Results 11 to 20 of about 8,484 (124)

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 receptor antagonist treatment (bisoprolol, 0.2 mg/kg per d i.v., 35 d) on components of the ...
Peipei Ping, Ramona Gelzer-Bell, David A. Roth, Douglas P. Kiel, Paul A. Insel, H. Kirk Hammond   +5 more
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Mechanism of beta-adrenergic receptor kinase activation by G proteins

Journal of Biological Chemistry, 1993
The beta-adrenergic receptor kinase (beta-ARK) specifically phosphorylates the activated form of various G protein-coupled receptors such as the beta 2-adrenergic receptor (beta 2-AR). Recently, G protein beta gamma subunits have been demonstrated to activate beta-ARK-mediated receptor phosphorylation.
C.M. Kim, Sarah Dion, Jeffrey Benovic
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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 specific beta-adrenergic receptor kinase (beta ARK) and the cyclic AMP-dependent protein kinase A (PKA), as
Neil S. Roth, P. Campbell, M G Caron, R.J. Lefkowitz, Martin J. Lohse   +4 more
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Association of the regulatory beta-adrenergic receptor kinase with rat liver microsomal membranes.

Journal of Biological Chemistry, 1994
beta-Adrenergic receptor kinase (beta ARK) is a regulatory enzyme involved in the modulation of beta-adrenergic and other G protein-coupled receptors. It has been described that beta ARK is a cytosolic protein that transiently translocates to the plasma membrane in order to specifically phosphorylate agonist-occupied receptors.
Irene García-Higuera, Petronila Penela, Cristina Murga, Gustavo Egea, Pedro Bonay, Jeffrey Benovic, Federico Mayor   +6 more
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Rapid agonist‐induced beta‐adrenergic receptor kinase translocation in C6 glioma cells [PDF]

FEBS Letters, 1992
Exposure of C6 glioma cells to 1 μM isoproterenol leads to fast desensitization of the β‐adrenergic receptor/adenylyl cyclase system and transient receptor sequestration. It also triggers a very rapid and transient translocation to the plasma membrane or β‐adrenergic receptor kinase (βARK), a specific cytoplasmic kinase that phosphorylates only the ...
Irene García-Higuera, Federico Mayor
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Expression of beta-arrestins and beta-adrenergic receptor kinases in the failing human heart. [PDF]

Circulation Research, 1994
The beta-adrenergic receptor system of the failing human heart is markedly desensitized. We have recently postulated that this desensitization may in part be caused by an increase in beta-adrenergic receptor kinase (beta ARK) expression. beta ARK is thought to effect desensitization by acting in concert with an inhibitor protein, called beta-arrestin ...
Martin Ungerer, Giustino Parruti, Michael Böhm, Mechthild Puzicha, Antonio DeBlasi, Erland Erdmann, Martin J. Lohse   +6 more
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Cloning, expression, and chromosomal localization of beta-adrenergic receptor kinase 2. A new member of the receptor kinase family

Journal of Biological Chemistry, 1991
The beta-adrenergic receptor kinase (beta ARK) specifically phosphorylates the agonist-occupied form of the beta-adrenergic and related G protein-coupled receptors. Structural features of this enzyme have been elucidated recently by the isolation of a cDNA that encodes bovine beta ARK.
J.L. Benovic, James J. Onorato, J.L. Arriza, W. Carl Stone, Martin J. Lohse, N.A. Jenkins, Debra J. Gilbert, Neal G. Copeland, Marc G. Caron, Robert J. Lefkowitz   +9 more
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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 binding proteins.
Rainer Winstel, Stefan M.V. Freund, Cornelius Krasel, E. Hoppe, Martin J. Lohse   +4 more
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Agonist-dependent phosphorylation of the alpha 2-adrenergic receptor by the beta-adrenergic receptor kinase.

Journal of Biological Chemistry, 1987
Desensitization of the beta-adrenergic receptor, a receptor which is coupled to the stimulation of adenylate cyclase, may be regulated via phosphorylation by a unique protein kinase. This recently discovered enzyme, known as the beta-adrenergic receptor kinase, only phosphorylates the agonist-occupied form of the beta-adrenergic receptor.
J.L. Benovic, John W. Regan, Hiroaki Matsui, Federico Mayor, Susanna Cotecchia, L.M. Fredrik Leeb-Lundberg, Marc G. Caron, Robert J. Lefkowitz   +7 more
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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. However, the nature of the protein kinase(s) involved in receptor phosphorylation remains largely unknown.
Jeffrey Benovic, R. H. Strasser, M G Caron, Robert J. Lefkowitz   +3 more
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