Increased renal dopamine and acute renal adaptation to a high-phosphate diet.
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The current experiments explore the role of dopamine in facilitating the acute increase in renal phosphate excretion in response to a high-phosphate diet. Compared with a low-phosphate (0.1%) diet for 24 h, mice fed a high-phosphate (1.2%) diet had significantly higher rates of phosphate excretion in the urine associated with a two- to threefold increase in the dopamine content of the kidney and in the urinary excretion of dopamine. Animals fed a high-phosphate diet had a significant increase in the abundance and activity of renal DOPA (l-dihydroxyphenylalanine) decarboxylase and significant reductions in renalase, monoamine oxidase A, and monoamine oxidase B. The activity of protein kinase A and protein kinase C, markers of activation of renal dopamine receptors, were significantly higher in animals fed a high-phosphate vs. a low-phosphate diet. Treatment of rats with carbidopa, an inhibitor of DOPA decarboxylase, impaired adaptation to a high-phosphate diet. These experiments indicate that the rapid adaptation to a high-phosphate diet involves alterations in key enzymes involved in dopamine synthesis and degradation, resulting in increased renal dopamine content and activation of the signaling cascade used by dopamine to inhibit the renal tubular reabsorption of phosphate.
Mice, Inbred C57BL
Cyclic AMP-Dependent Protein Kinases
Protein Kinase C
Analysis of Variance
Aromatic Amino Acid Decarboxylase Inhibitors
Published Version (Please cite this version)10.1152/ajprenal.00744.2010
Publication InfoWeinman, Edward J; Biswas, Rajatsubhra; Steplock, Deborah; Wang, Peili; Lau, Yuen-Sum; Desir, Gary V; & Shenolikar, Shirish (2011). Increased renal dopamine and acute renal adaptation to a high-phosphate diet. American journal of physiology. Renal physiology, 300(5). pp. F1123-F1129. 10.1152/ajprenal.00744.2010. Retrieved from https://hdl.handle.net/10161/17239.
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Professor Emeritus of Psychiatry and Behavioral Sciences
Protein phosphorylation controls a wide range of physiological processes in mammalian tissues. Phosphorylation state of cellular proteins is controlled by the opposing actions of protein kinases and phosphatases that are regulated by hormones, neurotransmitters, growth factors and other environmental cues. Our research attempts to understand the communication between protein kinases and phosphatases that dictates cellular protein phosphorylation and the cell's response to hormones. Over the