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Inhibition of Calmodulin‐Stimulated Phosphodiesterase Activity by Vasoactive Intestinal Peptide
Journal article   Peer reviewed

Inhibition of Calmodulin‐Stimulated Phosphodiesterase Activity by Vasoactive Intestinal Peptide

Mary S. Barnette and Benjamin Weiss
Journal of neurochemistry, v 45(2), pp 640-643
Aug 1985
PMID: 2989433

Abstract

Calmodulin Calmodulin‐sensitive phosphodiesterase Peptides Secretin Structure‐activity relationships Vasoactive intestinal peptide
: The effects of certain peptides of the glucagon family on calmodulin activity were determined from their capacity to inhibit a calmodulin‐dependent form of phosphodiesterase. Vasoactive intestinal peptide and secretin were potent inhibitors of calmodulin activity, having IC50 values of 0.5 μM and 2 μM, respectively. By contrast, glucagon failed to inhibit calmodulin activity even at concentrations of 100 μM. None of these compounds significantly inhibited the basal activity of phosphodiesterase at concentrations up to 100 μM. These findings support the suggestion that important structural features of peptides for anticalmodulin activity include a net positive charge and a hydrophobic surface.

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Web of Science research areas
Biochemistry & Molecular Biology
Neurosciences
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