Hirao K

References (4)

Title : Optical resolution of n-butyl D- and L-lactates using immobilized lipase catalyst - Ohara_2011_J.Biosci.Bioeng_111_19
Author(s) : Ohara H , Yamamoto M , Onogi A , Hirao K , Kobayashi S
Ref : J Biosci Bioeng , 111 :19 , 2011
Abstract : n-Butyl D- and L-lactates (BuDLa and BuLLa) were incubated with immobilized lipase. (1)H-NMR showed that BuDLa reacted to oligomers, while BuLLa did not react. A mixture containing 90.4% of BuLLa and 9.6% of BuDLa was incubated with the enzyme for 72 h, then distilled. The purity of BuLLa increased to 98.6%.
ESTHER : Ohara_2011_J.Biosci.Bioeng_111_19
PubMedSearch : Ohara_2011_J.Biosci.Bioeng_111_19
PubMedID: 20851671

Title : Interaction of S-SCAM with neural plakophilin-related Armadillo-repeat protein\/delta-catenin - Ide_1999_Biochem.Biophys.Res.Commun_256_456
Author(s) : Ide N , Hata Y , Deguchi M , Hirao K , Yao I , Takai Y
Ref : Biochemical & Biophysical Research Communications , 256 :456 , 1999
Abstract : Synaptic scaffolding molecule (S-SCAM) is a multiple PDZ domain-containing protein, which interacts with neuroligin, a cell adhesion molecule, and the NMDA receptor. In this study, we searched for S-SCAM-interacting proteins and obtained a neuralplakophilin-related armadillo-repeat protein (NPRAP)/delta-catenin. NPRAP/delta-catenin bound to the last PDZ domain of S-SCAM via its carboxyl-terminus in three different cell-free assay systems, was coimmunoprecipitated with S-SCAM from rat crude synaptosomes, and was localized at the excitatory synapses in rat hippocampal neurons. NPRAP/delta-catenin may be implicated in the molecular organization of synaptic junctions through the interaction with S-SCAM.
ESTHER : Ide_1999_Biochem.Biophys.Res.Commun_256_456
PubMedSearch : Ide_1999_Biochem.Biophys.Res.Commun_256_456
PubMedID: 10080919

Title : A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins - Hirao_1998_J.Biol.Chem_273_21105
Author(s) : Hirao K , Hata Y , Ide N , Takeuchi M , Irie M , Yao I , Deguchi M , Toyoda A , Sudhof TC , Takai Y
Ref : Journal of Biological Chemistry , 273 :21105 , 1998
Abstract : At synaptic junctions, pre- and postsynaptic membranes are connected by cell adhesion and have distinct structures for specialized functions. The presynaptic membranes have a machinery for fast neurotransmitter release, and the postsynaptic membranes have clusters of neurotransmitter receptors. The molecular mechanism of the assembly of synaptic junctions is not yet clear. Pioneering studies identified postsynaptic density (PSD)-95/SAP90 as a prototypic synaptic scaffolding protein to maintain the structure of synaptic junctions. PSD-95/SAP90 belongs to a family of membrane-associated guanylate kinases and binds N-methyl-D-aspartate receptors, potassium channels, and neuroligins through the PDZ domains and GKAP/SAPAP/DAP through the guanylate kinase (GK) domain. We performed here a yeast two-hybrid screening for SAPAP-interacting molecules and identified a novel protein that has an inverse structure of membrane-associated guanylate kinases with an NH2-terminal GK-like domain followed by two WW and five PDZ domains. It binds SAPAP through the GK-like domain and NMDA receptors and neuroligins through the PDZ domains. We named this protein S-SCAM (synaptic scaffolding molecule) because S-SCAM may assemble receptors and cell adhesion proteins at synaptic junctions.
ESTHER : Hirao_1998_J.Biol.Chem_273_21105
PubMedSearch : Hirao_1998_J.Biol.Chem_273_21105
PubMedID: 9694864
Gene_locus related to this paper: ratno-1neur

Title : Binding of neuroligins to PSD-95 - Irie_1997_Science_277_1511
Author(s) : Irie M , Hata Y , Takeuchi M , Ichtchenko K , Toyoda A , Hirao K , Takai Y , Rosahl TW , Sudhof TC
Ref : Science , 277 :1511 , 1997
Abstract : PSD-95 is a component of postsynaptic densities in central synapses. It contains three PDZ domains that localize N-methyl-D-aspartate receptor subunit 2 (NMDA2 receptor) and K+ channels to synapses. In mouse forebrain, PSD-95 bound to the cytoplasmic COOH-termini of neuroligins, which are neuronal cell adhesion molecules that interact with beta-neurexins and form intercellular junctions. Neuroligins bind to the third PDZ domain of PSD-95, whereas NMDA2 receptors and K+ channels interact with the first and second PDZ domains. Thus different PDZ domains of PSD-95 are specialized for distinct functions. PSD-95 may recruit ion channels and neurotransmitter receptors to intercellular junctions formed between neurons by neuroligins and beta-neurexins.
ESTHER : Irie_1997_Science_277_1511
PubMedSearch : Irie_1997_Science_277_1511
PubMedID: 9278515
Gene_locus related to this paper: human-NLGN1 , human-NLGN2 , human-NLGN3 , human-NLGN4X