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A biogenic amine and a neuropeptide act identically: tyramine signals through calcium in Drosophila tubule stellate cells

Insect osmoregulation is subject to highly sophisticated endocrine control. In Drosophila, both Drosophila kinin and tyramine act on the Malpighian (renal) tubule stellate cell to activate chloride shunt conductance, and so increase the fluid production rate. Drosophila kinin is known to act through...

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Autores principales: Cabrero, Pablo, Richmond, Laura, Nitabach, Michael, Davies, Shireen A., Dow, Julian A. T.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3619477/
https://www.ncbi.nlm.nih.gov/pubmed/23446525
http://dx.doi.org/10.1098/rspb.2012.2943
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author Cabrero, Pablo
Richmond, Laura
Nitabach, Michael
Davies, Shireen A.
Dow, Julian A. T.
author_facet Cabrero, Pablo
Richmond, Laura
Nitabach, Michael
Davies, Shireen A.
Dow, Julian A. T.
author_sort Cabrero, Pablo
collection PubMed
description Insect osmoregulation is subject to highly sophisticated endocrine control. In Drosophila, both Drosophila kinin and tyramine act on the Malpighian (renal) tubule stellate cell to activate chloride shunt conductance, and so increase the fluid production rate. Drosophila kinin is known to act through intracellular calcium, but the mode of action of tyramine is not known. Here, we used a transgenically encoded GFP::apoaequorin translational fusion, targeted to either principal or stellate cells under GAL4/UAS control, to demonstrate that tyramine indeed acts to raise calcium in stellate, but not principal cells. Furthermore, the EC(50) tyramine concentration for half-maximal activation of the intracellular calcium signal is the same as that calculated from previously published data on tyramine-induced increase in chloride flux. In addition, tyramine signalling to calcium is markedly reduced in mutants of NorpA (a phospholipase C) and itpr, the inositol trisphosphate receptor gene, which we have previously shown to be necessary for Drosophila kinin signalling. Therefore, tyramine and Drosophila kinin signals converge on phospholipase C, and thence on intracellular calcium; and both act to increase chloride shunt conductance by signalling through itpr. To test this model, we co-applied tyramine and Drosophila kinin, and showed that the calcium signals were neither additive nor synergistic. The two signalling pathways thus represent parallel, independent mechanisms for distinct tissues (nervous and epithelial) to control the same aspect of renal function.
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spelling pubmed-36194772013-04-22 A biogenic amine and a neuropeptide act identically: tyramine signals through calcium in Drosophila tubule stellate cells Cabrero, Pablo Richmond, Laura Nitabach, Michael Davies, Shireen A. Dow, Julian A. T. Proc Biol Sci Research Articles Insect osmoregulation is subject to highly sophisticated endocrine control. In Drosophila, both Drosophila kinin and tyramine act on the Malpighian (renal) tubule stellate cell to activate chloride shunt conductance, and so increase the fluid production rate. Drosophila kinin is known to act through intracellular calcium, but the mode of action of tyramine is not known. Here, we used a transgenically encoded GFP::apoaequorin translational fusion, targeted to either principal or stellate cells under GAL4/UAS control, to demonstrate that tyramine indeed acts to raise calcium in stellate, but not principal cells. Furthermore, the EC(50) tyramine concentration for half-maximal activation of the intracellular calcium signal is the same as that calculated from previously published data on tyramine-induced increase in chloride flux. In addition, tyramine signalling to calcium is markedly reduced in mutants of NorpA (a phospholipase C) and itpr, the inositol trisphosphate receptor gene, which we have previously shown to be necessary for Drosophila kinin signalling. Therefore, tyramine and Drosophila kinin signals converge on phospholipase C, and thence on intracellular calcium; and both act to increase chloride shunt conductance by signalling through itpr. To test this model, we co-applied tyramine and Drosophila kinin, and showed that the calcium signals were neither additive nor synergistic. The two signalling pathways thus represent parallel, independent mechanisms for distinct tissues (nervous and epithelial) to control the same aspect of renal function. The Royal Society 2013-04-22 /pmc/articles/PMC3619477/ /pubmed/23446525 http://dx.doi.org/10.1098/rspb.2012.2943 Text en http://creativecommons.org/licenses/by/3.0/ © 2013 The Authors. Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/3.0/, which permits unrestricted use, provided the original author and source are credited.
spellingShingle Research Articles
Cabrero, Pablo
Richmond, Laura
Nitabach, Michael
Davies, Shireen A.
Dow, Julian A. T.
A biogenic amine and a neuropeptide act identically: tyramine signals through calcium in Drosophila tubule stellate cells
title A biogenic amine and a neuropeptide act identically: tyramine signals through calcium in Drosophila tubule stellate cells
title_full A biogenic amine and a neuropeptide act identically: tyramine signals through calcium in Drosophila tubule stellate cells
title_fullStr A biogenic amine and a neuropeptide act identically: tyramine signals through calcium in Drosophila tubule stellate cells
title_full_unstemmed A biogenic amine and a neuropeptide act identically: tyramine signals through calcium in Drosophila tubule stellate cells
title_short A biogenic amine and a neuropeptide act identically: tyramine signals through calcium in Drosophila tubule stellate cells
title_sort biogenic amine and a neuropeptide act identically: tyramine signals through calcium in drosophila tubule stellate cells
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3619477/
https://www.ncbi.nlm.nih.gov/pubmed/23446525
http://dx.doi.org/10.1098/rspb.2012.2943
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