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Brain natriuretic peptide interacts with atrial natriuretic peptide receptor in cultured rat vascular smooth muscle cells
Author(s) -
Hirata Yukio,
Shichiri Masayoshi,
Emori Toshiaki,
Marumo Fumiaki,
Kangawa Kenji,
Matsuo Hisayuki
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80523-4
Subject(s) - npr1 , npr2 , atrial natriuretic peptide , vascular smooth muscle , receptor , medicine , natriuretic peptide , brain natriuretic peptide , peptide , intracellular , endocrinology , radioligand , chemistry , biology , microbiology and biotechnology , biochemistry , smooth muscle , heart failure
The effect of synthetic porcine brain natriuretic peptide (pBNP), a novel brain peptide with sequence homology to α‐human atrial natriuretic peptide (hANP), on receptor binding and cGMP generation, was studied in cultured rat vascular smooth muscle cells (VSMC) and compared with that of α‐hANP. 125 I‐pBNP bound to the cells in a time‐dependent manner similar to that of 125 I‐α‐hANP. Scatchard analysis indicated a single class of binding sites for pBNP with affinity and capacity identical to those of α‐hANP. pBNP and α‐hANP were almost equipotent in inhibiting the binding of either radioligand and stimulating intracellular cGMP generation. These data indicate that BNP and ANP interact with the same receptor sites to activate guanylate cyclase in rat VSMC.