Noradrenaline, oxymetazoline and phorbol myristate acetate induce distinct functional actions and phosphorylation patterns of α1A-adrenergic receptors.

@article{AlcntaraHernndez2017NoradrenalineOA,
  title={Noradrenaline, oxymetazoline and phorbol myristate acetate induce distinct functional actions and phosphorylation patterns of $\alpha$1A-adrenergic receptors.},
  author={Rocio J. Alc{\'a}ntara-Hern{\'a}ndez and Aurelio Hern{\'a}ndez‐M{\'e}ndez and M Teresa Romero-{\'A}vila and Marco A. Alfonzo‐M{\'e}ndez and Andr{\'e} Sampaio Pupo and J. Adolfo Garc{\'i}a-S{\'a}inz},
  journal={Biochimica et biophysica acta. Molecular cell research},
  year={2017},
  volume={1864 12},
  pages={
          2378-2388
        }
}
S1P1 receptor phosphorylation, internalization, and interaction with Rab proteins: effects of sphingosine 1-phosphate, FTY720-P, phorbol esters, and paroxetine
TLDR
The data suggested that the three agents induce interaction with early endosomes, but that the natural agonist induced rapid receptor recycling, whereas activation of protein kinase C favored interaction with late endosome and slow recycling and FTYp triggered receptor interaction with vesicles associated with proteasomal/lysosomal degradation.
Updates in the function and regulation of α1‐adrenoceptors
TLDR
The tissue distribution of the three α1‐adrenoceptor subtypes in the cardiovascular system, genitourinary system, and CNS is surveyed, highlighting the functions already identified as mediated by the predominant activation of specific subtypes.
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TLDR
The results demonstrate that stimulation of α1a-adrenergic receptor, or activation of protein kinase C, leads to α1 a-ad Renoreceptor phosphorylation, and chimeric receptors, where the carboxyl-terminal tails ofα1a and α1badrenergic receptors were exchanged, were constructed and expressed.
Differential Phosphorylation, Desensitization, and Internalization of α1A−Adrenoceptors Activated by Norepinephrine and Oxymetazoline
TLDR
It is shown in human embryonic kidney-293 cells that the low-efficacy agonist OXY induces G protein–coupled receptor kinase 2–dependent α1A-AR phosphorylation, leading to significant receptor desensitization and internalization, which is important in view of the therapeutic vasoconstrictor effects of this drug and the varied biologic process regulated by α1a-ARs.
Activation of Endothelin ETA Receptors Induces Phosphorylation of α1b-Adrenoreceptors in Rat-1 Fibroblasts*
TLDR
The data indicate that activation of ETA receptors by endothelin-1 induces α1b-adrenoreceptor phosphorylation and alters G protein coupling and phosphoaminoacid analysis revealed the presence of phosphoserine and traces of phosphothreonine, but not of phosphotyrosine, suggesting that the putative tyrosine kinase(s) could act in a step previous to receptor phosphorylated.
Roles of the α1A-adrenergic receptor carboxyl tail in protein kinase C-induced phosphorylation and desensitization
TLDR
The results suggest that the α1A-AR carboxyl terminus tail was not essential for signaling or desensitization, and the phosphorylation pattern of the receptors was “transplanted”, but the functional consequences of such a transplant were very limited.
Acute Agonist-mediated Desensitization of the Human α1a-Adrenergic Receptor Is Primarily Independent of Carboxyl Terminus Regulation
TLDR
Deletion of the α1aAR carboxyl terminus has no effect on receptor internalization or either agonist-induced or GRK-mediated receptor desensitization, suggesting mechanisms underlying acute agonists-mediated regulation of human α1 aARs are primarily independent of the carboxy terminus.
Effect of phorbol myristate acetate on alpha 1-adrenergic action in cells expressing recombinant alpha 1-adrenoceptor subtypes.
TLDR
The data indicate that there are differences in sensitivity to PMA among the alpha 1-adrenoceptor subtypes stably expressed in rat-1 fibroblasts, and this effect was not altered by overnight pretreatment with PMA.
Characterization of the Phosphorylation Sites Involved in G Protein-coupled Receptor Kinase- and Protein Kinase C-mediated Desensitization of the α1B-Adrenergic Receptor*
TLDR
Generalities about the biochemical mechanisms underlying homologous and heterologous desensitization of G protein-coupled receptors linked to the activation of phospholipase C are provided.
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