ISOLATION AND FUNCTIONAL EXPRESSION OF THE HUMAN ATRIAL-NATRIURETIC-PEPTIDE CLEARANCE RECEPTOR CDNA
ISOLATION AND FUNCTIONAL EXPRESSION OF THE HUMAN ATRIAL-NATRIURETIC-PEPTIDE CLEARANCE RECEPTOR CDNA
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DOI：
10.1016/0006-291x(90)91216-f
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发表时间：
1990-09-14
影响因子：
3.1
通讯作者：
LEWICKI, JA
中科院分区：
文献类型：
--
作者：
PORTER, JG;ARFSTEN, A;LEWICKI, JA
利用从人胎盘和肾脏cDNA文库中获得的cDNA克隆核苷酸序列，推导出了人心房钠肽清除受体（ANP c受体）的氨基酸序列。人类序列与已经描述的牛c受体序列高度同源，相应的mRNA在人类胎盘、成人和胎儿肾脏和胎儿心脏中表达。将该cDNA转染到哺乳动物细胞后，重组表达实验表明，人ANP c受体对ANP具有高亲和力（6倍）。10-9 M)，与在其他物种中观察到的受体相似。这些数据表明，以前在其他哺乳动物物种中发现的人类ANP c受体在结构上高度保守，并在各种人体组织中表达。
The amino acid sequences of the human atrial natriuretic peptide clearance receptor (ANP C-receptor) was deduced from the nucleotide sequence of cDNA clones obtained from human placental and kidney cDNA libraries. The human sequence is highly homologous to the bovine C-receptor sequence already described, and the corresponding mRNA is expressed in human placenta, adult and fetal kidney and fetal heart. Upon transfection of this cDNA into mammalian cells, recombinant expression experiments revealed that the human ANP C-receptor has a high affinity for ANP (6 .times. 10-9 M), similar to that observed for the receptor in other species. These data indicate that the human ANP C-receptor, previously characterized in other mammalian species, is highly conserved structurally and is expressed in various human tissues.