Key result
C-terminal tail deletion preserves BNP vasorelaxation and boosts cGMP, but impairs ANP activity.
Why the study?
The different effects of the C-terminal tail structures of ANP and BNP on their receptor interactions and biological actions were unclear.
BNP C-terminal tail deletion preserves vasorelaxation in vitro; leaves open its role in receptor selectivity.
Atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP) have different C-terminal tail structures compared with the rather conservative ring structures which consist of 17 amino acid residues. To examine the different effects of the tail structures of ANP and BNP on their interaction with receptors, we synthesized several peptide analogs and measured their biological actions in three different assay systems. Deletion of the C-terminal tail from rat BNP did not effect the vasorelaxation activity against rat aorta, but it promoted cGMP production in cultured rat aortic smooth muscle cells (RASMC). Deletion of the C-terminal tail from rat ANP diminished both vasorelaxant and cGMP producing activities. In a binding competition assay with RASMC and [125I]rat ANP-(1-28), the competition activities of both ANP and BNP were greatly reduced by C-terminal deletion. In addition, we obtained agonists with novel receptor selectivity.
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Shimekake et al. (1992) studied this question. C-terminal tail deletion of rat BNP and ANP vs. Intact rat BNP and ANP was evaluated on Vasorelaxation activity, cGMP production, and receptor binding competition. Deletion of the C-terminal tail from rat BNP did not affect vasorelaxation but promoted cGMP production, whereas deletion from rat ANP diminished both activities, yielding novel receptor selectivity.
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