Abstract
The effects of a peptide inhibitor of adenylate cyclase produced by the isolated, perfused rat liver under hypocalcemic conditions were studied. This inhibitory peptide non-competitively abolished the activation of adenylate cyclase in particulate preparations of rat liver by glucagon, epinephrine, and parathyroid hormone, as well as cyclic AMP production in glucagon-stimulated rat liver slices. Higher concentrations of inhibitor also decreased basal adenylate cyclase activity and its fluoride-responsiveness. The data suggest that this substance is normally present in liver, but is released only under hypocalcemic conditions. The peptide does not crossreact in the radioimmunoassay of glucagon, insulin, or parathyroid hormone. Its inhibitory effects are not duplicated by somatostatin, angiotensin I, renin substrate, or the desoctadecapeptide of insulin.
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© 1977 Springer-Verlag New York Inc.
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Lehotay, D.C., Levey, G.S., Canterbury, J.M., Bricker, L.A., Ruiz, E. (1977). A Peptide Inhibitor of Glucagon-Responsive Adenylate Cyclase in Liver. In: Foà , P.P., Bajaj, J.S., Foà , N.L. (eds) GLUCAGON: Its Role in Physiology and Clinical Medicine. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-6366-1_25
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DOI: https://doi.org/10.1007/978-1-4612-6366-1_25
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4612-6368-5
Online ISBN: 978-1-4612-6366-1
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