Binding of synthetic β‐human atrial natriuretic peptide to cultured rat vascular smooth muscle cells

FEBS Letters

Sakakibara, Shumpei¹  Chino, Naoyoshi¹  Hirata, Yukio²  Takata, Shoichiro²  Matsubara, Hiroaki²  Takagi, Yasuyuki²  Iida, Tatsuyoshi²  Yoshimi, Hiroki²  Watanabe, Takushi X.¹  Kimura, Terutoshi¹ 

[1] Hypertension-Endocrine Division Peptide Institute Inc., Protein Research Foundation, Minoh 562, Osaka, Japan;Hypertension-Endocrine Division, National Cardiovascular Center Research Institute, Suita 565, Osaka, Japan

关键词: Atrial natriuretic peptide;    Receptor binding;    cGMP;    (Vascular smooth muscle cell;    Human);   

DOI  :  10.1016/0014-5793(87)80255-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have studied the effects of synthetic β-human atrial natriuretic peptide (β-hANP), an antiparallel dimer of α-hANP, on receptor binding and cGMP generation in cultured rat vascular smooth muscle cells and compared the effects with those of α-hANP. Characteristics of temperature-dependent binding and degradation of ¹²⁵I-β-hANP were similar to those ¹²⁵I-α-hANP. Scatchard analysis indicated a single class of binding sites for β-hANP with a maximal binding capacity one-half that of α-hANP. Parallel and antiparallel dimers were equipotent in inhibiting the binding and stimulating intracellular cGMP formation, of which the maximal effect was about one-half that of α-hANP. Reverse-phase high performance liquid chromatography revealed that most of β-hANP added to cells was converted to a small molecular mass component corresponding to α-hANP after incubation. These data suggest that the less potent effect of β-hANP in receptor binding and cGMP generation may be partly accounted for by the possible conversion of β-HANP to α-hANP at the site of target cells.

【 授权许可】

Unknown