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Titolo:
Differential changes in the phosphorylation of the protein kinase C substrates myristoylated alanine-rich C kinase substrate and growth-associated protein-43/B-50 following Schaffer collateral long-term potentiation and long-term depression
Autore:
Ramakers, GMJ; McNamara, RK; Lenox, RH; De Graan, PNE;
Indirizzi:
Univ Penn, Sch Med, Dept Psychiat, Abramson Res Ctr, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 n Res Ctr, Philadelphia, PA 19104 USA Rudolf Magnus Inst Neurosci, Dept Med Pharmacol, NL-3508 TA Utrecht, Netherlands Rudolf Magnus Inst Neurosci Utrecht Netherlands NL-3508 TA , Netherlands
Titolo Testata:
JOURNAL OF NEUROCHEMISTRY
fascicolo: 5, volume: 73, anno: 1999,
pagine: 2175 - 2183
SICI:
0022-3042(199911)73:5<2175:DCITPO>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
NERVE-TERMINALS; RAT-BRAIN; GLUTAMATE RECEPTORS; SYNAPTIC PLASTICITY; ARACHIDONIC-ACID; 87-KDA PROTEIN; MARCKS; HIPPOCAMPUS; B-50; LTP;
Keywords:
protein kinase C; myristoylated alanine-rich C kinase substrate growth-associated protein-43; long-term potentiation; long-term depression; (RS)-alpha-methyl-4-carboxyphenylglycine-d-2-amino-5-phosphonopentanoic acid; glutamate;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
57
Recensione:
Indirizzi per estratti:
Indirizzo: McNamara, RK Univ Penn, Sch Med, Dept Psychiat, Abramson Res Ctr, 802B,34th St,Civ Ctr Blvd, Philadelphia, PA 19104 USA Univ Penn 802B,34th St,Civ Ctr Blvd Philadelphia PA USA 19104
Citazione:
G.M.J. Ramakers et al., "Differential changes in the phosphorylation of the protein kinase C substrates myristoylated alanine-rich C kinase substrate and growth-associated protein-43/B-50 following Schaffer collateral long-term potentiation and long-term depression", J NEUROCHEM, 73(5), 1999, pp. 2175-2183

Abstract

Activation of protein kinase C (PKC) is one of the biochemical pathways thought to be activated during activity-dependent synaptic plasticity in the brain, and long-term potentiation (LTP) and long-term depression (LTD) are two of the most extensively studied models of synaptic plasticity. Here we have examined changes in the in situ phosphorylation level of two major PKCsubstrates, myristoylated alanine-rich C kinase substrate (MARCKS) and growth-associated protein (GAP)-43/B-50, after pharmacological stimulation or induction of LTP or LTD in the CA1 field of the hippocampus. We find that direct PKC activation with phorbol esters, K+-induced depolarization, and activation of metabotropic glutamate receptors increase the in situ phosphorylation of both MARCKS and GAP-43/B-50. The induction of LTP increased the in situ phosphorylation of both MARCKS and GAP-43/B-50 at 10 min following high-frequency stimulation, but only GAP-43/B-50 phosphorylation remained elevated 60 min after ITP induction. Furthermore, blockade of LTP induction with the NMDA receptor antagonist D-2-amino-5-phosphonopentanoic acid prevented elevations in GAP-43/B-50 phosphorylation but did not prevent the elevation in MARCKS phosphorylation 10 min following LTP induction. The induction of LTD resulted in a reduction in GAP-43/B-50 phosphorylation but did notaffect MARCKS phosphorylation. Together these findings show that activity-dependent synaptic plasticity elicits PKC-mediated phosphorylation of substrate proteins in a highly selective and coordinated manner and demonstrate the compartmentalization of PKC-substrate interactions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 15:32:26