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Proteomic approaches for the study of tissue specific effects of 3,5,3′-triiodo-L-thyronine and 3,5-diiodo-L-thyronine in conditions of altered energy metabolism

In vertebrates and, specifically, in mammals, energy homeostasis is achieved by the integration of metabolic and neuroendocrine signals linked to one another in an intricate network hierarchically responding to the tight modulating action of hormones among which thyroid hormones (THs) play a central...

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Autores principales: Silvestri, Elena, Coppola, Maria, Cioffi, Federica, Goglia, Fernando
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4269122/
https://www.ncbi.nlm.nih.gov/pubmed/25566089
http://dx.doi.org/10.3389/fphys.2014.00491
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author Silvestri, Elena
Coppola, Maria
Cioffi, Federica
Goglia, Fernando
author_facet Silvestri, Elena
Coppola, Maria
Cioffi, Federica
Goglia, Fernando
author_sort Silvestri, Elena
collection PubMed
description In vertebrates and, specifically, in mammals, energy homeostasis is achieved by the integration of metabolic and neuroendocrine signals linked to one another in an intricate network hierarchically responding to the tight modulating action of hormones among which thyroid hormones (THs) play a central role. At the cellular level, 3,5,3′-triiodo-L-thyronine (T3) acts mainly by binding to specific nuclear receptors (TRs) but actually it is becoming more and more evident that some T3- actions are independent of TRs and that other iodothyronines, such as 3,5-diiodo-L-thyronine (T2), affect energy metabolism and adiposity. In the postgenomic era, clinical and basic biological researches are increasingly benefiting from the recently developed new omics approaches including, among the others, proteomics. Considering the recognized value of proteins as excellent targets in physiology, the functional and simultaneous analysis of the expression level and the cellular localization of multiple proteins can actually be considered fundamental in the understanding of complex mechanisms such as those involved in thyroid control of metabolism. Here, we will discuss new leads (i.e., target proteins and metabolic pathways) emerging in applying proteomics to the actions of T3 and T2 in conditions of altered energy metabolism in animal tissues having a central role in the control of energy balance.
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spelling pubmed-42691222015-01-06 Proteomic approaches for the study of tissue specific effects of 3,5,3′-triiodo-L-thyronine and 3,5-diiodo-L-thyronine in conditions of altered energy metabolism Silvestri, Elena Coppola, Maria Cioffi, Federica Goglia, Fernando Front Physiol Physiology In vertebrates and, specifically, in mammals, energy homeostasis is achieved by the integration of metabolic and neuroendocrine signals linked to one another in an intricate network hierarchically responding to the tight modulating action of hormones among which thyroid hormones (THs) play a central role. At the cellular level, 3,5,3′-triiodo-L-thyronine (T3) acts mainly by binding to specific nuclear receptors (TRs) but actually it is becoming more and more evident that some T3- actions are independent of TRs and that other iodothyronines, such as 3,5-diiodo-L-thyronine (T2), affect energy metabolism and adiposity. In the postgenomic era, clinical and basic biological researches are increasingly benefiting from the recently developed new omics approaches including, among the others, proteomics. Considering the recognized value of proteins as excellent targets in physiology, the functional and simultaneous analysis of the expression level and the cellular localization of multiple proteins can actually be considered fundamental in the understanding of complex mechanisms such as those involved in thyroid control of metabolism. Here, we will discuss new leads (i.e., target proteins and metabolic pathways) emerging in applying proteomics to the actions of T3 and T2 in conditions of altered energy metabolism in animal tissues having a central role in the control of energy balance. Frontiers Media S.A. 2014-12-17 /pmc/articles/PMC4269122/ /pubmed/25566089 http://dx.doi.org/10.3389/fphys.2014.00491 Text en Copyright © 2014 Silvestri, Coppola, Cioffi and Goglia. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Physiology
Silvestri, Elena
Coppola, Maria
Cioffi, Federica
Goglia, Fernando
Proteomic approaches for the study of tissue specific effects of 3,5,3′-triiodo-L-thyronine and 3,5-diiodo-L-thyronine in conditions of altered energy metabolism
title Proteomic approaches for the study of tissue specific effects of 3,5,3′-triiodo-L-thyronine and 3,5-diiodo-L-thyronine in conditions of altered energy metabolism
title_full Proteomic approaches for the study of tissue specific effects of 3,5,3′-triiodo-L-thyronine and 3,5-diiodo-L-thyronine in conditions of altered energy metabolism
title_fullStr Proteomic approaches for the study of tissue specific effects of 3,5,3′-triiodo-L-thyronine and 3,5-diiodo-L-thyronine in conditions of altered energy metabolism
title_full_unstemmed Proteomic approaches for the study of tissue specific effects of 3,5,3′-triiodo-L-thyronine and 3,5-diiodo-L-thyronine in conditions of altered energy metabolism
title_short Proteomic approaches for the study of tissue specific effects of 3,5,3′-triiodo-L-thyronine and 3,5-diiodo-L-thyronine in conditions of altered energy metabolism
title_sort proteomic approaches for the study of tissue specific effects of 3,5,3′-triiodo-l-thyronine and 3,5-diiodo-l-thyronine in conditions of altered energy metabolism
topic Physiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4269122/
https://www.ncbi.nlm.nih.gov/pubmed/25566089
http://dx.doi.org/10.3389/fphys.2014.00491
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