Key result
The 37-amino acid cytoplasmic domain of NPR-C (peptides R37A and TMC) inhibited adenylyl cyclase with a Ki of approximately 1 nM in a GTP-dependent, pertussis toxin-sensitive manner.
Population
Rat heart particulate fractions
Comparison
Synthetic peptides corresponding to the… vs Scrambled peptide control and pertussis toxin…
Design
Preclinical
Authors
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NPR-C cytoplasmic domain enables Gi-mediated signaling; extends its role beyond clearance to potential cardiovascular regulation.
The 37-amino acid cytoplasmic domain of NPR-C is sufficient to signal the inhibition of adenylyl cyclase via a pertussis toxin-sensitive G protein.
Anand‐Srivastava et al. (1996) studied this question. Cytoplasmic domain peptides (R37A and TMC) vs. K37E (scrambled peptide control) was evaluated on Inhibition of adenylyl cyclase. The 37-amino acid cytoplasmic domain of NPR-C (peptides R37A and TMC) inhibited adenylyl cyclase with a Ki of approximately 1 nM in a GTP-dependent, pertussis toxin-sensitive manner.
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