Oikawa S, Imai M, Ueno A, Tanaka S, Noguchi T, Nakazato H, Kangawa K, Fukuda A, Matsuo H
Nature. 1984;309(5970):724-6. doi: 10.1038/309724a0.
Recent identification of natriuretic-diuretic activity in peptides isolated from human and rat atrial tissue implicates them in the control of extracellular fluid volume and electrolytic homeostasis. The presence of multiple forms of the peptides ranging from 3,000 to 13,000 molecular weight (MW) suggests they may all derive from the same precursor. The established amino acid sequence of alpha-human atrial natriuretic polypeptide (alpha- hANP ), a 28-residue peptide with potent natriuretic activity, provided the means to elucidate the structure of the precursor for alpha- hANP and the gene encoding it. Here we report the cloning and sequence analysis of the cDNA of human atrial mRNA encoding a precursor of alpha- hANP . The cDNA encodes gamma-human atrial natriuretic polypeptide (gamma- hANP ) of 13,000 MW, whose C-terminal 28 amino acid residues may be processed as alpha- hANP .
最近从人和大鼠心房组织中分离出的肽类物质具有利钠利尿活性,这表明它们参与细胞外液量和电解质平衡的调节。分子量在3000至13000之间的多种肽类物质的存在表明它们可能都来源于同一前体。已确定的α-人心房利钠多肽(α-hANP)的氨基酸序列是一种具有强大利钠活性的28个残基的肽,为阐明α-hANP前体及其编码基因的结构提供了方法。在此,我们报告了编码α-hANP前体的人心房mRNA的cDNA的克隆和序列分析。该cDNA编码分子量为13000的γ-人心房利钠多肽(γ-hANP),其C末端的28个氨基酸残基可能被加工成α-hANP。