We have identified and characterized a cDNA encoding a novel isoform of the corticotropin-releasing factor (CRF) receptor, referred to as CRF2α-tr, from the rat amygdala cDNA library. The nucleotide sequence of the cloned cDNA has a structure of an alternatively spliced form of the CRF2α receptor, which contains unspliced introns 6 and 7 in the message, and encodes a 236-amino-acid truncated protein that comprises three unique transmembrane domains. Northern blot analysis shows that the CRF2α-tr receptor is more strongly expressed in the rat amygdala, thalamus, and hypothalamus than the intact CRF2α receptor. Western blot analysis also reveals that the CRF2α-tr protein can be expressed in transfected COS-7 cells as well as CRF2α. Furthermore, this receptor binds rat/human CRF with almost the same low affinity ( K d = 12.7 nM) as the CRF2α and without accumulation of intracellular cAMP. Interestingly, it does not bind sauvagine or rat urocortin. These findings suggest that this truncated CRF receptor is the major isoform of CRF2α receptor mRNA transcripts in the amygdala and would mediate some functions of CRF pathways in the central nervous system.
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Cloning and Characterization of a Short Variant of the Corticotropin-Releasing Factor Receptor Subtype from Rat Amygdala
Miyata, Ichiro; Shiota, Chiyo; Ikeda, Yoko; Oshida, Yuichi; Chaki, Shigeyuki; Okuyama, Shigeru; Inagami, Tadashi
Follow Biochemical and Biophysical Research Communications
, Volume 256 (3)
Elsevier – Mar 24, 1999
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