Key result
A 17-amino acid peptide of the middle region of NPR-C (Peptide 4) selectively bound to Gi1 and Gi2, activating phospholipase C-beta3 and inducing smooth muscle contraction.
Population
Gastric and tenia coli smooth muscle
Comparison
Synthetic peptide fragments of the cytoplasmic… vs Other peptide sequences and selective NPR-C…
Design
Preclinical
Authors
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Provides a tool to probe NPR-C/Gi coupling; leaves open relevance to cardiovascular signaling.
Identified a 17-amino acid sequence in the middle region of the NPR-C cytoplasmic domain responsible for G protein activation and downstream signaling.
Murthy et al. (1999) studied this question. Synthetic peptide fragments of the cytoplasmic domain of NPR-C (Peptide 4) vs. Other peptide sequences (Peptides 1, 2, 3) was evaluated on G protein activation (Gi1 and Gi2 binding, PLC-beta3 activation, adenylyl cyclase inhibition, and smooth muscle contraction). A 17-amino acid peptide of the middle region of NPR-C (Peptide 4) selectively bound to Gi1 and Gi2, activating phospholipase C-beta3 and inducing smooth muscle contraction.
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