Key result
Small peptide fragments of the cytoplasmic domain of the NPR-C receptor containing 12 or 17 amino acids inhibited adenylyl cyclase activity by 30-40% through a PT-sensitive G(i) protein.
Population
In vitro model assessing adenylyl cyclase activity
Comparison
Seven different peptide fragments of the… vs Scrambled peptide control and peptides with no…
Design
Preclinical
Authors
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These in vitro findings do not alter practice; extends mapping of NPR-C G(i) sequences for further mechanistic study.
Small peptide fragments of the cytoplasmic domain of the NPR-C receptor containing 12 or 17 amino acids with complete Gi activator sequences are sufficient to inhibit adenylyl cyclase activity through a PT-sensitive Gi protein.
Pagano et al. (2001) studied this question. Peptide fragments of the cytoplasmic domain of the NPR-C receptor vs. Scrambled peptide control or peptides with no structural specificity was evaluated on Inhibition of adenylyl cyclase activity. Small peptide fragments of the cytoplasmic domain of the NPR-C receptor containing 12 or 17 amino acids inhibited adenylyl cyclase activity by 30-40% through a PT-sensitive G(i) protein.
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