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Titolo:
CALPAIN-MEDIATED REGULATION OF NMDA RECEPTOR STRUCTURE AND FUNCTION
Autore:
BI XN; RONG YQ; CHEN J; DANG SD; WANG Z; BAUDRY M;
Indirizzi:
UNIV SO CALIF,PROGRAM NEUROSCI,HNB 309 LOS ANGELES CA 90089 UNIV SO CALIF,PROGRAM NEUROSCI LOS ANGELES CA 90089
Titolo Testata:
Brain research
fascicolo: 1-2, volume: 790, anno: 1998,
pagine: 245 - 253
SICI:
0006-8993(1998)790:1-2<245:CRONRS>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
INDUCED SEIZURE ACTIVITY; LONG-TERM POTENTIATION; D-ASPARTATE RECEPTORS; ADULT-RAT BRAIN; NR1 SUBUNIT; ACTIVATION; PROTEINS; DOMAIN; PROTEOLYSIS; INDUCTION;
Keywords:
CALPAIN; GLUTAMATE; RECEPTOR; PLASTICITY; CALCIUM; HIPPOCAMPUS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
X.N. Bi et al., "CALPAIN-MEDIATED REGULATION OF NMDA RECEPTOR STRUCTURE AND FUNCTION", Brain research, 790(1-2), 1998, pp. 245-253

Abstract

Calpains have been previously shown to regulate AMPA receptor properties by producing partial truncation of the C-terminal domains of several receptor subunits. We now report that NMDA receptor subunits, in particular NR2 subunits, are also subjected to calpain-mediated truncation. Treatment of synaptic membranes with calpain I resulted in truncation of both NR1 and NR2 subunits, with the appearance of NR2 species with lower mol.wt. than native subunits, but still recognized by antibodies directed at the C-terminal domain. This treatment did not modify the binding of several Ligands of the NMDA receptors, such as glutamate, glycine or TCP. Incubation of thin frozen-thawed brain sections with calcium resulted in calpain-mediated selective degradation of NR2 subunits, as truncation into smaller fragments was totally blocked by calpain inhibitors. Under the same conditions, TCP binding to sections was decreased by about 50%, an effect also blocked by calpain inhibitors. Treatment of hippocampal slices in culture with the excitotoxin, kainic acid, also produced calpain-mediated truncation of the C-terminaldomain of NR2 but not NR1 subunits of the NMDA receptors. The resultsindicate that calpain activation produces several modifications of NMDA receptors, including the truncation of the C-terminal domain of NR2subunits, and changes in channel binding properties. They suggest that calpain-mediated regulation of NMDA receptors might represent a feed-back regulation of the receptors which could be used to limit receptor activation. (C) 1998 Elsevier Science B.V.

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Documento generato il 20/01/21 alle ore 12:46:01