Results 41 to 50 of about 10,836 (202)
ABSTRACT Inflammatory bowel disease (IBD), primarily Crohn's disease and ulcerative colitis, is a chronic relapsing inflammatory disorder of the gastrointestinal tract and an important risk factor for IBD‐associated cancer. Increasing evidence suggests that gut microbiota dysbiosis, epithelial barrier dysfunction, and immune microenvironment remodeling
Xue Zhang +4 more
wiley +1 more source
Phosphorylation of Src by phosphoinositide 3-kinase regulates beta-adrenergic receptor-mediated EGFR transactivation [PDF]
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 +7 more
openaire +2 more sources
Major depressive disorder (MDD) and treatment‐resistant depression (TRD) remain leading causes of disability, providing the impetus for receptor‐level treatment strategies beyond monoamine reuptake. The serotonin 5‐HT2B receptor (5‐HT2BR) is uniquely positioned at the interface of central‐antidepressant mechanisms and peripheral cardiac risks.
Gia Han Le +8 more
wiley +1 more source
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 ...
R M, Richardson +3 more
openaire +2 more sources
Essential role of β-adrenergic receptor kinase 1 in cardiac development and function [PDF]
The β-adrenergic receptor kinase 1 (βARK1) is a member of the G protein-coupled receptor kinase (GRK) family that mediates the agonist-dependent phosphorylation and desensitization of G protein-coupled receptors. We have cloned and disrupted the βARK1 gene in mice by homologous recombination. No homozygote βARK1 −/−
Jaber, M +9 more
openaire +2 more sources
Systemic aging fuels heart failure: Molecular mechanisms and therapeutic avenues
Abstract Systemic aging influences various physiological processes and contributes to structural and functional decline in cardiac tissue. These alterations include an increased incidence of left ventricular hypertrophy, a decline in left ventricular diastolic function, left atrial dilation, atrial fibrillation, myocardial fibrosis and cardiac ...
Zhuyubing Fang +7 more
wiley +1 more source
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.
R, Winstel +4 more
openaire +3 more sources
Sequeira et al. reveal how the glucagon‐like peptide‐1 receptor agonist (GLP‐1‐RA) semaglutide restores cardiomyocyte function in rats subjected to a high‐fat/high‐fructose diet (HFD). Employing fluorescence‐ and patch‐clamp technology in isolated cardiac myocytes, they demonstrate that semaglutide reverses HFD‐induced activation of L‐type calcium ...
Vasco Sequeira +12 more
wiley +1 more source
We tested the hypothesis that angiotensin II type 1 receptor blocker (ARB) may improve beta-adrenergic receptor (AR) coupling in heart failure (HF) after myocardial infarction (MI).Beta-AR desensitization is one of the mechanisms underlying the transition from compensated to decompensated HF.
Takahashi, Toshiyuki +7 more
openaire +2 more sources
Inhibition of beta-adrenergic receptor kinase prevents rapid homologous desensitization of beta 2-adrenergic receptors. [PDF]
Homologous (agonist-specific) desensitization of beta-adrenergic receptors (beta ARs) is accompanied by and appears to require phosphorylation of the receptors. We have recently described a novel protein kinase, beta AR kinase, which phosphorylates beta ARs in vitro in an agonist-dependent manner.
Lohse, MJ +3 more
openaire +2 more sources

