Comparative Analysis of β-Adrenergic Receptor Kinase and β-Arrestin mRNA Expression in Human Cells [PDF]
Receptor phosphorylation is a key step in the process of rapid desensitization. beta-Adrenergic receptor kinase is a specific receptor kinase that is known to phosphorylate and induce desensitization of several G-coupled synaptic receptors only when they are occupied by their agonists.
Parruti G +3 more
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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]
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.
Marc G Caron, , J Codina
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Beta-agonist- and prostaglandin E1-induced translocation of the beta-adrenergic receptor kinase: evidence that the kinase may act on multiple adenylate cyclase-coupled receptors. [PDF]
beta-Adrenergic receptor kinase (beta-AR kinase) is a cytosolic enzyme that phosphorylates the beta-adrenergic receptor only when it is occupied by an agonist [Benovic, J. Strasser, R. H., Caron, M. G. & Lefkowitz, R. J. (1986) Proc. Natl. Acad. Sci. USA
Marc G Caron, , J L Benovic
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The β-adrenergic receptor kinase in heart failure
Journal of Molecular and Cellular Cardiology, 2003Heart failure (HF) remains a significant and increasing cause of worldwide morbidity and mortality. HF is less a disease than a common clinical endpoint resulting from diverse, but often co-existing etiologies-including hypertension, coronary artery disease, and viral cardiomyopathy.
Jason A, Petrofski, Walter J, Koch
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Previous studies have demonstrated that muscarinic cholinergic receptors (mAChR) become markedly phosphorylated when intact cardiac cells are stimulated with a muscarinic agonist. This process appears to be related to the process of receptor desensitization. However, the mechanism of agonist-induced phosphorylation of mAChR is not known.
M M, Kwatra +4 more
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Functionally active targeting domain of the beta-adrenergic receptor kinase: an inhibitor of G beta gamma-mediated stimulation of type II adenylyl cyclase. [PDF]
The beta-adrenergic receptor kinase (beta ARK) phosphorylates its membrane-associated receptor substrates, such as the beta-adrenergic receptor, triggering events leading to receptor desensitization.
James Inglese, , Louis Luttrell
exaly +1 more source
Light-dependent phosphorylation of rhodopsin by β-adrenergic receptor kinase
Nature, 1986The structural components involved in transduction of extracellular signals as diverse as a photon of light impinging on the retina or a hormone molecule impinging on a cell have been highly conserved. These components include a recognition unit or receptor (for example, the beta-adrenergic receptor (beta AR) for catecholamines or the 'light receptor ...
J L, Benovic +4 more
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Activation of β-Adrenergic Receptor Kinase During Myocardial Ischemia
Circulation Research, 1996During myocardial ischemia, a local release of noradrenaline coincides with an increased density of β-adrenergic receptors. The functional activity of these receptors, however, is mainly determined by their state of phosphorylation. The β-adrenergic receptor kinase (βARK) specifically phosphorylates and thereby inactivates β-adrenergic receptors after ...
M, Ungerer +4 more
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Functional consequences of A1 adenosine-receptor phosphorylation by the β-adrenergic receptor kinase
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1993Treatment of smooth-muscle cells with R-phenylisopropyladenosine (R-PIA) leads to a loss of A1 adenosine receptor (A1AR)-mediated inhibition of adenylate cyclase, a decrease in receptor number and an increase in receptor phosphorylation. In this study, the role of the beta-adrenergic receptor kinase (beta ARK) in the phosphorylation and inactivation of
V, Ramkumar +4 more
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Cardiac Function in Mice Overexpressing the β-Adrenergic Receptor Kinase or a βARK Inhibitor
Science, 1995Transgenic mice were created with cardiac-specific overexpression of the β-adrenergic receptor kinase-1 (βARK1) or a βARK inhibitor. Animals overexpressing βARK1 demonstrated attenuation of isoproterenol-stimulated left ventricular contractility in vivo, dampening of myocardial adenylyl cyclase activity, and reduced functional coupling of β-adrenergic ...
W J, Koch +6 more
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