HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 279, Issue 38, 39880-39885, September 17, 2004

This Article Full Text Full Text (PDF) All Versions of this Article: 279/38/39880    most recent M405624200v1 Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Humphries, J. E. Articles by Day, T. A. Search for Related Content PubMed PubMed Citation Articles by Humphries, J. E. Articles by Day, T. A. Social Bookmarking                      What's this?

Structure and Bioactivity of Neuropeptide F from the Human Parasites Schistosoma mansoni and Schistosoma japonicum^*

Judith E. Humphries, Michael J. Kimber, Yi-Wen Barton, Walter Hsu, Nikki J. Marks, Brett Greer, Pat Harriott, Aaron G. Maule, and Tim A. Day¶

From the Department of Biomedical Sciences and Neuroscience Program, Iowa State University, Ames, Iowa 50011 and Parasitology Research Group, School of Biology and Biochemistry, Queen's University Belfast, Belfast BT9 7BL, United Kingdom

The blood flukes Schistosoma mansoni and Schistosoma japonicum inflict immense suffering as agents of human schistosomiasis. Previous investigations have found the nervous systems of these worms contain abundant immunoreactivity to antisera targeting invertebrate neuropeptide Fs (NPFs) as well as structurally similar neuropeptides of the mammalian neuropeptide Y (NPY) family. Here, cDNAs encoding NPF in these worms were identified, and the mature neuropeptides from the two species differed by only a single amino acid. Both neuropeptides feature the characteristics common among NPFs; they are 36 amino acids long with a carboxyl-terminal Gly-Arg-X-Arg-Phe-amide and Tyr residues at positions 10 and 17 from the carboxyl terminus. Synthetic S. mansoni NPF potently inhibits the forskolin-stimulated accumulation of cAMP in worm homogenates, with significant effects at 10^-11 M. This is the first demonstration of an endogenous inhibition of cAMP by an NPF, and because this is the predominant pathway associated with vertebrate NPY family peptides, it demonstrates a conservation of downstream signaling pathways used by NPFs and NPY peptides.

Received for publication, May 20, 2004 , and in revised form, June 28, 2004.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY299474, AY533028, AY662954.

^* This work was supported by National Institutes of Health Grant R01-AI49162 (to T. A. D. and A. G. M.) and an Iowa Healthy Livestock Initiative grant (to T. A. D. and M. J. K.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence should be addressed. Tel.: 515-294-7100; Fax: 515-294-3415; E-mail: day{at}iastate.edu.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?