Irie M

References (3)

Title : Temporal deterioration of neurological symptoms and increase of serum acetylcholine receptor antibody levels after thymectomy: a case report of a cat with myasthenia gravis - Nagata_2017_J.Vet.Med.Sci_78_1893
Author(s) : Nagata N , Miyoshi T , Otake Y , Suzuki H , Kagawa Y , Yamagami T , Irie M
Ref : J Vet Med Sci , 78 :1893 , 2017
Abstract : Neurological signs and serum acetylcholine receptor antibody (AChR-Ab) levels before and after thymectomy were monitored in a 6-year-old male cat with acquired Myasthenia Gravis (MG) as a paraneoplastic syndrome of thymoma. Soon after surgery, the neurological symptoms relapsed, and the cholinesterase inhibitor was administered to control them. The AChR-Ab levels increased postoperatively until 90 days after surgery. This is the first report on long term measurements of serum AChR-Ab levels in a cat with MG. Although thymectomy is valuable for the removal of thymoma, it may not resolve MG symptoms, neurological signs and serum AChR-Ab levels, without medication early after surgery. Also, this case report indicates that the AChR-Ab level might be a guide to detect a deterioration of MG symptoms.
ESTHER : Nagata_2017_J.Vet.Med.Sci_78_1893
PubMedSearch : Nagata_2017_J.Vet.Med.Sci_78_1893
PubMedID: 27593682

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