FMRFamide-related peptides have been isolated from both invertebrates and vertebrates and exhibit a wide range of biological effects in rats. We show here that in humans 2 FMRFamide-related peptides are encoded by a single gene expressed as a spliced mRNA. The larger predicted peptide (AGEGLNSQFWSLAAPQRFamide) differs from the peptide isolated from bovines (AGEGLSSPFWSLAAPQRFamide) by the substitutions of 2 amino acids. The shorter predicted peptide (NPSF, SQAFLFQPQRFamide) is 3 amino acids longer than the bovine 8 amino-acid NPFF (FLFQPQRFamide) or the human NPFF peptide isolated from serum [5], suggesting that the encoded protein is subject to cleavage by a tripeptidyl peptidase or by a novel processing mechanism. On rat spinal cord, the larger peptide is indistinguishable in activity from the equivalent bovine peptide whereas the smaller extended peptide is inactive.
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http://dx.doi.org/10.1016/s0014-5793(97)00557-7 | DOI Listing |
Biosci Biotechnol Biochem
January 2025
Department of Agricultural Science, Graduate School of Sustainability Science.
FMRFamide-like peptides (FLPs) and their receptors FMRFamide-related peptide receptors (FRPRs) are widely conserved in free-living and parasitic nematodes. Herein, we identified FRPR-1 as a of FLP-1 receptor candidate involved in larval development and diapause in the model nematode Caenorhabditis elegans. Our molecular genetic study, supported by in silico research, revealed the following: 1) frpr-1 loss-of-function completely suppresses the promotion of larval diapause caused by flp-1 overexpression; 2) AlphaFold2 analysis revealed the binding of FLP-1 to FRPR-1; 3) FRPR-1 as well as FLP-1modulates the production and secretion of the predominant insulin-like peptide DAF-28, which is produced in ASI neurons; and 4) the suppression of larval diapause by frpr-1 loss-of-function is completely suppressed by a daf-28 defect.
View Article and Find Full Text PDFMicroPubl Biol
September 2023
Biology, City College of New York, CUNY.
Parasitic nematodes infect and cause morbidity in over one billion people worldwide, with current anthelmintic drugs decreasing in efficacy. To date, nematodes produce more types of neuropeptides than any other animal. We are interested in the role of neuropeptide signaling systems as a possible target for new anthelmintic drugs.
View Article and Find Full Text PDFBiomolecules
January 2023
Department of Fisheries Science, Chonnam National University, Yeosu 59626, Republic of Korea.
FMRFamide-related peptides are neuropeptides involved in a wide range of biological processes, including reproduction and larval development. To characterize the involvement of FMRFamide in the reproduction and larval development of Pacific abalone , an FMRFamide cDNA () was cloned from the cerebral ganglion (CG). Fluorescence in situ hybridization and qRT-PCR were performed for functional characterization.
View Article and Find Full Text PDFZoology (Jena)
December 2022
A.N. Severtsov Institute of Ecology and Evolution of Russian Academy of Sciences, Leninsky pr. 33, Moscow 119071, Russia; Institute of Zoology of Scientific Center for Zoology and Hydroecology, National Academy of Sciences of Republic of Armenia, P. Sevaka str.,7, Yerevan 0014, Armenia. Electronic address:
The parasitic flatworm, trematoda Dicrocoelium lanceatum or lancet fluke is the causative agent of a widespread parasite disease of grazing ruminants, dicrocoeliosis. The aim of this work is the study of the presence and localization of neuropeptide FMRFamide immunoreactive elements in the nervous system of D. lanceatum using immunocytochemical technique and confocal scanning laser microscopy.
View Article and Find Full Text PDFFront Biosci (Landmark Ed)
May 2022
Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI 48109-0660, USA.
Background: The structures and activities of invertebrate sulfakinins that influence gut motility and heart rate are like the vertebrate cholecystokinin (CCK) peptides. Typical of sulfakinin precursors encodes non-sulfated drosulfakinin I (nsDSK I; FDDYGHMRF-NH2) and nsDSK II (GGDDQFDDYGHMRF-NH2) that bind DSK-R1 and DSK-R2. To explore the role of the nsDSK II N-terminal extension (GGDDQ) in gut we delineated its structure-activity relationship (SAR) and identified novel agonists.
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