Molecular cloning and functional characterization of a prolactin-releasing peptide homolog from Xenopus laevis

Tatsuya Sakamoto*, Aiko Oda, Kazutoshi Yamamoto, Miyoko Kaneko, Sakae Kikuyama, Akio Nishikawa, Akiyoshi Takahashi, Hiroshi Kawauchi, Kazuyoshi Tsutsui, Masaaki Fujimoto

*この研究の対応する著者

研究成果: Article査読

15 被引用数 (Scopus)

抄録

Amino acid sequences for identified prolactin (PRL)-releasing peptides (PrRPs) were conserved in mammals (>90%) or teleost fishes (100%), but there were considerable differences between these classes in the sequence (<65%) as well as in the role of PrRP. In species other than fishes and mammals, we have identified frog PrRP. The cDNA encoding Xenopus laevis prepro-PrRP, which can generate putative PrRPs, was cloned and sequenced. Sequences for the coding region showed higher identity with teleost PrRPs than mammalian homologues, but suggested the occurrence of putative PrRPs of 20 and 31 residues as in mammals. The amino acid sequence of PrRP20 was only one residue different from teleost PrRP20, but shared 70% identity with mammalian PrRP20s. In primary cultures of bullfrog (Rana catesbeiana) pituitary cells, Xenopus PrRPs increased prolactin concentrations in culture medium to 130-160% of the control, but PrRPs was much less potent than thyrotropin-releasing hormone (TRH) causing a three- to four-fold increase in prolactin concentrations. PrRP mRNA levels in the developing Xenopus brain peak in early prometamorphosis, different from prolactin levels. PrRP may not be a major prolactin-releasing factor (PRF), at least in adult frogs, as in mammals.

本文言語English
ページ(範囲)3347-3351
ページ数5
ジャーナルPeptides
27
12
DOI
出版ステータスPublished - 2006 12月
外部発表はい

ASJC Scopus subject areas

  • 生化学
  • 内分泌学
  • 生理学
  • 細胞および分子神経科学

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