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Titolo:
Differential effects of unaggregated and aggregated amyloid beta protein (1-40) on K+ channel currents in primary cultures of rat cerebellar granule and cortical neurones
Autore:
Ramsden, M; Plant, LD; Webster, NJ; Vaughan, PFT; Henderson, Z; Pearson, HA;
Indirizzi:
Univ Leeds, Sch Biomed Sci, Leeds LS2 9JT, W Yorkshire, England Univ Leeds Leeds W Yorkshire England LS2 9JT S2 9JT, W Yorkshire, England Univ Leeds, Inst Cardiovasc Res, Leeds LS2 9JT, W Yorkshire, England Univ Leeds Leeds W Yorkshire England LS2 9JT S2 9JT, W Yorkshire, England
Titolo Testata:
JOURNAL OF NEUROCHEMISTRY
fascicolo: 3, volume: 79, anno: 2001,
pagine: 699 - 712
SICI:
0022-3042(200111)79:3<699:DEOUAA>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
SENSITIVE CA2+ CHANNELS; POTASSIUM CURRENTS; ALZHEIMERS-DISEASE; HIPPOCAMPAL SLICES; PRECURSOR PROTEIN; SENSORY NEURONS; A-TYPE; PEPTIDE; CELLS; ENHANCEMENT;
Keywords:
Alzheimer's disease; electrophysiology; ion channels; neurotoxicity; patch-clamp; potassium channels;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Pearson, HA Univ Leeds, Sch Biomed Sci, Leeds LS2 9JT, W Yorkshire, England Univ Leeds Leeds W Yorkshire England LS2 9JT rkshire, England
Citazione:
M. Ramsden et al., "Differential effects of unaggregated and aggregated amyloid beta protein (1-40) on K+ channel currents in primary cultures of rat cerebellar granule and cortical neurones", J NEUROCHEM, 79(3), 2001, pp. 699-712

Abstract

The effects of amyloid beta protein on voltage-gated K+ channel currents were studied using the whole-cell patch-clamp technique. The 1-40 amino acidform of amyloid beta protein was applied to primary cultures of rat cerebellar granule and cortical neurones for 24 h. Both the unaggregated and aggregated forms of the peptide, which have differing biological activities, were used. In cerebellar granule neurones, 24-h pre-incubation with 1 mum unaggregated amyloid beta protein resulted in a 60% increase in the 'A'-type component of K+ current. Increased delayed rectifier activity was Cd2+-sensitive and was presumed to be secondary to an increase in voltage-gated Ca2+ channel current activity. Unaggregated amyloid beta protein had no effect on any component of the K+ channel current in cortical neurones. One micromolar of aggregated amyloid beta protein had no effect on K+ channel current in either cell type but reduced cell survival within 24 h as measured usingthe 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) andterminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (TUNEL) assays. The unaggregated form of amyloid beta protein had no neurotoxic effects when applied to either neurone type for up to 72 h. These data indicate that the unaggregated, nonpathological form of amyloid beta protein causes changes in the ion channel function of neurones, possibly reflectinga physiological role for the peptide.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 20:50:45