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

Molecular cloning and functional characterization of a prolactin-releasing peptide homolog from Xenopus laevis. Research Abstract Details 

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Molecular cloning and functional characterization of a prolactin-releasing peptide homolog from Xenopus laevis. Abstract Text:

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

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.

Molecular cloning and functional characterization of a prolactin-releasing peptide homolog from Xenopus laevis. Publishing Authors By Initials

T Sakamoto,A Oda,K Yamamoto,M Kaneko,S Kikuyama,A Nishikawa,A Takahashi,H Kawauchi,K Tsutsui,M Fujimoto,T Sakamoto,A Oda,K Yamamoto,M Kaneko,S Kikuyama,A Nishikawa,A Takahashi,H Kawauchi,K Tsutsui,M Fujimoto,

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Molecular cloning and functional characterization of a prolactin-releasing peptide homolog from Xenopus laevis. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Peptides

VOLUME: 27

Page Numbers: 3347-51

Journal Abbreviation: Peptides

ISSN: 0196-9781

DAY: 18

MONTH: 09

YEAR: 2006

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

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LANGUAGE: eng

NlmUniqueID: 8008690

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Grant and Affiliation Information for Molecular cloning and functional characterization of a prolactin-releasing peptide homolog from Xenopus laevis.

AFFILIATION: Ushimado Marine Laboratory, Faculty of Science, Okayama University, 130-17 Kashino, Ushimado, Setouchi 701-4303, Japan.

Country: United States

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MEDLINETA: Peptides

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