Brain natriuretic peptide binding sites in rat kidney.

T Maeda, M Niwa, M Ozaki
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Abstract

Specific binding sites for [125I] porcine brain natriuretic peptide-26 ([125I]BNP-26) were investigated in the rat kidney by using receptor autoradiographic and membrane binding techniques. The binding sites were discretely localized in the glomeruli and inner medulla. There were no differences between the localization of [125I] BNP-26 and [125I] alpha-rat ANP binding sites. [125I]BNP-26 binding to solubilized membranes from isolated glomeruli of the rat kidney was saturable, and a single class of high-affinity sites. [125I]BNP-26 bound to two sites in solubilized inner medullary membranes. The rank order of potency to inhibit binding was BNP-26 = alpha-rat ANP (1-28) greater than atriopeptin III [ANP-(103-126)] much greater than atriopeptin I [ANP(103-123)] greater than des-Cys105, Cys121-ANP-(104-126). The possibility that BNP-26 regulates, as a circulating hormone, kidney functions by binding to ANP receptors would have to be considered.

大鼠肾内脑利钠肽结合位点。
采用受体放射自显影和膜结合技术研究了[125I]猪脑利钠肽-26 ([125I]BNP-26)在大鼠肾脏中的特异性结合位点。结合位点分别位于肾小球和内髓质。[125I] BNP-26和[125I] α -大鼠ANP结合位点的定位没有差异。[125I]BNP-26与大鼠离体肾小球溶解膜的结合是饱和的,并且具有一类高亲和力位点。[125I]BNP-26在溶解后的髓内膜上与两个位点结合。抑制结合的效价排序为:BNP-26 = α -大鼠ANP(1-28)大于心房肽III [ANP-(103-126)],远大于心房肽I [ANP(103-123)],大于des-Cys105、Cys121-ANP-(104-126)。必须考虑BNP-26作为一种循环激素,通过与ANP受体结合来调节肾功能的可能性。
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