High affinity binding of cholecystokinin to small cell lung cancer cells.
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.
D018288:Carcinoma, Small Cell / Q000378:metabolism*; D002460:Cell Line; D002766:Cholecystokinin / Q000378:metabolism / Q000031:analogs & derivatives; D005755:Gastrins / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D008175:Lung Neoplasms / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism; D011949:Receptors, Cholecystokinin / Q000378:metabolism*; D012844:Sincalide / Q000031:analogs & derivatives / Q000378:metabolism*; D013388:Succinimides / Q000378:metabolism; D013758:Tetragastrin / Q000378:metabolism
C044758:Bolton Hunter-cholecystokinin octapeptide; D005755:Gastrins; D010446:Peptide Fragments; D011949:Receptors, Cholecystokinin; D013388:Succinimides; D013758:Tetragastrin; C038242:cholecystokinin (27-32)-amide; D002766:Cholecystokinin; C036227:gastrin I; D012844:Sincalide