Takahashi E

References (6)

Title : Functional significance of rare neuroligin 1 variants found in autism - Nakanishi_2017_PLoS.Genet_13_e1006940
Author(s) : Nakanishi M , Nomura J , Ji X , Tamada K , Arai T , Takahashi E , Bucan M , Takumi T
Ref : PLoS Genet , 13 :e1006940 , 2017
Abstract : Genetic mutations contribute to the etiology of autism spectrum disorder (ASD), a common, heterogeneous neurodevelopmental disorder characterized by impairments in social interaction, communication, and repetitive and restricted patterns of behavior. Since neuroligin3 (NLGN3), a cell adhesion molecule at the neuronal synapse, was first identified as a risk gene for ASD, several additional variants in NLGN3 and NLGN4 were found in ASD patients. Moreover, synaptopathies are now known to cause several neuropsychiatric disorders including ASD. In humans, NLGNs consist of five family members, and neuroligin1 (NLGN1) is a major component forming a complex on excitatory glutamatergic synapses. However, the significance of NLGN1 in neuropsychiatric disorders remains unknown. Here, we systematically examine five missense variants of NLGN1 that were detected in ASD patients, and show molecular and cellular alterations caused by these variants. We show that a novel NLGN1 Pro89Leu (P89L) missense variant found in two ASD siblings leads to changes in cellular localization, protein degradation, and to the impairment of spine formation. Furthermore, we generated the knock-in P89L mice, and we show that the P89L heterozygote mice display abnormal social behavior, a core feature of ASD. These results, for the first time, implicate rare variants in NLGN1 as functionally significant and support that the NLGN synaptic pathway is of importance in the etiology of neuropsychiatric disorders.
ESTHER : Nakanishi_2017_PLoS.Genet_13_e1006940
PubMedSearch : Nakanishi_2017_PLoS.Genet_13_e1006940
PubMedID: 28841651
Gene_locus related to this paper: human-NLGN1

Title : Production and properties of lipase of Aeromonas sobria - Takahashi_2012_Microbiol.Immunol_56_295
Author(s) : Takahashi E , Ito H , Kobayashi H , Yamanaka H , Takeda Y , Balakrish Nair G , Arimoto S , Negishi T , Okamoto K
Ref : Microbiol Immunol , 56 :295 , 2012
Abstract : Aeromonas have been isolated from a wide variety of aquatic environments. However the number of Aeromonas in sea water is extremely small compared to that in fresh water. In in vitro culture, Aeromonas can grow in mediums containing NaCl at a concentration of 3.0%, this concentration corresponding to that of sea water. It is unclear why the number of Aeromonas is low in sea water. Exoproteins of bacteria are thought to be important for bacterial growth and survival in the environment. Previously, the present authors have shown that mediums containing 3.0% NaCl suppress production of two proteases, serine protease and metalloprotease. In this experiment, other exoproteins whose production is influenced by the amount of NaCl in the medium were analyzed. A protein whose production is repressed in medium containing 3.0% NaCl was found and purified. Biological assay of the purified protein showed that it degrades tributyrin and hydrolyzes para-nitrophenyl-fatty acylesters. These results show that the protein is a lipase. Subsequently, the nucleotide sequence of the gene encoding the lipase was determined and the amount of mRNA of the lipase gene in the cells measured. It was found that transcription of the gene is not inhibited by NaCl in the medium. This result indicates that the lipase might be synthesized, but the folding process to become an active structure does not progress smoothly in a medium containing 3.0% NaCl.
ESTHER : Takahashi_2012_Microbiol.Immunol_56_295
PubMedSearch : Takahashi_2012_Microbiol.Immunol_56_295
PubMedID: 22376235

Title : Dipeptidyl aminopeptidase IV from Stenotrophomonas maltophilia exhibits activity against a substrate containing a 4-hydroxyproline residue - Nakajima_2008_J.Bacteriol_190_7819
Author(s) : Nakajima Y , Ito K , Toshima T , Egawa T , Zheng H , Oyama H , Wu YF , Takahashi E , Kyono K , Yoshimoto T
Ref : Journal of Bacteriology , 190 :7819 , 2008
Abstract : The crystal structure of dipeptidyl aminopeptidase IV from Stenotrophomonas maltophilia was determined at 2.8-A resolution by the multiple isomorphous replacement method, using platinum and selenomethionine derivatives. The crystals belong to space group P4(3)2(1)2, with unit cell parameters a = b = 105.9 A and c = 161.9 A. Dipeptidyl aminopeptidase IV is a homodimer, and the subunit structure is composed of two domains, namely, N-terminal beta-propeller and C-terminal catalytic domains. At the active site, a hydrophobic pocket to accommodate a proline residue of the substrate is conserved as well as those of mammalian enzymes. Stenotrophomonas dipeptidyl aminopeptidase IV exhibited activity toward a substrate containing a 4-hydroxyproline residue at the second position from the N terminus. In the Stenotrophomonas enzyme, one of the residues composing the hydrophobic pocket at the active site is changed to Asn611 from the corresponding residue of Tyr631 in the porcine enzyme, which showed very low activity against the substrate containing 4-hydroxyproline. The N611Y mutant enzyme was generated by site-directed mutagenesis. The activity of this mutant enzyme toward a substrate containing 4-hydroxyproline decreased to 30.6% of that of the wild-type enzyme. Accordingly, it was considered that Asn611 would be one of the major factors involved in the recognition of substrates containing 4-hydroxyproline.
ESTHER : Nakajima_2008_J.Bacteriol_190_7819
PubMedSearch : Nakajima_2008_J.Bacteriol_190_7819
PubMedID: 18820015
Gene_locus related to this paper: xanma-P95782

Title : Decreased lipoprotein lipase as a risk factor for atypical neuroleptic-induced hypertriglyceridemia -
Author(s) : Yamamoto K , Fukuda M , Nogawa A , Takahashi E , Miyaoka H
Ref : J Clin Psychiatry , 68 :802 , 2007
PubMedID: 17503998

Title : Molecular cloning and sequencing of a cDNA encoding the feline T-cell activation antigen CD26 homologue -
Author(s) : Nishimura Y , Miyazawa T , Ikeda Y , Izumiya Y , Nakamura K , Sato E , Mikami T , Takahashi E
Ref : Immunogenetics , 50 :366 , 1999
PubMedID: 10630304
Gene_locus related to this paper: felca-CD26

Title : Structure, organization, and chromosomal mapping of the human macrophage scavenger receptor gene - Emi_1993_J.Biol.Chem_268_2120
Author(s) : Emi M , Asaoka H , Matsumoto A , Itakura H , Kurihara Y , Wada Y , Kanamori H , Yazaki Y , Takahashi E , Lepert M , Jean-Marc Lalouel JM , Kodama T , Mukai T
Ref : Journal of Biological Chemistry , 268 :2120 , 1993
Abstract : Macrophage scavenger receptors (MSR) mediate the binding, internalization, and processing of a wide range of negatively charged macromolecules. Functional MSR are trimers of two C-terminally different subunits that contain six functional domains. We have cloned an 80-kilobase human MSR gene and localized it to band p22 on chromosome 8 by fluorescent in situ hybridization and by genetic linkage using three common restriction fragment length polymorphisms. The human MSR gene consists of 11 exons, and two types of mRNAs are generated by alternative splicing from exon 8 to either exon 9 (type II) or to exons 10 and 11 (type I). The promoter has a 23-base pair inverted repeat with homology to the T cell element. Exon 1 encodes the 5'-untranslated region followed by a 12-kilobase intron which separates the transcription initiation and the translation initiation sites. Exon 2 encodes a cytoplasmic domain, exon 3, a transmembrane domain, exons 4 and 5, an alpha-helical coiled-coil, and exons 6-8, a collagen-like domain. The position of the gap in the coiled coil structure corresponds to the junction of exons 4 and 5. These results show that the human MSR gene consists of a mosaic of exons that encodes the functional domains. Furthermore, the specific arrangement of exons played a role in determining the structural characteristics of functional domains.
ESTHER : Emi_1993_J.Biol.Chem_268_2120
PubMedSearch : Emi_1993_J.Biol.Chem_268_2120
PubMedID: 8093617
Gene_locus related to this paper: human-LPL