Cloning of Two Thyrotropin-Releasing Hormone Receptor Subtypes from a Lower Vertebrate (Catostomus commersoni): Functional Expression, Gene Structure, and Evolution

2001 ◽  
Vol 124 (2) ◽  
pp. 236-245 ◽  
Author(s):  
Sönke Harder ◽  
Oliver Dammann ◽  
Friedrich Buck ◽  
Henk Zwiers ◽  
Karl Lederis ◽  
...  
Keyword(s):  
Gene Structure ◽  
Hormone Receptor ◽  
Functional Expression ◽  
Thyrotropin Releasing Hormone ◽  
Receptor Subtypes ◽  
Catostomus Commersoni ◽  
Lower Vertebrate ◽  
Releasing Hormone

scholarly journals The hemispheric functional expression of the thyrotropin-releasing-hormone receptor is not determined by the receptors' physical distribution

1994 ◽  
Vol 303 (1) ◽  
pp. 129-134 ◽  
Author(s):  
N Matus-Leibovitch ◽  
D R Nussenzveig ◽  
M C Gershengorn ◽  
Y Oron
Keyword(s):  
Hormone Receptor ◽  
Signal Transduction Pathway ◽  
Functional Expression ◽  
Thyrotropin Releasing Hormone ◽  
Releasing Hormone ◽  
Lipid Signal ◽  
Marked Preference ◽  
Receptor Number ◽  
Lower Ratio ◽  
G Protein Coupled

The thyrotropin-releasing-hormone receptor (TRH-R) is a member of a family of the G-protein-coupled receptors that share structural similarities and exert their physiological action via the inositol lipid signal-transduction pathway. The TRH-R when expressed in Xenopus oocytes exhibits marked preference of the response (increased chloride conductance) for the animal hemisphere. Whereas the rat TRH-R functional distribution was strongly asymmetric (animal/vegetal ratio = 9.5), the mouse TRH-R exhibited a significantly lower ratio (3.9). Truncation of the last 59 amino acids of the C-terminal region of the mouse TRH-R did not lead to any changes in the functional hemispheric distribution. Despite the polarization of response, receptor number was similar on both hemispheres. Moreover, the apparent half-life of the functional expression of the TRH-R was approx. 4 h on both hemispheres when the expression was inhibited by a specific antisense oligonucleotide. Inhibition of total protein synthesis with cycloheximide affected hemispheric responses mediated by each of the three TRH-Rs tested in a qualitatively different way. These results suggest that an additional, rapidly degraded, protein modulates the functional hemispheric expression of the TRH-Rs.

scholarly journals A Novel Transcript for the Thyrotropin-Releasing Hormone Receptor in Human Pituitary and Pituitary Tumors

1997 ◽  
Vol 82 (12) ◽  
pp. 4224-4228 ◽  
Author(s):  
Masanobu Yamada ◽  
Koushi Hashimoto ◽  
Teturou Satoh ◽  
Nobuyuki Shibusawa ◽  
Hideaki Kohga ◽  
...  
Keyword(s):  
Hormone Receptor ◽  
Pituitary Tumors ◽  
Thyrotropin Releasing Hormone ◽  
Human Pituitary ◽  
Releasing Hormone ◽  
Novel Transcript
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