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Comparison of the signalling properties of the long and short isoforms of the rat thyrotropin-releasing-hormone receptor following expression in rat 1 fibroblasts



Comparison of the signalling properties of the long and short isoforms of the rat thyrotropin-releasing-hormone receptor following expression in rat 1 fibroblasts



Biochemical Journal 310: 291-298



cDNA species encoding either the long or the short isoforms of the rat thyrotropin-releasing-hormone (TRH) receptor were expressed stably in Rat 1 fibroblasts, and clones expressing specific binding of (3H)TRH were detected and expanded. Clones expressing each of these receptors at levels up to 1 pmol/mg of membrane protein were selected for analysis. Reverse-transcriptase PCR on RNA isolated from these clones confirmed that each clone expressed only mRNA corresponding to the expected splice variant. Both receptor splice variants bound (3H)TRH with a K-d of some 80 nM when binding assays were performed in the presence of guanosine 5'-(beta-gamma-imido)triphosphate. In the presence of TRH, both receptor subtypes were able to cause stimulation of inositol phosphate generation in a pertussis-toxin-insensitive manner with similar EC-50 values and to stimulate the mobilization of intracellular Ca-2+, but, despite reports that TRH receptors can also interact with the G-proteins G-s and G-i2, neither receptor splice variant was able to modulate adenylate cyclase activity in either a positive or a negative manner. These data indicate that the long and short isoforms of the rat TRH receptor have similar affinities for TRH and display similar abilities to interact with the G-q-like G-proteins, but show no ability to regulate adenylate cyclase, at least when expressed in this genetic background.

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Accession: 008363407

Download citation: RISBibTeXText

PMID: 7646458

DOI: 10.1042/bj3100291


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