| Autor: |
Oikawa, Shinzo, Imai, Mayumi, Ueno, Atsuko, Tanaka, Shoji, Noguchi, Teruhisa, Nakazato, Hiroshi, Kangawa, Kenki, Fukuda, Ayako, Matsuo, Hisayuki |
| Zdroj: |
Nature; June 1984, Vol. 309 Issue: 5970 p724-726, 3p |
| Abstrakt: |
Recent identification of natriuretic–diuretic activity in peptides isolated from human1and rat 2–5atrial 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 precursor1–6. The established amino acid sequence of α-human atrial natriuretic poly peptide (α-hANP)1, a 28-residue peptide with potent natriuretic activity, provided the means to elucidate the structure of the precursor for α-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 α-hANP. The cDNA encodes γ-human atrial natriuretic polypeptide (γ-hANP) of 13,000 MW, whose C-terminal 28 amino acid residues may be processed as α-hANP. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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