Activation of phosphorylase in toad bladder and mammalian kidney by antidiuretic hormone
- 1 August 1963
- journal article
- research article
- Published by American Physiological Society in American Journal of Physiology-Legacy Content
- Vol. 205 (2) , 298-302
- https://doi.org/10.1152/ajplegacy.1963.205.2.298
Abstract
An increase in phosphorylase activity has been demonstrated in the intact urinary bladder of the toad and in slices of rabbit renal medulla and dog renal cortex and medulla incubated in vitro with vasopressin. A similar response occurred in the toad bladder incubated with adenosine-3',5'-monophosphate (cyclic-3',5'-AMP). Phosphorylase activation in the bladder was also produced by incubation with oxytocin or protopituitrin, but not by incubation with ACTH or epinephrine. The metabolic significance of hormone-induced phosphorylase activation is unclear. However, since activation of phosphorylase is a characteristic tissue response to hormones that act through cyclic-3',5'-AMP, the present observations support the suggestion that vasopressin alters the permeability to water of the urinary bladder of the toad and mammalian kidney through a pathway involving stimulation of the production of cyclic-3',5'-AMP.Keywords
This publication has 2 references indexed in Scilit:
- Effects of Serotonin (5-Hydroxytryptamine) and Adenosine 3‘,5‘-Phosphate on Phosphofructokinase from the Liver Fluke Fasciola hepaticaJournal of Biological Chemistry, 1962
- ADENOSINE 3',5'-PHOSPHATE IN BIOLOGICAL MATERIALS .1. PURIFICATION AND PROPERTIES OF CYCLIC 3',5'-NUCLEOTIDE PHOSPHODIESTERASE AND USE SF THIS ENZYME TO CHARACTERIZE ADENOSINE 3',5'-PHOSPHATE IN HUMAN URINE1962