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Identification of multiple functional receptors for tyramine on an insect secretory epithelium
The biogenic amine tyramine (TA) regulates many aspects of invertebrate physiology and development. Although three TA receptor subtypes have been identified (TAR1-3), specific receptors have not been linked to physiological responses in native tissue. In the Malpighian (renal) tubule of Drosophila m...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5427925/ https://www.ncbi.nlm.nih.gov/pubmed/28279025 http://dx.doi.org/10.1038/s41598-017-00120-z |
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author | Zhang, Haiying Blumenthal, Edward M. |
author_facet | Zhang, Haiying Blumenthal, Edward M. |
author_sort | Zhang, Haiying |
collection | PubMed |
description | The biogenic amine tyramine (TA) regulates many aspects of invertebrate physiology and development. Although three TA receptor subtypes have been identified (TAR1-3), specific receptors have not been linked to physiological responses in native tissue. In the Malpighian (renal) tubule of Drosophila melanogaster, TA activates a transepithelial chloride conductance, resulting in diuresis and depolarization of the transepithelial potential. In the current work, mutation or RNAi-mediated knockdown in the stellate cells of the tubule of TAR2 (tyrR, CG7431) resulted in a dramatic reduction, but not elimination, of the TA-mediated depolarization. Mutation or knockdown of TAR3 (tyrRII, CG16766) had no effect. However, deletion of both genes, or knockdown of TAR3 on a TAR2 mutant background, eliminated the TA responses. Thus while TAR2 is responsible for the majority of the TA sensitivity of the tubule, TAR3 also contributes to the response. Knockdown or mutation of TAR2 also eliminated the response of tubules to the related amine octopamine (OA), indicating that OA can activate TAR2. This finding contrasts to reports that heterologously expressed TAR2 is highly selective for TA over OA. This is the first report of TA receptor function in a native tissue and indicates unexpected complexity in the physiology of the Malpighian tubule. |
format | Online Article Text |
id | pubmed-5427925 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-54279252017-05-12 Identification of multiple functional receptors for tyramine on an insect secretory epithelium Zhang, Haiying Blumenthal, Edward M. Sci Rep Article The biogenic amine tyramine (TA) regulates many aspects of invertebrate physiology and development. Although three TA receptor subtypes have been identified (TAR1-3), specific receptors have not been linked to physiological responses in native tissue. In the Malpighian (renal) tubule of Drosophila melanogaster, TA activates a transepithelial chloride conductance, resulting in diuresis and depolarization of the transepithelial potential. In the current work, mutation or RNAi-mediated knockdown in the stellate cells of the tubule of TAR2 (tyrR, CG7431) resulted in a dramatic reduction, but not elimination, of the TA-mediated depolarization. Mutation or knockdown of TAR3 (tyrRII, CG16766) had no effect. However, deletion of both genes, or knockdown of TAR3 on a TAR2 mutant background, eliminated the TA responses. Thus while TAR2 is responsible for the majority of the TA sensitivity of the tubule, TAR3 also contributes to the response. Knockdown or mutation of TAR2 also eliminated the response of tubules to the related amine octopamine (OA), indicating that OA can activate TAR2. This finding contrasts to reports that heterologously expressed TAR2 is highly selective for TA over OA. This is the first report of TA receptor function in a native tissue and indicates unexpected complexity in the physiology of the Malpighian tubule. Nature Publishing Group UK 2017-03-13 /pmc/articles/PMC5427925/ /pubmed/28279025 http://dx.doi.org/10.1038/s41598-017-00120-z Text en © The Author(s) 2017 This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Zhang, Haiying Blumenthal, Edward M. Identification of multiple functional receptors for tyramine on an insect secretory epithelium |
title | Identification of multiple functional receptors for tyramine on an insect secretory epithelium |
title_full | Identification of multiple functional receptors for tyramine on an insect secretory epithelium |
title_fullStr | Identification of multiple functional receptors for tyramine on an insect secretory epithelium |
title_full_unstemmed | Identification of multiple functional receptors for tyramine on an insect secretory epithelium |
title_short | Identification of multiple functional receptors for tyramine on an insect secretory epithelium |
title_sort | identification of multiple functional receptors for tyramine on an insect secretory epithelium |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5427925/ https://www.ncbi.nlm.nih.gov/pubmed/28279025 http://dx.doi.org/10.1038/s41598-017-00120-z |
work_keys_str_mv | AT zhanghaiying identificationofmultiplefunctionalreceptorsfortyramineonaninsectsecretoryepithelium AT blumenthaledwardm identificationofmultiplefunctionalreceptorsfortyramineonaninsectsecretoryepithelium |