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

Aaron Maule, T.A. Day, J.E. Humphries, P. Harriott, M.J. Kimber, E. Barton, W. Hsu, N.J. Marks, B. Greer

Research output: Contribution to journalArticle

27 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)39880-39885
Number of pages6
JournalJournal of Biological Chemistry
Volume279(38)
Issue number38
DOIs
Publication statusPublished - 17 Sep 2004

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'Structure and bioactivity of neuropeptide F from the human parasites Schistosoma mansoni and Schistosoma japonicum'. Together they form a unique fingerprint.

  • Cite this