Comparative rates of desensitization of beta-adrenergic receptors by the beta-adrenergic receptor kinase and the cyclic AMP-dependent protein kinase. [PDF]
Proceedings of the National Academy of Sciences, 1991 Three separate processes may contribute to rapid beta-adrenergic receptor desensitization: functional uncoupling from the stimulatory guanine nucleotide-binding protein Gs, mediated by phosphorylation of the receptors by two distinct kinases, the ...
Neil S. Roth +4 more
semanticscholar +5 more sources
Altered expression of beta-adrenergic receptor kinase and beta 1-adrenergic receptors in the failing human heart. [PDF]
Circulation, 1993 BACKGROUND In chronic heart failure, the positive inotropic effects of beta-adrenergic receptor agonists are greatly reduced, in part as a result of two alterations of the cardiac beta-adrenergic receptors: loss of their function (receptor uncoupling ...
Martin Ungerer +4 more
semanticscholar +6 more sources
Rapid desensitization of neonatal rat liver beta-adrenergic receptors. A role for beta-adrenergic receptor kinase. [PDF]
Journal of Clinical Investigation, 1994 Exposure of beta-adrenergic receptors (BAR) to agonists often leads to a rapid loss of receptor responsiveness. The proposed mechanisms of such rapid receptor desensitization include receptor phosphorylation by either cAMP-dependent protein kinase or the
Irene García-Higuera, Federico Mayor
semanticscholar +5 more sources
Reduced beta-adrenergic receptor activation decreases G-protein expression and beta-adrenergic receptor kinase activity in porcine heart. [PDF]
Journal of Clinical Investigation, 1995 To determine whether beta-adrenergic receptor agonist activation influences guanosine 5'-triphosphate-binding protein (G-protein) expression and beta-adrenergic receptor kinase activity in the heart, we examined the effects of chronic beta 1-adrenergic ...
Peipei Ping +5 more
semanticscholar +5 more sources
Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor. [PDF]
Proceedings of the National Academy of Sciences, 1986 Agonist-promoted desensitization of adenylate cyclase is intimately associated with phosphorylation of the beta-adrenergic receptor in mammalian, avian, and amphibian cells.
Jeffrey Benovic +3 more
semanticscholar +4 more sources
A beta-adrenergic receptor kinase-like enzyme is involved in olfactory signal termination. [PDF]
Proceedings of the National Academy of Sciences, 1993 We have previously shown that second-messenger-dependent kinases (cAMP-dependent kinase, protein kinase C) in the olfactory system are essential in terminating second-messenger signaling in response to odorants. We now document that subtype 2 of the beta-
Sabine Schleicher +4 more
semanticscholar +5 more sources
Functional desensitization of the isolated beta-adrenergic receptor by the beta-adrenergic receptor kinase: potential role of an analog of the retinal protein arrestin (48-kDa protein). [PDF]
Proceedings of the National Academy of Sciences, 1987 The beta-adrenergic receptor kinase is an enzyme, possibly analogous to rhodopsin kinase, that multiply phosphorylates the beta-adrenergic receptor only when it is occupied by stimulatory agonists.
Jeffrey Benovic +5 more
semanticscholar +5 more sources
A beta-adrenergic receptor kinase dominant negative mutant attenuates desensitization of the beta 2-adrenergic receptor. [PDF]
Journal of Biological Chemistry, 1994 The beta-adrenergic receptor kinase (beta ARK) specifically phosphorylates the activated form of the beta 2-adrenergic receptor (beta 2AR) and related G protein-coupled receptors. To further elucidate the role of beta ARK in receptor desensitization, we generated a beta ARK dominant negative mutant by converting an invariant lysine residue in the ...
Guanghui Kong +2 more
semanticscholar +4 more sources
Protein kinase cross-talk: membrane targeting of the beta-adrenergic receptor kinase by protein kinase C. [PDF]
Proceedings of the National Academy of Sciences, 1996 The beta-adrenergic receptor kinase (betaARK) is the prototypical member of the family of cytosolic kinases that phosphorylate guanine nucleotide binding-protein-coupled receptors and thereby trigger uncoupling between receptors and guanine nucleotide ...
Rainer Winstel +4 more
semanticscholar +6 more sources
Journal of Biological Chemistry, 1993 The beta gamma subunits of heterotrimeric G proteins play important roles in regulating receptor-stimulated signal transduction processes. Recently appreciated among these is their role in the signaling events that lead to the phosphorylation and subsequent desensitization of muscarinic cholinergic (Haga, K., and Haga, T. (1992) J. Biol. Chem.
Walter J. Koch +3 more
semanticscholar +5 more sources