Campus Units

Biomedical Sciences, Neuroscience

Document Type

Article

Publication Version

Published Version

Publication Date

9-17-2004

Journal or Book Title

The Journal of Biological Chemistry

Volume

279

First Page

39880

Last Page

39885

DOI

10.1074/jbc.M405624200

Abstract

The blood flukes Schistosoma mansoni and Schistosoma japonicuminflict 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.

Comments

This research was originally published in The Journal of Biological Chemistry. 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. Structure and Bioactivity of Neuropeptide F from the Human Parasites Schistosoma mansoni and Schistosoma japonicum. Journal of Biological Chemistry. 2004; 279:39880–39885. © the American Society for Biochemistry and Molecular Biology.

Copyright Owner

American Society for Biochemistry and Molecular Biology

Language

en

File Format

application/pdf

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