@article {1738, title = {Gene organization and expression of a neuropeptide Y homolog from the land planarian Arthurdendyus triangulatus}, journal = {J Comp Neurol}, volume = {454}, year = {2002}, month = {2002 Dec 02}, pages = {58-64}, abstract = {

Neuropeptide Y is one of the most widespread regulatory peptides within the vertebrate nervous system and shares the C-terminal motif [FY]-x(3)-[LIVM]-x(2)-Y-x(3)-[LIVMFY]-x-R-x-R-[YF] with pancreatic polypeptide, peptide YY, and fish pancreatic peptide Y. All four peptides are believed to have arisen from a single ancestral gene through successive gene duplication events in vertebrates. The origin of this peptide family may date back further still; similarly sized peptide transmitters with an identical C-terminal motif have been identified in molluscs and flatworms and designated neuropeptide F (NPF). Cloning of the npf gene from the parasitic flatworm Moniezia expansa identified some unusual features within the peptide precursor organization but, at the same time, provided support for an evolutionary relationship of npf and npy genes through the presence of a single intron at a conserved position. To extend the analysis of the evolutionary relationships between invertebrate NPF and vertebrate NPY family peptides, the NPF precursor from the turbellarian Arthurdendyus triangulatus was characterized. Sequence analysis revealed the npf transcript to be 362 base pairs in length encoding a single open reading frame of 81 amino acids. The precursor comprises a signal peptide followed by the mature peptide of 36 amino acids in length, terminating in the typical invertebrate GRPRF motif, followed by a carboxyterminal glycyl extension. The NPF precursor of A. triangulatus shows significant similarities to the vertebrate NPY peptides. Indeed, the N-terminus of A. triangulatus prepro-NPF corresponds more closely to that of the vertebrate peptide homologs than to that of other invertebrate NPFs isolated to date. Immunocytochemical localization studies have demonstrated NPF immunoreactivity throughout the nervous system of A. triangulatus, particularly in association with muscular structures. The data support an early evolutionary origin for this peptide transmitter family within the nervous system of basal bilaterians.

}, keywords = {Amino Acid Sequence, Animals, Base Sequence, DNA, Complementary, Genomic Library, Helminth Proteins, Introns, Molecular Sequence Data, Nervous system, Neuropeptide Y, Organ Specificity, planarians, Reverse Transcriptase Polymerase Chain Reaction, Sequence Analysis, DNA, Sequence Homology, Amino Acid}, issn = {0021-9967}, doi = {10.1002/cne.10440}, author = {Dougan, Paula M and Mair, Gunnar R and Halton, David W and Curry, W James and Day, Tim A and Maule, Aaron G} } @article {1734, title = {Neuropeptide F: primary structure from the tubellarian, Artioposthia triangulata.}, journal = {Comp Biochem Physiol C}, volume = {101}, year = {1992}, month = {1992 Feb}, pages = {269-74}, abstract = {

1. A neuropeptide exhibiting vertebrate pancreatic polypeptide immunoreactivity has been isolated and sequenced from extracts of the terrestrial turbellarian, Artioposthia triangulata. 2. This neuropeptide, designated neuropeptide F, consists of 36 amino acid residues terminating in a phenylalaninamide. 3. The full primary structure was established as: KVVHLRPRSSFSSEDEYQIYLRNVSKYIQLYGRPRF.NH2. The molecular mass, deduced from this sequence, was 4433 Da. 4. This neuropeptide exhibits C-terminal homology with neuropeptide F (Moniezia expansa) and with the vertebrate neuropeptide Y/pancreatic polypeptide superfamily of which it may represent a phylogenetic precursor.

}, keywords = {Amino Acid Sequence, Animals, Helminth Proteins, Immunohistochemistry, Mass Spectrometry, Molecular Sequence Data, Molecular Weight, Neuropeptide Y, Neuropeptides, Pancreatic Polypeptide, Platyhelminths, Sequence Homology, Nucleic Acid}, issn = {0742-8413}, author = {Curry, W J and Shaw, C and Johnston, C F and Thim, L and Buchanan, K D} }