Lyall F, Balmforth A J, Morton J J
MRC Blood Pressure Unit, Western Infirmary, Glasgow.
J Endocrinol. 1988 May;117(2):315-21. doi: 10.1677/joe.0.1170315.
Specific high-affinity binding sites (dissociation constant 100 pmol/l) for atrial natriuretic peptide (ANP) have been identified in the clone D384 derived from the human astrocytoma cell line G-CCM. Unrelated peptides such as angiotensin II, vasopressin and bradykinin did not compete for these sites. Of the atrial natriuretic peptides studied, both the human and rat ANP competed equally, while peptides with either C- or N-terminal residue missing or with no internal -S-S-bond either competed less effectively or did not compete at all. Human ANP stimulated the cells to increase their intracellular level of cyclic GMP in a time- and dose-dependent manner with maximum stimulation being approached but not reached at concentrations of 1 mumol/l. These results support both the notion that ANP has an important functional role within the brain and the concept of neurotransmitter/neuromodulator communication between neurones and glia.
在源自人星形细胞瘤细胞系G-CCM的克隆D384中,已鉴定出心房利钠肽(ANP)的特异性高亲和力结合位点(解离常数为100 pmol/l)。血管紧张素II、血管加压素和缓激肽等无关肽不与这些位点竞争。在所研究的心房利钠肽中,人ANP和大鼠ANP的竞争能力相同,而C端或N端残基缺失或没有内部二硫键的肽竞争能力较弱或根本不竞争。人ANP以时间和剂量依赖性方式刺激细胞增加其细胞内环磷酸鸟苷水平,在1 μmol/l浓度时接近但未达到最大刺激。这些结果支持了ANP在脑内具有重要功能作用的观点以及神经元与神经胶质细胞之间神经递质/神经调质通讯的概念。