Reappearance of beta-adrenergic receptors after isoproterenol treatment in intact C6-cells.

Hertel, Cornelia; Staehelin, Matthys

doi:10.1083/jcb.97.5.1538

Cited by 39 publications

(18 citation statements)

References 30 publications

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“…3H-PN200-110 (Amersham Corp., Arlington Heights, IL) is a lipophilic dihydropyridine Ca channel antagonist with high affinity and specificity for the Ca channel (22,23). 3H-CGPl2177 (Amersham Corp.) is a relatively hydrophilic beta-adrenergic antagonist that binds predominantly, if not exclusively, to cell surface beta-adrenergic receptors (24,25). Cells were grown on six-well plates in the presence or absence of 10 nM T3 for 48 h. Cells were washed with Hepes-buffered medium (pH 7.35) and then incubated with concentrations of 3H-PN200-l 1O ranging from 100 to 1,400 pM, or 3H-CGPl2177 ranging from 50 to 2,000 pM for 30 min (steady state) at 370C.…”

Section: Methodsmentioning

confidence: 99%

Effect of thyroid hormone on slow calcium channel function in cultured chick ventricular cells.

Kim¹,

Smith²,

Marsh³

1987

J. Clin. Invest.

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The hyperthyroid state is associated with increased myocardial contractility. To clarify responsible mechanisms, we examined the effects of thyroid hormone on slow Ca channels, beta-adrenergic receptors, transsarcolemmal 45Ca flux and cytosolic free calcium in cultured chick ventricular cells. Compared with cells grown without triiodothyronine (T3), cells grown in 10 nM T3 possessed (a) 67% (P < 0.05) more dihydropyridine 3H-PN200-110 binding sites, (b) 24% (P < 0.05) more beta-adrenergic antagonist 3H-CGP12177 binding sites, (c) a 57% (P < 0.05) greater nifedipine-sensitive initial 45Ca uptake rate, and (d) a 31% (P < 0.05) greater nifedipine-sensitive 45Ca uptake rate in response to BAY k 8644. Time-averaged mean intracellular free Ca concentration ([Cali) measured with fura-2, total protein content,

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Section: Methodsmentioning

confidence: 99%

Effect of thyroid hormone on slow calcium channel function in cultured chick ventricular cells.

Kim¹,

Smith²,

Marsh³

1987

J. Clin. Invest.

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“…There is then in most systems a 'sorting process' whereby receptors and hormones are dissociated by acidificiation of the vesicles (Tycko & Maxfield, 1982;Forgac & Cantley, 1984;Wolkoff et al, 1984) and then separated into two endosomal compartments. The ligand is degraded in the lysosomes and the products subsequently released (Harford et al, 1983;Ascoli & Puett, 1978), whilst there is strong evidence that the receptors are returned to the cell surface (Hertel & Staehelin, 1983;Schwartz et al, 1984).…”

Section: Introductionmentioning

confidence: 99%

Evidence for the rapid internalization and recycling of lutropin receptors in rat testis Leydig cells

Habberfield¹,

Dix²,

Cooke³

1986

Biochemical Journal

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A study into the binding of 1251-human chorionic gonadotropin (hCG) to the lutropin (LH) receptor in rat testis Leydig cells, and subsequent internalization of the hormone-receptor complex, has been carried out. The results show that there is rapid internalization of the hormone-receptor complex; 240 receptors/cell (from a total of approx. 4000 receptors/cell) were internalized each minute in the first hour after exposure to hCG. Radioactivity was released from the cell 1 h after internalization and was found to be associated with highly degraded hCG. The endocytic process was found to have two temperature-sensitive steps. At 4°C, movement of the hormone-receptor complex inside the cell did not occur, and at 21°C hormone accumulated within the cytoplasm but was not degraded or released from the cell. At 34°C, internalization, degradation and loss of the degraded hormone from the cell occurred. These processes appeared to reach a steady state after 2 h. Even though there is rapid internalization of the hormone-receptor complex following exposure to hCG, the binding sites on the cell surface were maintained for at least 4 h. The number of binding sites on the cell surface was not decreased by a protein synthesis inhibitor but was reduced to undetectable levels by monensin. This compound inhibits acidification of endocytic vesicles, which is known to be an important prerequisite to receptor cycling. It is concluded that, in the rat testis Leydig cells, following binding of hCG to the LH receptor there is rapid internalization of the complex and that recycling of the receptor occurs to the cell surface. This process may be essential in maintaining the capacity of the Leydig cell to bind fresh hormone.

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“…Receptor internalization involves phosphorylation by at least two kinases, protein kinase A and G protein receptor kinases and subsequent binding of the phosphorylated receptors to arrestins, which serves as adaptor proteins recruiting components of the transport machinery to the clathrin-coated pits and initiating formation of the early endosome (Krupnick and Benovic 1998;Baillie et al, 2003). The internalized receptors in the early endosome may be sorted to the lysosome for degradation or to the recycling endosome for return to the plasma membrane (Hertel and Staehelin, 1983;Morrison et al, 1996). The balance of intracellular trafficking (i.e., export, endocytosis, recycling, and degradation) dictates the level of receptor at the plasma membrane and, in turn, will influence the magnitude of the cellular response to a given signal.…”

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confidence: 99%

Differential Regulation of the Cell-Surface Targeting and Function of β- and α₁-Adrenergic Receptors by Rab1 GTPase in Cardiac Myocytes

et al. 2006

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The molecular mechanism underlying the export from the endoplasmic reticulum (ER) to the cell surface and its role in the regulation of signaling of adrenergic receptors (ARs) remain largely unknown. In this report, we determined the role of Rab1, a Ras-like GTPase that coordinates protein transport specifically from the ER to the Golgi, in the cell surface targeting and function of endogenous ␤-and ␣ 1 -ARs in neonatal rat ventricular myocytes. Adenovirus-driven expression of Rab1 into myocytes selectively increased the cell-surface number of ␣ 1 -AR, but not ␤-AR, whereas the dominant-negative mutant Rab1N124I significantly reduced the cell-surface expression of ␤-AR and ␣ 1 -AR. Brefeldin A inhibited ␤-AR and ␣ 1 -AR export and antagonized the Rab1 effect on ␣ 1 -AR expression. Manipulation of Rab1 function similarly influenced the transport of ␣ 1A -and ␣ 1B -ARs as well as ␤ 1 -and ␤ 2 -ARs. Fluorescent microscopy analysis demonstrated that expression of Rab1N124I and Rab1 small interfering RNA induced a marked accumulation of GFP-tagged ␤ 2 -AR and ␣ 1B -AR in the ER. Consistent with the effects on receptor cell-surface targeting, Rab1 selectively enhanced ERK1/2 activation and hypertrophic growth in response to the ␣ 1 -AR agonist phenylephrine but not to the ␤-AR agonist isoproterenol. Rab1N124I inhibited both agonist-mediated ERK1/2 activation and hypertrophic growth in neonatal myocytes. These results demonstrate that the cellsurface targeting and signaling of ␤-and ␣ 1 -ARs require Rab1 and are differentially modulated by augmentation of Rab1 function. Our data provide strong evidence implicating the ER-toGolgi traffic as a site for selective manipulation of distinct AR function in cardiac myocytes.

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Reappearance of beta-adrenergic receptors after isoproterenol treatment in intact C6-cells.

Cited by 39 publications

References 30 publications

Effect of thyroid hormone on slow calcium channel function in cultured chick ventricular cells.

Effect of thyroid hormone on slow calcium channel function in cultured chick ventricular cells.

Evidence for the rapid internalization and recycling of lutropin receptors in rat testis Leydig cells

Differential Regulation of the Cell-Surface Targeting and Function of β- and α₁-Adrenergic Receptors by Rab1 GTPase in Cardiac Myocytes

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Reappearance of beta-adrenergic receptors after isoproterenol treatment in intact C6-cells.

Cited by 39 publications

References 30 publications

Effect of thyroid hormone on slow calcium channel function in cultured chick ventricular cells.

Effect of thyroid hormone on slow calcium channel function in cultured chick ventricular cells.

Evidence for the rapid internalization and recycling of lutropin receptors in rat testis Leydig cells

Differential Regulation of the Cell-Surface Targeting and Function of β- and α1-Adrenergic Receptors by Rab1 GTPase in Cardiac Myocytes

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Product

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Differential Regulation of the Cell-Surface Targeting and Function of β- and α₁-Adrenergic Receptors by Rab1 GTPase in Cardiac Myocytes