QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) All Versions of this Article: jpet.102.047118v1 305/3/825    most recent Submit a response Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Engström, M. Articles by Panula, P. Search for Related Content PubMed PubMed Citation Articles by Engström, M. Articles by Panula, P. Pubmed/NCBI databases Gene GEO Profiles HomoloGene Protein UniGene Compound via MeSH Substance via MeSH

NEUROPHARMACOLOGY

Prolactin Releasing Peptide Has High Affinity and Efficacy at Neuropeptide FF2 Receptors

Juvantia Pharma Ltd., Turku, Finland (M.E., S.W., J.-M.S.); Department of Biology, åbo Akademi University, Turku, Finland (A.B., P.P.); and Institute of Biomedicine/Anatomy, University of Helsinki, Helsinki, Finland (P.P.)

Neuropeptide FF (NPFF) and prolactin-releasing peptide (PrRP) are two members of the RFamide peptide family. In this study we investigated whether these RFamide peptides, which have common structural features in their C-terminal RFamide motif and share several physiologically important functions, could exert their effects through the same set of receptors. The affinity and functional activity of several related RFamide peptides were determined at the human neuropeptide FF receptor subtype 2 (hNPFF2) and the human prolactin-releasing peptide (hPrRP) receptors. The full-length human prolactin releasing peptide 31 (hPrRP31) had significantly higher efficacy compared with NPFF and its stable analog, (1DMe)Y8Fa, at the hNPFF2 receptor. In contrast, NPFF and (1DMe)Y8Fa were not efficacious at the hPrRP receptor. Our study indicated a generally relatively low level of discrimination for RFamide peptides at the NPFF receptor, whereas the hPrRP receptor clearly preferred PrRP or very closely related peptides. The seemingly promiscuous binding of the RFamide peptides to the NPFF receptor was further confirmed by receptor autoradiography. PrRP may thus signal through the NPFF receptors in vivo.

Address correspondence to: Mia Engström, Lemminkäisenkatu 5, FIN-20520 Turku, Finland; e-mail: mia.engstrom{at}juvantia.com

This article has been cited by other articles:

				J. H. Jhamandas, F. Simonin, J.-J. Bourguignon, and K. H. Harris Neuropeptide FF and neuropeptide VF inhibit GABAergic neurotransmission in parvocellular neurons of the rat hypothalamic paraventricular nucleus Am J Physiol Regulatory Integrative Comp Physiol, May 1, 2007; 292(5): R1872 - R1880. [Abstract] [Full Text] [PDF]

				D. A Bechtold and S. M Luckman The role of RFamide peptides in feeding J. Endocrinol., January 1, 2007; 192(1): 3 - 15. [Abstract] [Full Text] [PDF]

				D. A. Bechtold and S. M. Luckman Prolactin-Releasing Peptide Mediates Cholecystokinin-Induced Satiety in Mice Endocrinology, October 1, 2006; 147(10): 4723 - 4729. [Abstract] [Full Text] [PDF]

				M. Engstrom, J.-M. Savola, and S. Wurster Differential Efficacies of Somatostatin Receptor Agonists for G-Protein Activation and Desensitization of Somatostatin Receptor Subtype 4-Mediated Responses J. Pharmacol. Exp. Ther., March 1, 2006; 316(3): 1262 - 1268. [Abstract] [Full Text] [PDF]

				M. Engstrom, J. Tomperi, K. El-Darwish, M. Ahman, J.-M. Savola, and S. Wurster Superagonism at the Human Somatostatin Receptor Subtype 4 J. Pharmacol. Exp. Ther., January 1, 2005; 312(1): 332 - 338. [Abstract] [Full Text] [PDF]

				G. J. Dockray The expanding family of -RFamide peptides and their effects on feeding behaviour Exp Physiol, May 1, 2004; 89(3): 229 - 235. [Abstract] [Full Text] [PDF]