Porter J G, Arfsten A, Fuller F, Miller J A, Gregory L C, Lewicki J A
California Biotechnology Inc., Mountain View 94043.
Biochem Biophys Res Commun. 1990 Sep 14;171(2):796-803. doi: 10.1016/0006-291x(90)91216-f.
The amino acid sequence 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 x 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.
