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Temporal differences in the phosphorylation state of pre- and postsynaptic protein kinase C substrates B-50/GAP-43 and neurogranin during long-term potentiation.
Ramakers, G M; De Graan, P N; Urban, I J; Kraay, D; Tang, T; Pasinelli, P; Oestreicher, A B; Gispen, W H.
Afiliación
  • Ramakers GM; Department of Medical Pharmacology, Rudolf Magnus Institute for Neurosciences, University of Utrecht, The Netherlands.
J Biol Chem ; 270(23): 13892-8, 1995 Jun 09.
Article en En | MEDLINE | ID: mdl-7775448
The phosphorylation state of two identified neuralspecific protein kinase C substrates (the presynaptic protein B-50 and the postsynaptic protein neurogranin) was monitored after the induction of long term potentiation in the CA1 field of rat hippocampus slices by quantitative immunoprecipitation following 32Pi labeling in the recording chamber. B-50 phosphorylation was increased from 10 to 60 min, but no longer at 90 min after long term potentiation had been induced, neurogranin phosphorylation only at 60 min. Increased phosphorylation was not found when long term potentiation was blocked with the N-methyl-D-aspartate receptor antagonist D-2-amino-5-phosphonovalerate, when only low frequency stimulation was applied or tetanic stimulation failed to induce long term-potentiation. Our data show that both B-50 and neurogranin phosphorylation are increased following the induction of long term potentiation, thus providing strong evidence for pre- and postsynaptic protein kinase C activation during narrow, partially overlapping, time windows after the induction of long term potentiation.
Asunto(s)
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Unión a Calmodulina / Proteína Quinasa C / Glicoproteínas de Membrana / Potenciación a Largo Plazo / Proteínas del Tejido Nervioso Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: J Biol Chem Año: 1995 Tipo del documento: Article País de afiliación: Países Bajos Pais de publicación: Estados Unidos
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Unión a Calmodulina / Proteína Quinasa C / Glicoproteínas de Membrana / Potenciación a Largo Plazo / Proteínas del Tejido Nervioso Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: J Biol Chem Año: 1995 Tipo del documento: Article País de afiliación: Países Bajos Pais de publicación: Estados Unidos