Key result
Synthetic porcine brain natriuretic peptide and alpha-human atrial natriuretic peptide were almost equipotent in binding to the same receptor sites and stimulating cGMP generation in rat VSMC.
Brain natriuretic peptide and atrial natriuretic peptide interact with the same receptor sites to activate guanylate cyclase in rat vascular smooth muscle cells.
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pBNP receptor data in VSMC warrant no clinical change; leaves open its utility as ANP analog for further mechanistic studies.
The effect of synthetic porcine brain natriuretic peptide (pBNP), a novel brain peptide with sequence homology to alpha-human atrial natriuretic peptide (hANP), on receptor binding and cGMP generation, was studied in cultured rat vascular smooth muscle cells (VSMC) and compared with that of alpha-hANP. 125I-pBNP bound to the cells in a time-dependent manner similar to that of 125I-alpha-hANP. Scatchard analysis indicated a single class of binding sites for pBNP with affinity and capacity identical to those of alpha-hANP. pBNP and alpha-hANP were almost equipotent in inhibiting the binding of either radioligand and stimulating intracellular cGMP generation. These data indicate that BNP and ANP interact with the same receptor sites to activate guanylate cyclase in rat VSMC.
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Hirata et al. (1988) studied this question. synthetic porcine brain natriuretic peptide (pBNP) vs. alpha-human atrial natriuretic peptide (alpha-hANP) was evaluated on receptor binding and cGMP generation. Synthetic porcine brain natriuretic peptide and alpha-human atrial natriuretic peptide were almost equipotent in binding to the same receptor sites and stimulating cGMP generation in rat VSMC.
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