Your browser doesn't support javascript.
loading
Functional characterization of human N-methyl-D-aspartate subtype 1A/2D receptors.
Hess, S D; Daggett, L P; Deal, C; Lu, C C; Johnson, E C; Veliçelebi, G.
Afiliación
  • Hess SD; SIBIA Neurosciences, Inc., La Jolla, California 92037, USA.
J Neurochem ; 70(3): 1269-79, 1998 Mar.
Article en En | MEDLINE | ID: mdl-9489750
The human NMDAR2D subunit was cloned, and the pharmacological properties of receptors resulting from injection of transcripts encoding human NMDAR1A and NMDAR2D subunits in Xenopus oocytes were characterized by profiling NMDA receptor agonists and antagonists. We found that glutamate, NMDA, glycine, and D-serine were significantly more potent on hNMDAR1A/2D than on hNMDAR1A/2A or hNMDAR1A/2B. Also, the potencies of NMDA and glycine were higher for hNMDAR1A/2D than for hNMDAR1A/2C. Ifenprodil was more potent at hNMDAR1A/2B than at hNMDAR1A/2D, whereas 5,7-dichlorokynurenate was more potent at hNMDAR1A/2A than at hNMDAR1A/2D. As measured in transiently transfected human embryonic kidney 293 cells, the maximal inward current in the presence of external Mg2 occurred at -40 mV, and full block was not observed at negative potentials. Kinetic measurements revealed that the higher affinity of hNMDAR1A/2D for both glutamate and glycine relative to hNMDAR1A/2A and hNMDA1A/2B can be explained by slower dissociation of each agonist from hNMDAR1A/2D. The hNMDAR1A/2D combination represents a pharmacologically and functionally distinct receptor subtype and may constitute a potentially important target for therapeutic agents active in the human CNS.
Asunto(s)
Buscar en Google
Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Receptores de N-Metil-D-Aspartato Límite: Animals / Humans Idioma: En Revista: J Neurochem Año: 1998 Tipo del documento: Article País de afiliación: Estados Unidos
Buscar en Google
Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Receptores de N-Metil-D-Aspartato Límite: Animals / Humans Idioma: En Revista: J Neurochem Año: 1998 Tipo del documento: Article País de afiliación: Estados Unidos