Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT

Freigegeben

Zeitschriftenartikel

Cloning, tissue distribution and functional characterization of the chicken P2X(1) receptor

MPG-Autoren
/persons/resource/persons182417

Soto,  Florentina
Molecular biology of neuronal signals, Max Planck Institute of Experimental Medicine, Max Planck Society;

/persons/resource/persons182094

Borchardt,  Kerstin
Molecular biology of neuronal signals, Max Planck Institute of Experimental Medicine, Max Planck Society;

Externe Ressourcen
Es sind keine externen Ressourcen hinterlegt
Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte in PuRe verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

Soto, F., Krause, U., Borchardt, K., & Ruppelt, A. (2003). Cloning, tissue distribution and functional characterization of the chicken P2X(1) receptor. FEBS Letters, 533(1-3), 54-58.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0029-26FA-E
Zusammenfassung
We describe a new chicken P2X subunit that is an orthologue of the mammalian P2X(1) receptor. Functional characterization of chicken P2X(1) receptors was performed using the amphotericin B perforated patch configuration to avoid the current run-down observed under whole-cell patch-clamp conditions. Responses to agonists and to the antagonist PPADS (pyridoxal 5-phosphate 6- azophenyl-2',4'-disulfonic acid) were similar to what has been described for mammalian orthologues. However, the antagonists suramin and NF023 were much less potent at chicken P2X(1) receptors than at human P2X(1) receptors. In embryonic tissues, transcript expression is predominant in lung, liver and skeletal muscle. Overlapping expression with cP2X(4) and cP2X(5) subunits in several embryonic tissues, including skeletal muscle, indicates that the native embryonic P2X receptors could be heteromultimeric. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.