Structure and bioactivity of neuropeptide F from the human parasites Schistosoma mansoni and Schistosoma japonicum

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dc.contributor.author Humphries, Judith E.
dc.contributor.author Kimber, Michael J.
dc.contributor.author Barton, Yi-Wen
dc.contributor.author Hsu, Walter
dc.contributor.author Marks, Nikki J.
dc.contributor.author Greer, Brett
dc.contributor.author Harriott, Pat
dc.contributor.author Maule, Aaron G.
dc.contributor.author Day, Tim A.
dc.date.accessioned 2008-12-15T09:37:18Z
dc.date.available 2008-12-15T09:37:18Z
dc.date.issued 2004-09-17
dc.identifier.citation Humphries , J E , Kimber , M J , Barton , Y-W , Hsu , W , Marks , N J , Greer , B , Harriott , P , Maule , A G & Day , T A 2004 , ' Structure and bioactivity of neuropeptide F from the human parasites Schistosoma mansoni and Schistosoma japonicum ' Journal of Biological Chemistry , vol 279 , pp. 39880-39885 . en
dc.identifier.issn 1083-351X
dc.identifier.other PURE: 92979
dc.identifier.other dspace: 2160/1602
dc.identifier.uri http://hdl.handle.net/2160/1602
dc.identifier.uri http://www.jbc.org/cgi/content/full/279/38/39880 en
dc.description Humphries, J. E., Kimber, M. J., Barton, Y-W., Hsu, W., Marks, N. J., Greer, B., Harriott, P., Maule, A. G., Day, T. A. (2004). Structure and bioactivity of neuropeptide F from the human parasites Schistosoma mansoni and Schistosoma japonicum. Journal of Biological Chemistry, 279, 39880-39885. Sponsorship: National Institutes of Health Grant R01-AI49162 /Iowa Healthy Livestock Initiative grant RAE2008 en
dc.description.abstract 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. en
dc.format.extent 6 en
dc.language.iso eng
dc.relation.ispartof Journal of Biological Chemistry en
dc.title Structure and bioactivity of neuropeptide F from the human parasites Schistosoma mansoni and Schistosoma japonicum en
dc.type Text en
dc.type.publicationtype Article (Journal) en
dc.identifier.doi http://dx.doi.org/10.1074/jbc.M405624200
dc.contributor.institution Aberystwyth University en
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en


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