Molecular and cellular biology of thyrotropin-releasing hormone receptors

1996 ◽  
Vol 76 (1) ◽  
pp. 175-191 ◽  
Author(s):  
M. C. Gershengorn ◽  
R. Osman
Keyword(s):  
Hormone Receptors ◽  
Three Dimensional ◽  
Binding Pocket ◽  
Amino Acid Sequences ◽  
Thyrotropin Releasing Hormone ◽  
Cellular Biology ◽  
Dimensional Structure ◽  
Releasing Hormone ◽  
G Protein Coupled ◽  
Trh Receptor

Thyrotropin-releasing hormone (TRH) receptor (TRH-R) complementary DNAs have been cloned from several species. The deduced amino acid sequences are compatible with TRH-R being a seven-transmembrane-spanning G protein-coupled receptor. These complementary DNAs and reagents derived from them have permitted detailed study of TRH-R biology at the molecular and cellular levels. Studies that have been performed since 1990 are reviewed in this article under the following headings: TRH-R gene, tissue distribution of TRH-R, primary structure of TRH-Rs, three-dimensional structure of the TRH-R binding pocket, TRH-R and G proteins, TRH-R activation, TRH desensitization, TRH-R endocytosis, and regulation of TRH-R number. It is evident that many new insights into the structure, function, and regulation of TRH-Rs have been gained in the last several years but that our understanding of these processes is incomplete. We look forward to even greater progress in the future.

scholarly journals Thyrotropin-releasing hormone receptors -- similarities and differences

2003 ◽  
Vol 30 (2) ◽  
pp. 87-97 ◽  
Author(s):  
Y Sun ◽  
X Lu ◽  
MC Gershengorn
Keyword(s):  
Hormone Receptors ◽  
Surface Membrane ◽  
Thyrotropin Releasing Hormone ◽  
Membrane Receptors ◽  
Receptor Type ◽  
Binding Affinities ◽  
Peripheral Tissues ◽  
Releasing Hormone ◽  
G Protein Coupled ◽  
Trh Receptor

Thyrotropin-releasing hormone (TRH) initiates its effects by interacting with cell-surface membrane receptors. Two G protein-coupled receptors for TRH, TRH receptor type 1 (TRH-R1) and TRH receptor type 2 (TRH-R2), have been cloned from mammals. In this review, we compare TRH-R1 and TRH-R2 with regard to their tIssue distribution, binding affinities for TRH and TRH analogs, basal and activated signaling activities and characteristics of internalization. TRH-R1 and TRH-R2 are distributed differently in the brain and peripheral tIssues, but exhibit indistinguishable binding affinities for TRH and TRH analogs. Although they both can be stimulated by TRH to similar maximal signaling levels, TRH-R2 exhibits higher basal signaling activity and is more rapidly internalized than TRH-R1. These differences in signaling and internalization properties are probably important in the distinct parts that TRH-R1 and TRH-R2 may play in mammalian physiology.

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