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Modulation of calcitonin binding by calcium: differential effects of divalent cations



Modulation of calcitonin binding by calcium: differential effects of divalent cations



Journal of Receptor Research 13(8): 1173-1197



Binding of salmon calcitonin to bovine hypothalamic membranes is enhanced about 25% by calcium with a half-maximal effect at 15 mM calcium. In contrast, membranes prepared from a cell line expressing a recombinant human calcitonin receptor show no effect of calcium under similar conditions. The hypothalamic calcitonin receptor solubilized with CHAPS detergent retains an apparent Kd of 0.3 nM for salmon calcitonin; however, binding of calcitonin to the detergent-solubilized receptor complex can be inhibited by divalent cations in order of potency Mn gt Ca apprxeq Sr apprxeq Mg mchgt NaCl with Mn and Ca having apparent Ki's of 5 mM and 20 mM respectively. Dixon and Scatchard plots of Mn and Ca inhibition of binding to the soluble receptor complex suggest a noncompetitive mechanism of inhibition. Calcium also inhibits calcitonin binding to a detergent-solubilized recombinant human calcitonin receptor. Inhibition of calcitonin binding is observed using two independent methods for determining soluble receptor-hormone complex and inhibition is reversed by EDTA. These data suggest that a low-affinity divalent-cation binding site exists on the calcitonin receptor complex with a binding preference for calcium and manganese. Binding of calcium to this site can perturb the binding of calcitonin. This divalent-cation site may be an important structural component of the calcitonin receptor complex and have a potential physiological role in regions of high extracellular calcium such as at sites of bone resorption.

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Accession: 009035672

Download citation: RISBibTeXText

PMID: 8254582

DOI: 10.3109/10799899309063271


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