Isolation and characterization of a novel endogenous peptide ligand for the human APJ receptor
Isolation and characterization of a novel endogenous peptide ligand for the human APJ receptor
复制标题
DOI：
10.1006/bbrc.1998.9489
复制
发表时间：
1998-10-20
影响因子：
3.1
通讯作者：
Fujino, M
中科院分区：
文献类型：
--
作者：
Tatemoto, K;Hosoya, M;Fujino, M
在寻找孤儿G蛋白偶联受体APJ的内源性配体时，通过测量表达APJ受体的细胞的细胞外酸化速率的增加来检查各种组织提取物中配体的存在，所述APJ受体作为由受体和配体的相互作用诱导的特异性信号。通过监测这种活性，我们从牛胃提取物中分离出一种APJ受体配体，命名为apelin。牛和人爱帕琳前原蛋白的结构由相应的cDNA序列推断。前原蛋白由77个氨基酸残基组成，并且爱帕琳序列编码在C-末端区域。衍生自牛前爱帕琳原的C-末端氨基酸序列的合成肽能够在10（-7）至10（-10）M的范围内特异性地促进表达APJ受体的细胞中的酸化速率，表明爱帕琳是APJ受体的内源性配体，（C）1998 Academic Press。
In the search for an endogenous ligand of the orphan G protein-coupled receptor APJ, the presence of the ligand in various tissue extracts was examined by measuring the increase in extracellular acidification rate of the cells expressing the APJ receptor as a specific signal induced by the interaction of the receptor and ligand. By monitoring this activity, we isolated an APJ receptor ligand, designated apelin, from bovine stomach extracts. The structures of bovine and human apelin preproproteins were deduced from the sequences of the corresponding cDNAs. The preproproteins consisted of 77 amino acid residues, and the apelin sequence was encoded in the C-terminal regions. Synthetic peptides derived from the C-terminal amino acid sequence of bovine preproapelin were capable of specifically promoting the acidification rate in the cells expressing the APJ receptor in a range from 10(-7) to 10(-10) M, indicating that apelin is an endogenous ligand for the APJ receptor, (C) 1998 Academic Press.