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Vasoactive intestinal polypeptide binds with high affinity to non-small cell lung cancer cells and elevates cyclic AMP levels.

作者信息

Lee M, Jensen R T, Huang S C, Bepler G, Korman L, Moody T W

机构信息

Department of Biochemistry and Molecular Biology, George Washington University School of Medicine and Health Sciences, Washington, DC 20037.

出版信息

Peptides. 1990 Nov-Dec;11(6):1205-9. doi: 10.1016/0196-9781(90)90153-v.

Abstract

Vasoactive intestinal polypeptide (VIP) receptors were characterized on non-small cell lung cancer (NSCLC) cells. 125I-VIP bound specifically to membranes derived from 6 NSCLC cell lines. Specific 125I-VIP was time dependent and a linear function of EPLC-65H membrane concentration. 125I-VIP bound with high (Kd = 0.2 nM) and moderate (Kd = 39 nM) affinity to two classes of sites. Pharmacology studies indicated that the order of peptide potency was VIP greater than rGHRH greater than PHI = helodermin greater than secretin greater than glucagon. Also VIP elevated the cAMP levels 10-fold using cell line ADLC-5M2. These data indicate that functional VIP receptors are present on NSCLC cells.

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