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Antisense oligonucleotides against receptor kinase GRK2 disrupt target selectivity of β‐adrenergic receptors in atrial myocytes
Author(s) -
Wellner-Kienitz Marie-Cécile,
Bender Kirsten,
Brandts Bodo,
Meyer Thomas,
Pott Lutz
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00594-3
Subject(s) - pertussis toxin , receptor , beta adrenergic receptor kinase , g protein coupled inwardly rectifying potassium channel , agonist , microbiology and biotechnology , g protein coupled receptor kinase , chemistry , g protein , g protein coupled receptor , biophysics , biology , biochemistry
K + channels composed of GIRK subunits are predominantly expressed in the heart and various regions of the brain. They are activated by βγ‐subunits released from pertussis toxin‐sensitive G‐proteins coupled to different seven‐helix receptors. In rat atrial myocytes, activation of K (ACh) channels is strictly limited to receptors coupled to pertussis toxin‐sensitive G‐proteins. Upon treatment of myocytes with antisense oligodesoxynucleotides against GRK2, a receptor kinase with G βγ binding sites, in a fraction of cells, K (ACh) channels can be activated by β‐adrenergic receptors. Sensitivity to β‐agonist is insensitive to pertussis toxin treatment. These findings demonstrate a potential role of G βγ binding proteins for target selectivity of G‐protein‐coupled receptors