Characterization of a cDNA encoding a precursor of Carassius RFamide, structurally related to a mammalian prolactin‐releasing peptide

FEBS Letters

Minakata, Hiroyuki¹  Satake, Honoo¹  Fujimoto, Masaaki²  Wang, Xiaoyan² 

[1] Suntory Institute for Bioorganic Research, Wakayamadai 1-1-1, Shimamoto-cho, Mishimagun, Osaka 618-8503, Japan;Department of Biological Science, Faculty of Life and Environmental Science, Shimane University, Nishikawatsu-cho 1060, Matsue 690-8504, Japan

关键词: RFamide;    Precursor;    Expression;    Carassius auratus langsdorfi;    ACEP-1;    Achatina cardioexcitatory peptide;    C-RFa;    Carassius RFamide;    DIG;    digoxigenin;    HCIP;    Helix cardioinhibitory peptide;    LyCEP;    Lymnaea cardioexcitatory peptide;    PrRP;    prolactin-releasing peptide;    RACE;    rapid amplification of cDNA end;    RT-PCR;    reverse transcription-polymerase chain reaction;   

DOI  :  10.1016/S0014-5793(99)00215-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have characterized the cDNA encoding Carassius RFamide (C-RFa), which is structurally related to mammalian prolactin-releasing peptides (PrRPs), from the brain of the crucian carp. The deduced C-RFa precursor has been shown to comprise 117 amino acids, encoding a single C-RFa sequence. A comparative study of amino acid sequences has revealed that several sequences conserved in preproPrRPs are also found in the C-RFa precursor. Furthermore, the abundant presence of the C-RFa mRNA in the telencephalon, optic tectum, medulla oblongata, and proximal half eye ball was demonstrated by Southern blot analysis of RT-PCR products.

【 授权许可】

Unknown