Results 1 to 10 of about 28,040 (141)

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

Harmine and 7,8-dihydroxyflavone synergistically suitable for amyotrophic lateral sclerosis management: An in silico study [PDF]

Research Results in Pharmacology, 2022
Introduction: Amyotrophic lateral sclerosis (ALS) is a fatal neurological disease characterized by progressive degeneration of both upper and lower motor neurons, resulting in paralysis and eventually leads to death from respiratory failure typically ...
Toluwase Fatoki, Stanley Chukwuejim, Omodele Ibraheem, Christiana Oke, Blessing Ejimadu, Isaiah Olaoye, Oluwabukola Oyegbenro, Taiwo Salami, Romilola Basorun, Oluwafisayomi Oluwadare, Yetunde Salawudeen   +10 more
doaj   +3 more sources

ADAM17, A Key Player of Cardiac Inflammation and Fibrosis in Heart Failure Development During Chronic Catecholamine Stress

Frontiers in Cell and Developmental Biology, 2021
Heart failure development is characterized by persistent inflammation and progressive fibrosis owing to chronic catecholamine stress. In a chronic stress state, elevated catecholamines result in the overstimulation of beta-adrenergic receptors (βARs ...
Joseph Adu-Amankwaah, Gabriel Komla Adzika, Adebayo Oluwafemi Adekunle, Marie Louise Ndzie Noah, Richard Mprah, Aisha Bushi, Nazma Akhter, Fei Huang, Yaxin Xu, Seyram Yao Adzraku, Iqra Nadeem, Hong Sun   +11 more
doaj   +1 more source

Activation of the Thiazide-Sensitive Sodium-Chloride Cotransporter by Beta3-Adrenoreceptor in the Distal Convoluted Tubule

Frontiers in Physiology, 2021
We previously showed that the beta-3 adrenergic receptor (BAR3) is expressed in most segments of the nephron where its agonism promotes a potent antidiuretic effect.
Serena Milano, Monica Carmosino, Andrea Gerbino, Ilenia Saponara, Dominga Lapi, Massimo Dal Monte, Paola Bagnoli, Maria Svelto, Giuseppe Procino   +8 more
doaj   +1 more source

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

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

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

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

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 ...
Garcia-Higuera, Irene, Mayor, Federico
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