Nachman R J, Holman G M, Cook B J, Haddon W F, Ling N
Biochem Biophys Res Commun. 1986 Oct 15;140(1):357-64. doi: 10.1016/0006-291x(86)91098-3.
A sulfated neuropeptide [pGlu-Ser-Asp-Asp-Tyr(SO3H)-Gly-His-Met-Arg-Phe-NH2], with a blocked N-terminus and related to the undecapeptide leucosulfakinin, has been isolated from head extracts of the cockroach, Leucophaea maderae. It exhibits sequence homology with the hormonally-active portion of vertebrate hormones cholecystokinin, human gastrin II and caerulin. This peptide, termed leucosulfakinin-II, shares a common C-terminal heptapeptide fragment with leucosulfakinin and a comparison of the two sequences provides an assessment of the importance of the constituent amino acids to biological activity. Leucosulfakinin-II shows a greater resemblance to cholecystokinin than does leucosulfakinin. Leucosulfakinin-II and leucosulfakinin are the only two reported invertebrate sulfated neuropeptides. As with leucosulfakinin, the intestinal myotropic activity of leucosulfakinin-II is analogous to that of gastrin and cholecystokinin. The sequence homology between the leucosulfakinins and the vertebrate hormones, as well as their analogous myotropic activity, suggest that gastrin/cholecystokinin-like neuropeptides are not confined to vertebrates, but also occur in invertebrates.
一种硫酸化神经肽[pGlu-Ser-Asp-Asp-Tyr(SO3H)-Gly-His-Met-Arg-Phe-NH2],其N端封闭,与十一肽亮氨酸硫酸激肽相关,已从德国蜚蠊的头部提取物中分离出来。它与脊椎动物激素胆囊收缩素、人胃泌素II和蛙皮素的激素活性部分表现出序列同源性。这种肽被称为亮氨酸硫酸激肽-II,与亮氨酸硫酸激肽共享一个共同的C端七肽片段,对这两个序列的比较提供了对组成氨基酸对生物活性重要性的评估。亮氨酸硫酸激肽-II比亮氨酸硫酸激肽与胆囊收缩素的相似性更高。亮氨酸硫酸激肽-II和亮氨酸硫酸激肽是仅有的两种已报道的无脊椎动物硫酸化神经肽。与亮氨酸硫酸激肽一样,亮氨酸硫酸激肽-II的肠促肌活性类似于胃泌素和胆囊收缩素。亮氨酸硫酸激肽与脊椎动物激素之间的序列同源性以及它们类似的促肌活性表明,胃泌素/胆囊收缩素样神经肽不仅存在于脊椎动物中,也存在于无脊椎动物中。