Purification, sequencing and synthesis of natriuretic and vasoactive rat atrial peptide

Abstract

Mammalian atria contain potent natriuretic and diuretic substances1,2 which exist in high- and low-molecular-weight forms2,3 and which appear to be associated with atrium-specific granules4. The natriuretic effect of atrial extract is largely accountable for by its renal haemodynamic effects5–7; atrial extracts also antagonize hormone- and non-hormone-induced contraction of the isolated rabbit aorta8–10 and isolated rat kidney vasculature6. We have completely purified a low-molecular-weight natriuretic and vasoactive substance from rat atria and characterized it as a 24-amino acid peptide. Synthetic peptide, produced by solid-phase synthesis, mimics biological effects of crude atrial extract and purified peptide; its activity is enhanced by slow oxidation, suggesting a disulphide (Cys 4–Cys 20) configuration for the native peptide. If secreted into blood, this atrial natriuretic peptide (‘auriculin B‘) could be a novel peptide hormone of considerable importance to renal and cardiovascular homeostasis.

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Atlas, S., Kleinert, H., Camargo, M. et al. Purification, sequencing and synthesis of natriuretic and vasoactive rat atrial peptide. Nature 309, 717–719 (1984). https://doi.org/10.1038/309717a0

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