Evolutionary origin and divergence of PQRFamide peptides and LPXRFamide peptides in the RFamide peptide family

Insights from novel lamprey RFamide peptides

Tomohiro Osugi, Kazuyoshi Ukena, Stacia A. Sower, Hiroshi Kawauchi, Kazuyoshi Tsutsui

Research output: Contribution to journalArticle

67 Citations (Scopus)

Abstract

Among the RFamide peptide groups, PQRFamide peptides, such as neuropeptide FF (NPFF) and neuropeptide AF (NPAF), share a common C-terminal Pro-Gln-Arg-Phe-NH2 motif. LPXRFamide (X = L or Q) peptides, such as gonadotropin-inhibitory hormone (GnIH), frog growth hormone-releasing peptide (fGRP), goldfish LPXRFamide peptide and mammalian RFamide-related peptides (RFRPs), also share a C-terminal Leu-Pro-Leu/Gln-Arg-Phe-NH2 motif. Such a similar C-terminal structure suggests that these two groups may have diverged from a common ancestral gene. In this study, we sought to clarify the evolutionary origin and divergence of these two groups, by identifying novel RFamide peptides from the brain of sea lamprey, one of only two extant groups of the oldest lineage of vertebrates, Agnatha. A novel lamprey RFamide peptide was identified by immunoaffinity purification using the antiserum against LPXRFamide peptide. The lamprey RFamide peptide did not contain a C-terminal LPXRFamide motif, but had the sequence SWGAPAEKFWMRAMPQRFamide (lamprey PQRFa). A cDNA of the precursor encoded one lamprey PQRFa and two related peptides. These related peptides, which also had the C-terminal PQRFamide motif, were further identified as mature endogenous ligands. Phylogenetic analysis revealed that lamprey PQRFamide peptide precursor belongs to the PQRFamide peptide group. In situ hybridization demonstrated that lamprey PQRFamide peptide mRNA is expressed in the regions predicted to be involved in neuroendocrine and behavioral functions. This is the first demonstration of the presence of RFamide peptides in the agnathan brain. Lamprey PQRFamide peptides are considered to have retained the most ancestral features of PQRFamide peptides.

Original languageEnglish
Pages (from-to)1731-1743
Number of pages13
JournalFEBS Journal
Volume273
Issue number8
DOIs
Publication statusPublished - 2006 Apr
Externally publishedYes

Fingerprint

Lampreys
Peptides
Brain
Petromyzon
RFamide peptide
Goldfish
Gonadotropins
Anura
In Situ Hybridization
Vertebrates
Immune Sera
Purification
Complementary DNA
Demonstrations
Hormones
Genes
Ligands

Keywords

  • Agnathan
  • LPXRFamide peptide
  • Molecular evolution
  • Neuropeptide FF
  • PQRFamide peptide

ASJC Scopus subject areas

  • Biochemistry

Cite this

Evolutionary origin and divergence of PQRFamide peptides and LPXRFamide peptides in the RFamide peptide family : Insights from novel lamprey RFamide peptides. / Osugi, Tomohiro; Ukena, Kazuyoshi; Sower, Stacia A.; Kawauchi, Hiroshi; Tsutsui, Kazuyoshi.

In: FEBS Journal, Vol. 273, No. 8, 04.2006, p. 1731-1743.

Research output: Contribution to journalArticle

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abstract = "Among the RFamide peptide groups, PQRFamide peptides, such as neuropeptide FF (NPFF) and neuropeptide AF (NPAF), share a common C-terminal Pro-Gln-Arg-Phe-NH2 motif. LPXRFamide (X = L or Q) peptides, such as gonadotropin-inhibitory hormone (GnIH), frog growth hormone-releasing peptide (fGRP), goldfish LPXRFamide peptide and mammalian RFamide-related peptides (RFRPs), also share a C-terminal Leu-Pro-Leu/Gln-Arg-Phe-NH2 motif. Such a similar C-terminal structure suggests that these two groups may have diverged from a common ancestral gene. In this study, we sought to clarify the evolutionary origin and divergence of these two groups, by identifying novel RFamide peptides from the brain of sea lamprey, one of only two extant groups of the oldest lineage of vertebrates, Agnatha. A novel lamprey RFamide peptide was identified by immunoaffinity purification using the antiserum against LPXRFamide peptide. The lamprey RFamide peptide did not contain a C-terminal LPXRFamide motif, but had the sequence SWGAPAEKFWMRAMPQRFamide (lamprey PQRFa). A cDNA of the precursor encoded one lamprey PQRFa and two related peptides. These related peptides, which also had the C-terminal PQRFamide motif, were further identified as mature endogenous ligands. Phylogenetic analysis revealed that lamprey PQRFamide peptide precursor belongs to the PQRFamide peptide group. In situ hybridization demonstrated that lamprey PQRFamide peptide mRNA is expressed in the regions predicted to be involved in neuroendocrine and behavioral functions. This is the first demonstration of the presence of RFamide peptides in the agnathan brain. Lamprey PQRFamide peptides are considered to have retained the most ancestral features of PQRFamide peptides.",
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AU - Kawauchi, Hiroshi

AU - Tsutsui, Kazuyoshi

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