| Literature DB >> 3778455 |
R J Nachman, G M Holman, B J Cook, W F Haddon, N Ling.
Abstract
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.Entities:
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Year: 1986 PMID: 3778455 DOI: 10.1016/0006-291x(86)91098-3
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575