Fujimoto M, Takeshita K, Wang X, Takabatake I, Fujisawa Y, Teranishi H, Ohtani M, Muneoka Y, Ohta S
Department of Biological Science, Faculty of Life and Environmental Science, Shimane University, Matsue, Japan.
Biochem Biophys Res Commun. 1998 Jan 14;242(2):436-40. doi: 10.1006/bbrc.1997.7973.
A novel bioactive peptide with the C-terminal RFamide was isolated from the brain of the Japanese crucian carp, Carassius auratus langsdorfii, by using the intestine of the fish as the bioassay system. The primary structure of the peptide was determined to be SPEIDPFWYVGRGVRPIGRFamide and it was designated Carassius RFamide (C-RFa). The sequence of C-RFa was found to be significantly homologous to the molluscan neuropeptide termed Achatina cardioexcitatory peptide 1 (ACEP-1). Both peptides have RPXGRFamide structure in their C-terminal moieties. C-RFa was found to have an excitatory effect on visceral muscle tissues of fish, newt, quail, and rat. In the stomach of the fish, Zacco temminckii, IGRFamide (C-RFa 17-20) was shown to be the minimal structure required for the excitatory effect and PIGRFamide (C-RFa 16-20) to be almost equipotent with the parent peptide C-RFa.
通过将鱼的肠道作为生物测定系统，从日本鲫鱼（Carassius auratus langsdorfii）的脑中分离出一种具有C末端RFamide的新型生物活性肽。该肽的一级结构被确定为SPEIDPFWYVGRGVRPIGRFamide，并被命名为鲫鱼RFamide（C-RFa）。发现C-RFa的序列与被称为玛瑙螺心脏兴奋肽1（ACEP-1）的软体动物神经肽具有显著同源性。两种肽在其C末端部分都具有RPXGRFamide结构。发现C-RFa对鱼、蝾螈、鹌鹑和大鼠的内脏肌肉组织有兴奋作用。在马口鱼（Zacco temminckii）的胃中，IGRFamide（C-RFa 17-20）被证明是产生兴奋作用所需的最小结构，而PIGRFamide（C-RFa 16-20）与母体肽C-RFa几乎具有同等效力。
