Abstract
Corticotropin-releasing factor (CRF) receptors in IMR-32 human neuroblastoma cells were characterized after differentiation with 2.5 μM 5′-bromo-2′-deoxyuridine for 10 days. Scatchard analysis of [ 125I-Tyr 0]ovine CRF binding revealed a high affinity binding site with a dissociation constant of 0.59 nM and a maximum binding capacity of 142 fmol/mg, the affinity of which was decreased by guanosine 5′- o-(3-thiotriphosphate). This binding was displaced in the following order of potency: human/rat CRF > ovine CRF > urotensin I > sauvagine > bovine CRF > [ d-Phe 12,Nle 21.38,C α-MeLeu 37]human/rat CRF-(12-41) > α-helical CRF-(9-41), indicative of the CRF 1 receptor subtype. Functional coupling of this receptor was confirmed by CRF-induced increases in cyclic AMP, which were antagonised by α-helical CRF-(9-41) and [ d-Phe 12,Nle 21.38,C α-MeLeu 37]human/rat CRF-(12-41).
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