Results 1 to 10 of about 28,167 (157)

Differences in the signaling pathways of α1A- and α1B-adrenoceptors are related to different endosomal targeting [PDF]

, 2013
Aims: To compare the constitutive and agonist-dependent endosomal trafficking of α1A- and α1B-adrenoceptors (ARs) and to establish if the internalization pattern determines the signaling pathways of each subtype.
A Hirasawa, AC Hanyaloglu, AL Lattion, B Lei, BL Wolfe, C Moyano, C Stenbergen, CD Wright, D Calebiro, D Chalothorn, D Diviani, D Gesty-Palmer, D Wu, DM Perez, DP Morris, DP Morris, E Oliver, EJ Adie, EJ Adie, Elena Carceller, F Liu, Fermí Montó, Graeme Milligan, Ian Christie McGrath, James Porter, JB Morris, JD Pediani, JD Pediani, JL Benovic, John Pediani, KA DeFea, L Stanasila, LM Luttrell, M von Zastrow, María Antonia Noguera, MC Lyssand JS De Fino, Miguel Pérez-Aso, MW Lee, MY Tsang, P Lajoie, PA Patel, Pilar D’Ocon, RH Oakley, RR Price, S Ahn, S Alexander, S Keffel, S Mhaouty-Kodja, S Terrillon, SK Shenoy, SM DeWire, SS Ferguson, TL Theroux, Vanessa Segura, Y Huang   +54 more
core   +24 more sources

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
N S, Roth, P T, Campbell, M G, Caron, R J, Lefkowitz, M J, Lohse   +4 more
openaire   +2 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 specific beta-adrenergic receptor kinase (BARK), leading to functional uncoupling from adenylyl ...
I, García-Higuera, F, Mayor
openaire   +2 more sources

The receptor kinase family: primary structure of rhodopsin kinase reveals similarities to the beta-adrenergic receptor kinase. [PDF]

Proceedings of the National Academy of Sciences, 1991
Light-dependent deactivation of rhodopsin as well as homologous desensitization of beta-adrenergic receptors involves receptor phosphorylation that is mediated by the highly specific protein kinases rhodopsin kinase (RK) and beta-adrenergic receptor kinase (beta ARK), respectively. We report here the cloning of a complementary DNA for RK.
Lorenz, W, Inglese, J, Palczewski, K, Onorato, JJ, Caron, MG, Lefkowitz, RJ   +5 more
openaire   +2 more sources

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, S B, Dion, J L, Benovic
openaire   +4 more sources

Regulation of Neuromodulator Receptor Efficacy - Implications for Whole-Neuron and Synaptic Plasticity [PDF]

, 2004
Membrane receptors for neuromodulators (NM) are highly regulated in their distribution and efficacy - a phenomenon which influences the individual cell's response to central signals of NM release.
Scheler, Gabriele
core   +1 more source

Tailoring therapy for heart failure: the pharmacogenomics of adrenergic receptor signaling. [PDF]

, 2014
Heart failure is one of the leading causes of mortality in Western countries, and β-blockers are a cornerstone of its treatment. However, the response to these drugs is variable among individuals, which might be explained, at least in part, by genetic ...
Barrese, V, Femminella, GD, Ferrara, N, Rengo, G   +3 more
core   +2 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 receptor antagonist treatment (bisoprolol, 0.2 mg/kg per d i.v., 35 d) on components of the ...
P, Ping, R, Gelzer-Bell, D A, Roth, D, Kiel, P A, Insel, H K, Hammond   +5 more
openaire   +2 more sources

Inhibition of the beta-adrenergic receptor kinase by polyanions.

The Journal of biological chemistry, 1989
The beta-adrenergic receptor kinase, which specifically phosphorylates the agonist-occupied beta-adrenergic receptor, is strongly inhibited by polyanions. Heparin and dextran sulfate inhibit the enzyme with an IC50 of approximately 0.15 microM. De-N-sulfated heparin is approximately 8-fold less potent.
J L, Benovic, W C, Stone, M G, Caron, R J, Lefkowitz   +3 more
openaire   +2 more sources

β-Adrenergic Receptor Kinase (GRK2) Colocalizes with β-Adrenergic Receptors during Agonist-induced Receptor Internalization [PDF]

Journal of Biological Chemistry, 1997
Rapid regulation of G protein-coupled receptors appears to involve agonist-promoted receptor phosphorylation by G protein-coupled receptor kinases (GRKs). This is followed by binding of uncoupling proteins termed arrestins and transient receptor internalization. In this report we show that the beta-adrenergic receptor kinase (betaARK-1 or GRK2) follows
A, Ruiz-Gómez, F, Mayor
openaire   +4 more sources