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Gewählte Publikation:

Lohberger, B; Groschner, K; Tritthart, H; Schreibmayer, W.
IK.ACh activation by arachidonic acid occurs via a G-protein-independent pathway mediated by the GIRK1 subunit.
Pflugers Arch. 2000; 441(2-3):251-256 Doi: 10.1007/s004240000405
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Führende Autor*innen der Med Uni Graz
Lohberger Birgit
Schreibmayer Wolfgang
Co-Autor*innen der Med Uni Graz
Groschner Klaus
Tritthart Helmut
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Abstract:
The molecular target of arachidonic-acid-derived metabolites, serving as second messengers that activate atrial acetylcholine-activated potassium current (IK.ACh) in addition to G-protein beta/gamma subunits (Gbeta/gamma), is unknown. Co-expression of two isoforms of G-protein-activated, inwardly rectifying potassium channels (GIRKs) in oocytes of Xenopus laevis revealed that these heterologous co-expressed GIRKs, which are responsible for the formation of IK.ACh in the atrium, are activated by arachidonic acid metabolites, like their counterparts in atrial cells. The expression of homooligomeric GIRK1(F137S) and GIRK4wt channels revealed that this activatory mechanism is specific to the GIRKI subunit. Sequestrating available Gbeta/gamma by overexpression of C-betaARK (a Gbeta/gamma binding protein) failed to abolish the activation of GIRK currents by arachidonic acid. From our experiments we conclude that the GIRKI subunit itself is the molecular target for regulation of GIRK channels by arachidonic acid metabolites.
Find related publications in this database (using NLM MeSH Indexing)
Acetylcholine - pharmacology
Animals -
Arachidonic Acid - pharmacology
Cyclic AMP-Dependent Protein Kinases - genetics
Electric Conductivity -
Female -
G Protein-Coupled Inwardly-Rectifying Potassium Channels -
GTP-Binding Proteins - physiology
Gene Expression -
Oligonucleotides, Antisense - pharmacology
Oocytes - physiology
Peptide Fragments - genetics
Potassium Channels - drug effects Potassium Channels - genetics Potassium Channels - physiology
Potassium Channels, Inwardly Rectifying -
Receptors, Muscarinic - genetics Receptors, Muscarinic - physiology
Recombinant Proteins -
Transfection -
Xenopus laevis -

Find related publications in this database (Keywords)
arachidonic acid
GIRK
two-electrode voltage clamp
Xenopus laevis
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