High affinity binding of cholecystokinin to small cell lung cancer cells (original) (raw)

affinity binding of cholecystokinin to small cell lung cancer cells. PEPTIDES 8(1) 103-107, 1987.-The binding of '2'~I-Bolton Hunter-cholecystokinin octapeptide ('2'~I-BH-CCK-8) to small cell lung cancer cell lines was investigated. ~zSI-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 ~2~I-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. CCK CCK receptors Small cell lung cancer Neuroendocrine peptides