Staley J, Jensen R T, Moody T W
Department of Biochemistry and Molecular Biology, George Washington University School of Medicine and Health Sciences, Washington, DC 20037.
Peptides. 1990 Sep-Oct;11(5):1033-6. doi: 10.1016/0196-9781(90)90029-5.
The ability of cholecystokinin (CCK) receptor antagonists to interact with CCK receptors in small cell lung cancer (SCLC) cells was investigated. L-365,260, CCK-8, L-364,718, CBZ-CCK(27-32)-NH2 and proglumide analogue 10 inhibited specific 125I-CCK-8 binding to SCLC cells with IC50 values of 0.2, 2, 500, 100,000 and 500,000 nM, respectively. Gastrin-I and CCK-8 elevated the cytosolic Ca2+ when SCLC cells were loaded with Fura 2-AM. L-365,260 inhibited the cytosolic Ca2+ increase caused by 10 nM CCK-8 in a dose-dependent manner. The effects of 10 nM L-365,260 were reversed by high concentrations of CCK-8. These data indicate that L-365,260 functions as a reversible CCK-8 antagonist using SCLC cells.
研究了胆囊收缩素（CCK）受体拮抗剂与小细胞肺癌（SCLC）细胞中CCK受体相互作用的能力。L-365,260、CCK-8、L-364,718、CBZ-CCK(27 - 32)-NH2和丙谷胺类似物10抑制125I-CCK-8与SCLC细胞的特异性结合，IC50值分别为0.2、2、500、100,000和500,000 nM。当SCLC细胞用Fura 2-AM负载时，胃泌素-I和CCK-8可升高胞质Ca2+。L-365,260以剂量依赖的方式抑制10 nM CCK-8引起的胞质Ca2+增加。高浓度的CCK-8可逆转10 nM L-365,260的作用。这些数据表明，L-365,260在SCLC细胞中作为一种可逆的CCK-8拮抗剂发挥作用。
