Document Detail


Analogs of sulfakinin-related peptides demonstrate reduction in food intake in the red flour beetle, Tribolium castaneum, while putative antagonists increase consumption.
MedLine Citation:
PMID:  23246802     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
The insect sulfakinins (SKs) constitute a family of neuropeptides that display both structural and functional similarities to the mammalian hormones gastrin and cholecystokinin (CCK). As a multifunctional neuropeptide, SKs are involved in muscle contractions as well as food intake regulation in many insects. In the red flour beetle Tribolium castaneum, the action on food intake by a series of synthetic SK analogs and one putative antagonist was investigated by injection in beetle adults. The most remarkable result was that both sulfated and non-sulfated SKs [FDDY(SO(3)H)GHMRFamide] inhibited food intake by about 70%. Strong activity observed for SK analogs featuring a residue that mimics the acidic nature of Tyr(SO(3)H) but lack the phenyl ring of Tyr, indicate that aromaticity is not a critical characteristic for this position of the peptide. SK demonstrated considerable tolerance to Ser and Ala substitution in position 8 (basic Arg), as analogs featuring these uncharged substitutions retained almost all of the food intake inhibitory activity. Also, the Phe in position 1 could be replaced by Ser without complete loss of activity. Conversely, substitution of Met by Nle in position 3 led to inactive compounds. Finally, the Caenorhabditis elegans sulfated neuropeptide-like protein-12 (NLP-12), that shares some sequence similarities with the SKs but features a Gln-Phe-amide rather than an Arg-Phe-amide at the C-terminus, elicited increased food intake in T. castaneum, which may indicate an antagonist activity. Co-injection NLP-12 with nsSK blocked the food intake inhibitory effects of nsSK.
Authors:
Na Yu; Veronica Benzi; Moises João Zotti; Dorien Staljanssens; Krzysztof Kaczmarek; Janusz Zabrocki; Ronald J Nachman; Guy Smagghe
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-12-11
Journal Detail:
Title:  Peptides     Volume:  -     ISSN:  1873-5169     ISO Abbreviation:  Peptides     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-12-18     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8008690     Medline TA:  Peptides     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2012. Published by Elsevier Inc.
Affiliation:
Department of Crop Protection, Faculty of Bioscience Engineering, Ghent University, 9000 Ghent, Belgium.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Dynamics of gas micronuclei formed on a flat hydrophobic surface, the predecessors of decompression ...
Next Document:  Out-of-field beam characteristics of a 6MV photon beam: Results of a Monte Carlo study.