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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1973 Jun;70(6):1831–1835. doi: 10.1073/pnas.70.6.1831

Activation by Adenosine 3′:5′-Monophosphate of a Membrane-Bound Phosphoprotein Phosphatase from Toad Bladder

Robert J Delorenzo 1, Paul Greengard 1
PMCID: PMC433607  PMID: 4352657

Abstract

Adenosine 3′:5′-monophosphate (cyclic AMP) caused a decrease in the net rate of incorporation of radioactive phosphate into a specific protein (protein D) in a membrane fraction from toad bladder. Moreover, when the membrane protein was prelabeled with radioactive phosphate, cyclic AMP caused an increase in the net rate of removal of radioactive phosphate from this specific protein. Certain agents were shown to be selective inhibitors of membrane-bound protein D kinase or protein D phosphatase. With the help of these agents, it was concluded that cyclic AMP caused the activation of membrane-bound protein D phosphatase. The present data, together with earlier studies, are compatible with the possibility that the cyclic AMP-induced activation of a membrane-bound phosphoprotein phosphatase in toad bladder, with the consequent dephosphorylation of protein D, may be responsible for the physiological effects of antidiuretic hormone on sodium and/or water transport in this tissue.

Keywords: cyclic AMP, protein D, antidiuretic hormone

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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