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Titolo:
Effect of protein kinase A-induced phosphorylation on the gating mechanismof the brain Na+ channel: Model fitting to whole-cell current traces
Autore:
dAlcantara, P; Schiffmann, SN; Swillens, S;
Indirizzi:
Free Univ Brussels, Fac Med, Inst Rech Interdisciplinaire Biol Humaine & Nucl, B-1070 Brussels, Belgium Free Univ Brussels Brussels Belgium B-1070 ucl, B-1070 Brussels, Belgium Free Univ Brussels, Fac Med, Unite Rech Cerveau, B-1070 Brussels, Belgium Free Univ Brussels Brussels Belgium B-1070 eau, B-1070 Brussels, Belgium
Titolo Testata:
BIOPHYSICAL JOURNAL
fascicolo: 1, volume: 77, anno: 1999,
pagine: 204 - 216
SICI:
0006-3495(199907)77:1<204:EOPKAP>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
CAMP-DEPENDENT PHOSPHORYLATION; SINGLE SODIUM-CHANNELS; RAT STRIATAL NEURONS; SQUID GIANT-AXON; ALPHA-SUBUNIT; SELECTIVE PHOSPHORYLATION; FUNCTIONAL MODULATION; HIPPOCAMPAL-NEURONS; RECEPTOR SUBTYPES; XENOPUS OOCYTES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: d'Alcantara, P Free Univ Brussels, Fac Med, Inst Rech Interdisciplinaire Biol Humaine & Nucl, 808 Route Lennik,CP601, B-1070 Brussels, Belgium Free Univ Brussels 808 Route Lennik,CP601 Brussels Belgium B-1070
Citazione:
P. d'Alcantara et al., "Effect of protein kinase A-induced phosphorylation on the gating mechanismof the brain Na+ channel: Model fitting to whole-cell current traces", BIOPHYS J, 77(1), 1999, pp. 204-216

Abstract

The activity of the voltage-gated Na+ channel is subjected to modulation through covalent modifications. It has been previously shown that brain Na+ currents are reduced following the activation of the protein kinase A (PKA)pathway, but the effect of the phosphorylation on the gating mechanism of the channel has not been demonstrated so far. In this study, we analyze thewhole-cell Na+ current recorded in the absence or presence of forskolin, which stimulates the PKA pathway. A minimal molecular model of the gating mechanism of the Na+ channel is defined to fit the experimental data: it consists of three closed states, one opens state, and two inactivated states. We experimentally demonstrate that the kinetics of inactivation from the closed states are not affected by phosphorylation. The results obtained by computer fitting indicate that, among all the kinetic parameters describing the transitions between states, only one parameter is significantly modified in the presence of forskolin, and corresponds to the acceleration of the inactivation from the open state. This conclusion is supported by the analysis of current traces obtained from cells in the presence of a phosphatase inhibitor or loaded with the PKA catalytic unit, and is in agreement with previously reported single channel records.

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Documento generato il 20/09/20 alle ore 20:16:41