Svoboda M, Tastenoy M, Van Rampelbergh J, Goossens J F, De Neef P, Waelbroeck M, Robberecht P
Department of Biochemistry and Nutrition, Medical School, Université Libre de Bruxelles, Belgium.
Biochem Biophys Res Commun. 1994 Dec 30;205(3):1617-24. doi: 10.1006/bbrc.1994.2852.
We have cloned and sequenced a cDNA isolated from a human SUP-T1 lymphoblast cell line library. It encoded a 457 amino acids protein having 87% identity with the rat PACAP type II, VIP2 receptor. Chinese hamster ovary (CHO) cells stably transfected with cloned cDNA expressed a specific binding of 125I[Acetyl-His1]PACAP-27. This binding was inhibited by GTP, and by the peptides helodermin, VIP, PACAP-27 and PACAP-38 that also stimulated adenylate cyclase activity. The order of potency was PACAP-38 > VIP > or = helodermin > or = PACAP-27. Comparison of the results in two cell lines expressing different receptor densities suggested that helodermin and PACAP-38 had a higher intrinsic activity than VIP and PACAP-27.
我们已经克隆并测序了从人SUP-T1淋巴母细胞系文库中分离出的一个cDNA。它编码一种由457个氨基酸组成的蛋白质，与大鼠PACAP II型VIP2受体有87%的同源性。用克隆的cDNA稳定转染的中国仓鼠卵巢（CHO）细胞表达了125I[乙酰基 - 组氨酸1]PACAP - 27的特异性结合。这种结合被GTP以及也能刺激腺苷酸环化酶活性的肽类海洛德明、VIP、PACAP - 27和PACAP - 38所抑制。其效力顺序为PACAP - 38 > VIP ≥ 海洛德明 ≥ PACAP - 27。在表达不同受体密度的两种细胞系中的结果比较表明，海洛德明和PACAP - 38比VIP和PACAP - 27具有更高的内在活性。
