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心房利钠因子(ANF)的构效关系。III. 受体亲和力与对肾小球带细胞醛固酮生成相对效力的相关性。

Structure-activity relationships of atrial natriuretic factor (ANF). III. Correlation of receptor affinity with relative potency on aldosterone production in zona glomerulosa cells.

作者信息

De Léan A, Thibault G, Seidah N G, Lazure C, Gutkowska J, Chrétien M, Genest J, Cantin M

出版信息

Biochem Biophys Res Commun. 1985 Oct 15;132(1):360-7. doi: 10.1016/0006-291x(85)91030-7.

Abstract

The activity of various fragments of ANF as inhibitors of aldosterone secretion and as competitors of [125I] ANF (Arg101-Tyr126) binding to specific receptors was studied in bovine zona glomerulosa. Shortening or lengthening the N-terminal segment of ANF does not alter its biological activity while minimally altering affinity for its receptor. Removal of the C-terminal to Cys121 or expansion up to Arg128 leads to 1000-fold decrease in receptor affinity and activity. The results indicate the importance of the C-terminal segment of ANF in determining its active conformation.

摘要

在牛肾小球带中研究了心房钠尿肽(ANF)各种片段作为醛固酮分泌抑制剂以及作为[125I]ANF(精氨酸101-酪氨酸126)与特异性受体结合的竞争者的活性。缩短或延长ANF的N末端片段不会改变其生物学活性,同时对其受体的亲和力仅有微小改变。去除C末端至半胱氨酸121或扩展至精氨酸128会导致受体亲和力和活性降低1000倍。结果表明ANF的C末端片段在确定其活性构象中具有重要作用。

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