Results 31 to 40 of about 8,484 (124)

Purification and characterization of the beta-adrenergic receptor kinase.

Journal of Biological Chemistry, 1987
The beta-adrenergic receptor kinase (beta-ARK) is a recently discovered enzyme which specifically phosphorylates the agonist-occupied form of the beta-adrenergic receptor (beta-AR) as well as the light-bleached form of rhodopsin. beta-ARK is present in a wide variety of mammalian tissues.
M G Caron, Jeffery L. Benovic, Robert J. Lefkowitz, Federico Mayor, C Staniszewski   +4 more
openaire   +3 more sources

Phosphorylation of Src by phosphoinositide 3-kinase regulates beta-adrenergic receptor-mediated EGFR transactivation [PDF]

Cellular Signalling, 2016
β2-Adrenergic receptors (β2AR) transactivate epidermal growth factor receptors (EGFR) through formation of a β2AR-EGFR complex that requires activation of Src to mediate signaling. Here, we show that both lipid and protein kinase activities of the bifunctional phosphoinositide 3-kinase (PI3K) enzyme are required for β2AR-stimulated EGFR transactivation.
Lewis J. Watson, Kevin Alexander, Maradumane L. Mohan, Amber L. Bowman, Supachoke Mangmool, Kunhong Xiao, Sathyamangla V. Naga Prasad, Howard A. Rockman   +7 more
openalex   +3 more sources

Phosphorylation and desensitization of human m2 muscarinic cholinergic receptors by two isoforms of the beta-adrenergic receptor kinase

Journal of Biological Chemistry, 1993
Studies of the human m2 (hm2) muscarinic cholinergic receptors (mAChR) have been performed to provide further insights into the potential regulation of these receptors by isoforms of the beta-adrenergic receptor kinase (beta ARK). The hm2 mAChR and the isoforms beta ARK1 and beta ARK2 were individually expressed in, and purified from, insect Sf9 cells ...
Ricardo M. Richardson, C. Kim, Jeffrey Benovic, Marie Thérèse Hosey   +3 more
openalex   +4 more sources

Protein kinase translocation following beta-adrenergic receptor activation in C6 glioma cells.

Journal of Biological Chemistry, 1980
Incubation of C6 glioma cells with isoproterenol elicits an increase in cyclic AMP content, followed by an activation of cyclic AMP-dependent protein kinase (ATP:protein phosphotransferase, EC 2.7.1.37). The cytoplasm of these glioma cells contains type II protein kinase and a small amount of cyclic AMP-independent protein kinase.
Joan P. Schwartz, E. Costa
openalex   +4 more sources

The G protein coupled receptor kinase 2 plays an essential role in beta-adrenergic receptor-induced insulin resistance [PDF]

Cardiovascular Research, 2009
Insulin (Ins) resistance (IRES) associates to increased cardiovascular risk as observed in metabolic syndrome. Chronic stimulation of beta-adrenergic receptors (betaAR) due to exaggerated sympathetic nervous system activity is involved in the pathogenesis of IRES. The cellular levels of G protein coupled receptor kinase 2 (GRK2) increase during chronic
Ersilia Cipolletta, Alfonso Campanile, Gaetano Santulli, Emma Sanzari, Dario Leosco, Pietro Campiglia, Bruno Trimarco, Guido Iaccarino   +7 more
openalex   +6 more sources

Somatostatin induces translocation of the beta-adrenergic receptor kinase and desensitizes somatostatin receptors in S49 lymphoma cells.

Journal of Biological Chemistry, 1987
The beta-adrenergic receptor kinase is a cytosolic enzyme that specifically phosphorylates the agonist-occupied form of the beta-adrenergic receptor (beta AR). Beta AR kinase appears to be translocated from the cytosol to the plasma membrane when kin- S49 lymphoma cells are incubated with either beta-adrenergic agonists or prostaglandin E1, both of ...
Federico Mayor, Jeffrey Benovic, M G Caron, R J Lefkowitz   +3 more
openalex   +3 more sources

Inhibition of the β-Adrenergic Receptor Kinase by Polyanions

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.
Robert J. Lefkowitz, Marc G. Caron, Jeffrey L. Benovic, W.C. Stone   +3 more
openaire   +3 more sources

The β-Adrenergic Receptor Is a Substrate for the Insulin Receptor Tyrosine Kinase [PDF]

Journal of Biological Chemistry, 1996
G-protein-linked receptors and intrinsic tyrosine-kinase growth receptors represent two prominent modalities in cell signaling. Cross-regulation among members of both receptor superfamilies has been reported, including the counter-regulatory effects of insulin on beta-adrenergic catecholamine action.
Baltensperger, Kurt, Karoor, Vijaya, Paul, Hyacinth, Ruoho, Arnold E., Czech, Michael P., Malbon, Craig C.   +5 more
openaire   +4 more sources

Overexpression of beta-arrestin and beta-adrenergic receptor kinase augment desensitization of beta 2-adrenergic receptors.

Journal of Biological Chemistry, 1993
Receptor-specific or homologous desensitization of beta 2-adrenergic receptors is thought to be effected via phosphorylation of the receptor by the beta-adrenergic receptor kinase (beta ARK), followed by binding of beta-arrestin. We have generated stably transfected Chinese hamster ovary cell lines overexpressing either of the two regulatory proteins ...
Susanne Pippig, S Andexinger, Kratika Daniel, Mechthild Puzicha, M G Caron, R J Lefkowitz, Martin J. Lohse   +6 more
openalex   +4 more sources

The substance P receptor, which couples to Gq/11, is a substrate of beta-adrenergic receptor kinase 1 and 2

Journal of Biological Chemistry, 1993
The agonist-occupied forms of several G-protein-coupled receptors that modulate the activity of adenylycyclase via Gs (e.g. beta 2-adrenergic) or Gi (e.g. alpha 2-adrenergic and cardiac muscarinic) are phosphorylated by beta-adrenergic receptor kinases (beta ARK 1 and beta ARK 2).
Madan M. Kwatra, Debra A. Schwinn, Jolanda Schreurs, Jonathan L. Blank, C.M. Kim, Jeffrey Benovic, James E. Krause, Marc G. Caron, Robert J. Lefkowitz   +8 more
openalex   +4 more sources