ArticleThe Journal of physiology1998
Role of receptor kinase in short-term desensitization of cardiac muscarinic K+ channels expressed in Chinese hamster ovary cells.
Article in The Journal of physiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Short-term desensitization of muscarinic K+ current in the heart.Biophysical journal · 2013Article
- Acute desensitization of acetylcholine and endothelin-1 activated inward rectifier K+ current in myocytes from the cardiac atrioventricular node.Biochemical and biophysical research communications · 2012Article
- Endogenous RGS proteins enhance acute desensitization of GABA(B) receptor-activated GIRK currents in HEK-293T cells.Pflugers Archiv : European journal of physiology · 2005Article
- Acute desensitization of GIRK current in rat atrial myocytes is related to K+ current flow.The Journal of physiology · 2004Article
- G-protein coupled receptor kinases as modulators of G-protein signalling.The Journal of physiology · 1999Review
- Evidence that the nucleotide exchange and hydrolysis cycle of G proteins causes acute desensitization of G-protein gated inward rectifier K+ channels.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
1. The cardiac muscarinic receptor-K+ channel system was reconstructed in Chinese hamster ovary (CHO) cells by transfecting the cells with the various components of the system. The activity of the muscarinic K+ channel was measured with the cell-attached configuration of the patch clamp technique. 2. In CHO cells transfected with the channel (Kir3.1/Kir3.4), receptor (hm2) and receptor kinase (GRK2), on exposure to agonist, there was a decline in channel activity as a result of desensitization, similar to that in atrial cells. 3. Whereas the desensitization was almost abolished by not transfecting with the receptor kinase or by transfecting with a mutant receptor lacking phosphorylation sites, it was only reduced (by approximately 39%) by transfecting with a mutant receptor kinase with little/kinase activity. 4. These results suggest that the receptor kinase is responsible for desensitization of the muscarinic K+ channel and that this involves phosphorylation-dependent and -independent mechanisms.
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