High affinity binding of cholecystokinin to small cell lung cancer cells |
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| Authors: | D G Yoder T W Moody |
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| Affiliation: | 1. Department of Radiation Oncology, Gustave Roussy Cancer Campus, Villejuif, France;2. Department of Medical Oncology, Gustave Roussy Cancer Campus, Villejuif, France;3. Department of Medical Oncology, Hôpital d’Instruction des Armées Bégin, Saint Mandé, France;4. Institut de Recherche Biomédicale des Armées, Brétigny sur Orge, France;2. Sir Peter MacCallum Dept of Oncology, The University of Melbourne, Melbourne, Australia |
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| Abstract: | The binding of 125I-Bolton Hunter-cholecystokinin octapeptide (125I-BH-CCK-8) to small cell lung cancer cell lines was investigated. 125I-BH-CCK-8 bound with high affinity (Kd = 2.4 nM) to an apparent single class of sites (1700/cell) using cell line NCI-H209. Binding was time dependent and the ratio of specific/nonspecific binding was 8/1. Pharmacology studies indicated that gastrin, caerulein, CCK-33 and nonsulfated CCK-8 were potent inhibitors of specific 125I-BH-CCK-8 binding whereas CCK-26-32-NH2 was not. Because CCK receptors are present on small cell lung cancer cells, CCK may function as a regulatory peptide in this disease. |
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