In this study we characterized calcitonin (CT) receptors in human neuroblas
toma IMR 32 cells. Saturation binding assays indicated that [I-125]-human C
T bound with high affinity to IMR 32 cell membranes (K-d = 253.6 PM; B-max
= 3.84 fmol/ mg protein). In competition binding studies, human adrenomedul
lin displayed high affinity for these sites (IC50 = 30 nM) whereas human al
pha calcitonin-gene related peptide (alpha CGRP; IC50 = 145 nM) and human a
mylin (IC50 = 415 nM) showed lower affinity. These peptides increased cAMP
levels in viable cells; the relative potencies were: human CT > human adren
omedullin > human alpha CGRP greater than or equal to human amylin. The exp
ression of mRNA coding for the published sequences of the human calcitonin
receptor and of the human calcitonin receptor-like receptor was evaluated b
y reverse transcriptase-polymerase chain reaction. Electrophoretic analysis
did not confirm the occurrence of mRNA coding for the above mentioned rece
ptors in these cells. This study suggests the presence of a novel, putative
CT receptor in IMR 32 cells. (C) 1999 Elsevier Science Ireland Ltd. All ri
ghts reserved.