| Literature DB >> 15752583 |
Kate L J Ellacott1, Emma L Donald, Paul Clarkson, John Morten, Dave Masters, John Brennand, Simon M Luckman.
Abstract
The rat orphan receptor UHR-1 and its human orthologue, GPR10, were first isolated in 1995. The ligand for this receptor, prolactin-releasing peptide (PrRP), was identified in 1998 by reverse pharmacology and has subsequently been implicated in a number of physiological processes. As supported by its localization and regulation in the hypothalamus and brainstem, we have shown previously that PrRP is involved in energy homeostasis. Here we describe a naturally occurring polymorphism in the UHR-1 gene that results in an ATG to ATA change at the putative translational initiation site. The presence of the polymorphism abolished the binding of 125I PrRP in rat brain slices but did not affect the ability of PrRP to reduce fast-induced food intake. Together this data suggest that PrRP may be exerting its feeding effects through a receptor other than UHR-1.Entities:
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Year: 2005 PMID： 15752583 DOI： 10.1016/j.peptides.2004.11.020
Source DB: PubMed Journal: Peptides ISSN： 0196-9781 Impact factor: 3.750