Molecular evolution of GPCRs

26Rfa/GPR103

Kazuyoshi Ukena, Tomohiro Osugi, Jérôme Leprince, Hubert Vaudry, Kazuyoshi Tsutsui

    Research output: Contribution to journalArticle

    19 Citations (Scopus)

    Abstract

    Neuropeptides possessing the Arg-Phe-NH2 (RFamide) motif at their C-termini (designated as RFamide peptides) have been characterized in a variety of animals. Among these, neuropeptide 26RFa (also termed QRFP) is the latest member of the RFamide peptide family to be discovered in the hypothalamus of vertebrates. The neuropeptide 26RFa/QRFP is a 26-amino acid residue peptide that was originally identified in the frog brain. It has been shown to exert orexigenic activity in mammals and to be a ligand for the previously identified orphan G protein-coupled receptor, GPR103 (QRFPR). The cDNAs encoding 26RFa/QRFP and QRFPR have now been characterized in representative species of mammals, birds, and fish. Functional studies have shown that, in mammals, the 26RFa/QRFP-QRFPR system may regulate various functions, including food intake, energy homeostasis, bone formation, pituitary hormone secretion, steroidogenesis, nociceptive transmission, and blood pressure. Several biological actions have also been reported in birds and fish. This review summarizes the current state of identification, localization, and understanding of the functions of 26RFaQRFP and its cognate receptor, QRFPR, in vertebrates.

    Original languageEnglish
    JournalJournal of Molecular Endocrinology
    Volume52
    Issue number3
    DOIs
    Publication statusPublished - 2014 Feb 14

    Fingerprint

    Molecular Evolution
    Neuropeptides
    Mammals
    Birds
    Vertebrates
    Fishes
    Pituitary Hormones
    G-Protein-Coupled Receptors
    Osteogenesis
    Anura
    Hypothalamus
    Homeostasis
    Complementary DNA
    Eating
    Blood Pressure
    Ligands
    Amino Acids
    Peptides
    Brain
    arginylphenylalaninamide

    Keywords

    • 26RFa/QRFP
    • Food intake
    • G protein-coupled receptor
    • Hypothalamus
    • Neuropeptide

    ASJC Scopus subject areas

    • Endocrinology
    • Molecular Biology

    Cite this

    Molecular evolution of GPCRs : 26Rfa/GPR103. / Ukena, Kazuyoshi; Osugi, Tomohiro; Leprince, Jérôme; Vaudry, Hubert; Tsutsui, Kazuyoshi.

    In: Journal of Molecular Endocrinology, Vol. 52, No. 3, 14.02.2014.

    Research output: Contribution to journalArticle

    Ukena, Kazuyoshi ; Osugi, Tomohiro ; Leprince, Jérôme ; Vaudry, Hubert ; Tsutsui, Kazuyoshi. / Molecular evolution of GPCRs : 26Rfa/GPR103. In: Journal of Molecular Endocrinology. 2014 ; Vol. 52, No. 3.
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