A型和B型利钠素在两种南极硬骨鱼(红血伯氏银耳鱼和无血红蛋白滨龙鱼)心脏中的不同结合活性

Maria Carmela Cerra , Marcello Canonaco , Raffaele Acierno , Bruno Tota
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引用次数: 22

摘要

用体外定量放射自显影技术评价了125I大鼠心钠肽在两种南极类硬骨鱼,即红血的伯氏震颤和无血红蛋白的钩龙心脏中的不同结合活性。在两种鱼类的心房、心室心肌、心室心内膜以及动脉球的内外层都发现了大鼠心房利钠肽的饱和和特异性结合位点。对饱和数据的Scatchard分析表明,伯氏锥虫的心房、心室心内膜和球外层具有一类高亲和力利钠肽结合位点(Kd=14±3.2、9.7±2.3和6.2±1.3 pM),而心室心肌和球内层含有数量增加的两类高亲和力和低亲和力利钠肽结合位点(1.8±0.6<Kd<209±66pM)。相反,在C.hamatus中,在所有心脏区域都检测到高亲和力和低亲和力结合位点(2.1±0.7<;Kd<;262±90pM)。在这两种鱼类中,在未标记的大鼠心房利钠肽或猪脑利钠肽存在的情况下的竞争实验表明了不同的置换能力。与大鼠心房利钠肽相比,猪脑利钠肽能够与这两种类脊酸的所有心脏区域的利钠肽位点结合,在伯氏T.bernacchii的心房中提供了更高的置换能力。
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Different binding activities of A- and B-type natriuretic hormones in the heart of two Antarctic teleosts, the red-blooded Trematomus bernacchii and the hemoglobinless Chionodraco hamatus

Different binding activities of 125I-rat atrial natriuretic peptide were evaluated using in vitro quantitative autoradiography in the heart of two antarctic notothenioid teleosts, the red-blooded Trematomus bernacchii and hemoglobinless Chionodraco hamatus. Saturable and specific binding sites for rat atrial natriuretic peptide were found in the atrium, ventricular myocardium, ventricular endocardium and inner and outer layers of the bulbus arteriosus of both fishes. Scatchard analysis of the saturation data showed that the atrium, ventricular endocardium and outer bulbar layer of T. bernacchii were characterized by a single class of high affinity natriuretic peptide binding sites (Kd = 14 ± 3.2, 9.7 ± 2.3 and 6.2 ± 1.3 pM, respectively), whereas the ventricular myocardium and the inner bulbar layer contained elevated numbers of two classes of high and low affinity natriuretic peptide binding sites (1.8 ± 0.6 < Kd < 209 ± 66 pM). In contrast, in C. hamatus, both high and low affinity binding sites were detected in all cardiac regions (2.1 ± 0.7 < Kd < 262 ± 90 pM). In both fishes, competition experiments in the presence of either unlabeled rat atrial natriuretic peptide or porcine brain natriuretic peptide indicated different displacement capacities. Porcine brain natriuretic peptide, able to bind to natriuretic peptides sites in all the heart regions of both notothenioids, provided a higher displacement capacity with respect to that of rat atrial natriuretic peptide in the atrium of T. bernacchii.

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