Cloning and functional characterisation of the human TRH receptor

@article{Duthie1993CloningAF,
  title={Cloning and functional characterisation of the human TRH receptor},
  author={Sarah M. Duthie and Philip L. Taylor and L. Anderson and J V Cook and Karin Ann Eidne},
  journal={Molecular and Cellular Endocrinology},
  year={1993},
  volume={95},
  pages={R11-R15}
}
Thyrotrophin-releasing hormone (TRH) is a hypothalamic tripeptide known to act via its receptor in the anterior pituitary gland to stimulate the release of thyrotrophin (TSH) from thyrotrophs and prolactin (PRL) from lactotrophs. It is also thought to act as a neurotransmitter/neuromodulator in the central and peripheral nervous systems. We have isolated a cDNA encoding the human pituitary TRH receptor (TRH-R) protein with a predicted amino acid sequence of 398 amino acids. Comparison of the… Expand
TRH acts as a multifunctional hypophysiotropic factor in vertebrates.
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Although TRH was originally named for its ability to trigger the release of thyroid-stimulating hormone in mammals, it later became apparent that it exerts multiple, species-dependent hypophysiotropic activities, and in fish TRH stimulates growth hormone and prolactin release but does not affect TSH secretion. Expand
Molecular cloning and functional expression of a human thyrotropin-releasing hormone (TRH) receptor gene.
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All of these data further the notion that the TRH-DE is not an ordinary enzyme but a specific neuropeptidase that has been highly conserved among species. Expand
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TLDR
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Two isoforms of the thyrotropin-releasing hormone receptor generated by alternative splicing have indistinguishable functional properties.
TLDR
Functional expression in Xenopus laevis oocytes indicates that both cDNAs encode fully functional TRH receptors, and the perfect colinearity between genomic DNA and TRH-R(412) cDNA demonstrates that no other introns are present within the coding region of the TRH receptor gene. Expand
Functional expression and molecular characterization of the thyrotrophin-releasing hormone receptor from the rat anterior pituitary gland.
TLDR
The rat TRH-R protein showed considerable homology with that of the mouse, except for a deletion of 232 bp in the 3'-coding region, which did not appear to affect the functional characteristics of the receptor, as shown by electrophysiological studies with Xenopus oocytes and by transfection of the cDNA into COS-7 cells. Expand
Cloning and expression of the thyrotropin-releasing hormone receptor from GH3 rat anterior pituitary cells.
TLDR
Full functionality of the predicted 412-amino-acid receptor protein was demonstrated by functional expression of cell surface receptors in Xenopus oocytes after both cytoplasmic injection of sense RNA transcribed in vitro from this cDNA and nuclear injection of the cDNA under the control of the Herpes simplex virus thymidine kinase promoter. Expand
Distribution of thyrotrophin-releasing hormone receptor messenger RNA in rat pituitary and brain
TLDR
This study has shown for the first time the exact site of thyrotrophin-releasing hormone receptor expression in the central nervous system and these results correlate well with regions thought to possess thyrotrophic hormone recognition sites. Expand
Molecular cloning of a complementary deoxyribonucleic acid encoding the thyrotropin-releasing hormone receptor and regulation of its messenger ribonucleic acid in rat GH cells.
TLDR
It is concluded that the rat TRH receptor (rTRHR) shares high primary sequence similarity to the mouse thyrotrope TRHR, but the rTRHR has an extension of 19 amino acids at its carboxy-terminus, which is lacking in the mTRHR. Expand
Agonist-stimulated internalization of the thyrotropin-releasing hormone receptor is dependent on two domains in the receptor carboxyl terminus.
TLDR
It is concluded that rapid internalization of the TRHR is dependent on two dissimilar domains within the receptor carboxyl terminus, which are shown to affect transformation equally. Expand
Characterization of the gonadotrophin-releasing hormone receptor in alpha T3-1 pituitary gonadotroph cells.
TLDR
Results show that the GnRH receptors expressed in alpha T3-1 cells are coupled to the phosphatidylinositol second messenger pathway via a specific G-protein. Expand
Distribution of thyrotropin-releasing hormone binding sites: autoradiographic study in infant and adult human hippocampal formation
TLDR
The rostrocaudal distribution of thyrotropin-releasing hormone (TRH) binding sites was studied in the human hippocampus and a single class of high affinity [3H]MeTRH binding sites with an apparent dissociation constant in the nanomolar range has been shown both in the infant and the adult. Expand
Thyrotropin‐Releasing hormone gene expression and receptors are differentially modified in limbic foci by seizures
TLDR
Results are consistent with the hypothesis that TRH may have an important role in the pathophysiology of epilepsy by modulating excitatory processes and in situ hybridization histochemistry in the hippocampus, hippocampus, and the amygdala. Expand
Characterization of the gonadotrophin-releasing hormone calcium response in single αT3-1 pituitary gonadotroph cells
TLDR
The initial calcium response to GnRH involves both an IP3-mediated rise in cytosolic calcium due to the release from intracellular stores and an influx of extracellular calcium through second messenger-operated calcium channels. Expand
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