and liver microsomes were inhibited by epigallocatechin gallate, a specific inhibitor of AADAC, by 82% and 88% of the control, respectively. The hydrolase activities in liver microsomes from 25 human livers were significantly correlated (r = 0.87, P < 0.001) with AADAC protein levels, suggesting that the enzyme AADAC is responsible for the hydrolysis of eslicarbazepine acetate. The effects of genetic polymorphisms of AADAC on eslicarbazepine acetate hydrolysis were examined by using the constructed recombinant AADAC variants with T74A, V172I, R248S, V281I, N366K, or X400Q. AADAC variants with R248S or X400Q showed lower activity than wild type (5% or 21%, respectively), whereas those with V172I showed higher activity than wild type (174%). Similar tendencies were observed in the other 4 substrates of AADAC; that is, p-nitrophenyl acetate, ketoconazole, phenacetin, and rifampicin. Collectively, we found that eslicarbazepine acetate is specifically and efficiently hydrolyzed by human AADAC, and several AADAC polymorphic alleles would be a factor affecting the enzyme activity and drug response. Significance Statement This is the first study to clarify that AADAC is responsible for the activation of eslicarbazepine acetate, an antiepileptic prodrug, to eslicarbazepine, an active form, in the human liver and intestines. In addition, we found that several AADAC polymorphic alleles would be a factor affecting the enzyme activity and drug response.
ESTHER : Hirosawa_2021_Drug.Metab.Dispos__
PubMedSearch : Hirosawa_2021_Drug.Metab.Dispos__
PubMedID: 33446525
Gene_locus related to this paper: human-AADAC

Title : Draft Genome Sequence of Thiostrepton-Producing Streptomyces azureus ATCC 14921 - Sakihara_2015_Genome.Announc_3_e01183
Author(s) : Sakihara K , Maeda J , Tashiro K , Fujino Y , Kuhara S , Ohshima T , Ogata S , Doi K
Ref : Genome Announc , 3 : , 2015
Abstract : Streptomyces azureus ATCC 14921 belongs to the Streptomyces cyaneus cluster and is known to be a thiostrepton producer. Here, we report a draft genome sequence for this strain, consisting of 350 contigs containing a total of 8,790,525 bp, 8,164 predicted coding sequences, and a G+C content of 70.9%.
ESTHER : Sakihara_2015_Genome.Announc_3_e01183
PubMedSearch : Sakihara_2015_Genome.Announc_3_e01183
PubMedID: 26494661
Gene_locus related to this paper: straj-a0a0k8pgz2 , straj-a0a0k8pxt3

Title : Draft Genome Sequence of Entomopathogenic Serratia liquefaciens Strain FK01 - Taira_2014_Genome.Announc_2_e00609
Author(s) : Taira E , Iiyama K , Mon H , Mori K , Akasaka T , Tashiro K , Yasunaga-Aoki C , Lee JM , Kusakabe T
Ref : Genome Announc , 2 : , 2014
Abstract : In the present study, we determined the draft genome sequence of the entomopathogenic bacterium Serratia liquefaciens FK01, which is highly virulent to the silkworm. The draft genome is ~5.28 Mb in size, and the G+C content is 55.8%.
ESTHER : Taira_2014_Genome.Announc_2_e00609
PubMedSearch : Taira_2014_Genome.Announc_2_e00609
PubMedID: 24970828

Title : Draft Genome Sequence of D-Branched-Chain Amino Acid Producer Lactobacillus otakiensis JCM 15040T, Isolated from a Traditional Japanese Pickle - Doi_2013_Genome.Announc_1_e00546
Author(s) : Doi K , Mori K , Mutaguchi Y , Tashiro K , Fujino Y , Ohmori T , Kuhara S , Ohshima T
Ref : Genome Announc , 1 : , 2013
Abstract : Lactobacillus otakiensis strain JCM 15040(T) was isolated from an unsalted pickling solution used in the production of sunki, a traditional Japanese pickle. Here, we prepared a draft genome sequence for this strain consisting of 40 contigs containing a total of 2,347,132 bp, 2,310 predicted coding sequences, and a G+C content of 42.4%.
ESTHER : Doi_2013_Genome.Announc_1_e00546
PubMedSearch : Doi_2013_Genome.Announc_1_e00546
PubMedID: 23929467
Gene_locus related to this paper: 9laco-s4nei2

Title : Draft Genome Sequence of Geobacillus kaustophilus GBlys, a Lysogenic Strain with Bacteriophage OH2 - Doi_2013_Genome.Announc_1_e00634
Author(s) : Doi K , Mori K , Martono H , Nagayoshi Y , Fujino Y , Tashiro K , Kuhara S , Ohshima T
Ref : Genome Announc , 1 :e00634 , 2013
Abstract : Geobacillus kaustophilus strain GBlys was isolated along with the bacteriophage OH2, which infects G. kaustophilus NBRC 102445(T). Here we present a draft sequence of this strain's genome, which consists of 216 contigs for a total of 3,541,481 bp, 3,679 predicted coding sequences, and a G+C content of 52.1%.
ESTHER : Doi_2013_Genome.Announc_1_e00634
PubMedSearch : Doi_2013_Genome.Announc_1_e00634
PubMedID: 23950135
Gene_locus related to this paper: bac25-mglp , geoka-q5kvf2 , geoka-q5l3h0 , geotn-a4isp0

Title : Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used for brewing the Japanese distilled spirit shochu - Futagami_2011_Eukaryot.Cell_10_1586
Author(s) : Futagami T , Mori K , Yamashita A , Wada S , Kajiwara Y , Takashita H , Omori T , Takegawa K , Tashiro K , Kuhara S , Goto M
Ref : Eukaryot Cell , 10 :1586 , 2011
Abstract : The filamentous fungus Aspergillus kawachii has traditionally been used for brewing the Japanese distilled spirit shochu. A. kawachii characteristically hyperproduces citric acid and a variety of polysaccharide glycoside hydrolases. Here the genome sequence of A. kawachii IFO 4308 was determined and annotated. Analysis of the sequence may provide insight into the properties of this fungus that make it superior for use in shochu production, leading to the further development of A. kawachii for industrial applications.
ESTHER : Futagami_2011_Eukaryot.Cell_10_1586
PubMedSearch : Futagami_2011_Eukaryot.Cell_10_1586
PubMedID: 22045919
Gene_locus related to this paper: aspaw-AXE1 , aspkw-g7x761 , aspkw-g7xcc9 , aspkw-g7xum1 , aspkw-g7xy77 , aspna-g3yal2 , aspnc-a2qe77 , aspnc-a2qf54 , aspnc-a2qfe9 , aspnc-a2qh76 , aspnc-a2qhe2 , aspnc-a2qi32 , aspnc-a2ql89 , aspnc-a2ql90 , aspnc-a2qla0 , aspnc-a2qmk5 , aspnc-a2qn56 , aspnc-a2qs22 , aspnc-a2qti9 , aspnc-a2qtz0 , aspnc-a2quc1 , aspnc-a2qx92 , aspnc-a2qyf0 , aspnc-a2qys7 , aspnc-a2qz72 , aspnc-a2qzn6 , aspnc-a2qzr0 , aspnc-a2qzx4 , aspnc-a2r0p4 , aspnc-a2r1r5 , aspnc-a2r2i5 , aspnc-a2r5r4 , aspnc-a2r8r3 , aspnc-a2r8z3 , aspnc-a2r273 , aspnc-a2r496 , aspnc-a2r502 , aspnc-a5abe5 , aspnc-a5abe8 , aspnc-a5abh9 , aspnc-a5abk1 , aspnc-cuti2 , aspng-a2qst4 , aspni-EstA , aspkw-g7y0v7 , aspnc-a2qt47 , aspkw-g7xj51 , aspkw-g7xru4 , aspkw-g7xr60 , aspna-g3y5a6 , 9euro-a0a146f3d2 , aspkw-g7xq95 , aspkw-g7xzf8 , asptc-a0a1l9nby7 , aspkw-g7xen3