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Vol. 293, Issue 3, 788-798, June 2000
1-Receptors: Novel
Regulatory Mechanism Affecting Intracellular Ca2+
Concentration1
Cellular Pathobiology Unit, Intramural Research Program, National
Institute on Drug Abuse, National Institutes of Health, Baltimore,
Maryland (T.H., T.-P.S.); and Institut National de la Santé et de
la Recherche Médicale, Unité 336-Développement,
Vieillissement et Plasticité du Système Nerveux, Montpellier,
France (T.M.)
The 
1-receptor is a one-transmembrane endoplasmic
reticulum protein that binds neurosteroids and dextrorotatory
benzomorphans. The roles of 1-receptors in regulating
intracellular Ca2+ in NG108 cells were examined in this
study. 1-Ligands pregnenolone sulfate, (+)-pentazocine,
and 2-(4-morpholino)ethyl-1-phenylcyclohexane-1-carboxylate hydrochloride modulate Ca2+ signaling in NG108 cells via
two modes of action. First, nanomolar concentrations of the ligands,
without effect by themselves, potentiated the bradykinin-induced
increase of the cytosolic free Ca2+ concentration in a
bell-shaped manner. This effect of 1-ligands was
unaffected by depletion of Ca2+ from perfusion buffer and
was blocked by a 21-mer antisense oligodeoxynucleotide against the
cloned 1-receptors. Second, after the cells were depleted of the endoplasmic reticulum Ca2+ stores, the
depolarization (75 mM KCl)-induced increase in cytosolic free
Ca2+ was potentiated by
2-(4-morpholino)ethyl-1-phenylcyclohexane-1-carboxylate hydrochloride,
whereas it was inhibited by pregnenolone sulfate and (+)-pentazocine.
These effects, albeit opposite in direction, were blocked by both the
21-mer antisense oligodeoxynucleotide and pertussis toxin. Western
blotting indicates that 1-receptors are increased on the
plasma membrane and the nuclear membrane in the presence of
1-ligand. These results suggest that Ca2+
signaling via 1-receptors may represent a novel
mechanism that affects intracellular Ca2+ concentrations.
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