Mini-review: Cell surface receptor for thyroid hormone and nongenomic regulation of ion fluxes in excitable cells

2010 ◽  
Vol 99 (2) ◽  
pp. 237-239 ◽  
Author(s):  
Paul J. Davis ◽  
Min Zhou ◽  
Faith B. Davis ◽  
Larry Lansing ◽  
Shaker A. Mousa ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Cell Surface ◽  
Ion Fluxes ◽  
Cell Surface Receptor ◽  
Excitable Cells ◽  
Surface Receptor

scholarly journals Acting via a Cell Surface Receptor, Thyroid Hormone Is a Growth Factor for Glioma Cells

2006 ◽  
Vol 66 (14) ◽  
pp. 7270-7275 ◽  
Author(s):  
Faith B. Davis ◽  
Heng-Yuan Tang ◽  
Ai Shih ◽  
Travis Keating ◽  
Lawrence Lansing ◽  
...  
Keyword(s):  
Growth Factor ◽  
Thyroid Hormone ◽  
Cell Surface ◽  
Glioma Cells ◽  
Cell Surface Receptor ◽  
Surface Receptor ◽  
A Cell

scholarly journals Integrin αVβ3 Contains a Cell Surface Receptor Site for Thyroid Hormone that Is Linked to Activation of Mitogen-Activated Protein Kinase and Induction of Angiogenesis

Endocrinology ◽  
2005 ◽  
Vol 146 (7) ◽  
pp. 2864-2871 ◽  
Author(s):  
Joel J. Bergh ◽  
Hung-Yun Lin ◽  
Lawrence Lansing ◽  
Seema N. Mohamed ◽  
Faith B. Davis ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Thyroid Hormone ◽  
Cell Surface ◽  
Matrix Protein ◽  
Integrin Αvβ3 ◽  
Recognition Site ◽  
Cell Surface Receptor ◽  
Extracellular Matrix Protein ◽  
Surface Receptor ◽  
A Cell

Abstract Integrin αVβ3 is a heterodimeric plasma membrane protein whose several extracellular matrix protein ligands contain an RGD recognition sequence. This study identifies integrin αVβ3 as a cell surface receptor for thyroid hormone [l-T4 (T4)] and as the initiation site for T4-induced activation of intracellular signaling cascades. Integrin αVβ3 dissociably binds radiolabeled T4 with high affinity, and this binding is displaced by tetraiodothyroacetic acid, αVβ3 antibodies, and an integrin RGD recognition site peptide. CV-1 cells lack nuclear thyroid hormone receptor, but express plasma membrane αVβ3; treatment of these cells with physiological concentrations of T4 activates the MAPK pathway, an effect inhibited by tetraiodothyroacetic acid, RGD peptide, and αVβ3 antibodies. Inhibitors of T4 binding to the integrin also block the MAPK-mediated proangiogenic action of T4. T4-induced phosphorylation of MAPK is inhibited by small interfering RNA knockdown of αV and β3. These findings suggest that T4 binds to αVβ3 near the RGD recognition site and show that hormone-binding to αVβ3 has physiological consequences.

Cell-surface receptor for thyroid hormone and tumor cell proliferation

2006 ◽  
Vol 1 (6) ◽  
pp. 753-761 ◽  
Author(s):  
Paul J Davis ◽  
Faith B Davis ◽  
Hung-Yun Lin ◽  
Joel J Bergh ◽  
Shaker Mousa ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Thyroid Hormone ◽  
Cell Surface ◽  
Tumor Cell ◽  
Cell Surface Receptor ◽  
Tumor Cell Proliferation ◽  
Surface Receptor

Adjunctive Input to the Nuclear Thyroid Hormone Receptor from the Cell Surface Receptor for the Hormone

Thyroid ◽  
2013 ◽  
Vol 23 (12) ◽  
pp. 1503-1509 ◽  
Author(s):  
Paul J. Davis ◽  
Hung-Yun Lin ◽  
Heng-Yuan Tang ◽  
Faith B. Davis ◽  
Shaker A. Mousa
Keyword(s):  
Thyroid Hormone ◽  
Cell Surface ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Cell Surface Receptor ◽  
Surface Receptor

Expression, function, and localization of the REG cell surface receptor

2001 ◽  
Vol 120 (5) ◽  
pp. A18-A19
Author(s):  
B DIECKGRAEFE ◽  
C HOUCHEN ◽  
H ZHANG
Keyword(s):  
Cell Surface ◽  
Cell Surface Receptor ◽  
Surface Receptor

Inhibition of rat ventricular automaticity by adenosine

1985 ◽  
Vol 248 (6) ◽  
pp. H907-H913 ◽  
Author(s):  
L. J. Heller ◽  
R. A. Olsson
Keyword(s):  
Cell Surface ◽  
Cell Surface Receptor ◽  
Chronotropic Effect ◽  
Surface Receptors ◽  
Adenosine Concentration ◽  
Surface Receptor ◽  
Ventricular Automaticity ◽  
Beating Rate ◽  
Chronotropic Effects ◽  
Developed Pressure

This study was designed to characterize adenosine's negative chronotropic effect on ventricular pacemakers. The spontaneous beating rate of isolated, isovolumic rat ventricular preparations perfused with Krebs-Henseleit solution decreased as the adenosine concentration was increased [log M effective concentration 50% (EC50) = -5.22 +/- 0.17]. The lack of effect of propranolol or atropine on this adenosine response eliminates the involvement of endogenous neurotransmitters. Support for the involvement of an external cell surface receptor was provided by findings that theophylline and 8-(4-sulfophenyl)theophylline, an analogue thought to act solely at the cell surface, significantly increased the adenosine log M EC50 to -3.94 +/- 0.22 and -3.61 +/- 0.22, respectively. An increase in spontaneous beating rate induced by theophylline, but not by its analogue, was blocked by the addition of propranolol. The relative chronotropic potency of the adenosine analogues R-PIA, S-PIA, and NECA suggests that the cell surface receptors may be of the Ri type. The negative chronotropic effects of adenosine and its analogues occurred at concentrations that had no effect on the developed pressure of the paced preparation. Electrocardiographic evaluations indicate that at high agonist concentrations, there was an abrupt alteration in electrical properties of the preparation, which could be blocked by theophylline and its analogue.

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