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Aquaporins in insulin resistance and diabetes: More than channels!
Aquaporins (AQPs) are part of the family of the integral membrane proteins. Their function is dedicated to the transport of water, glycerol, ammonia, urea, H(2)O(2), and other small molecules across the biological membranes. Although for many years they were scarcely considered, AQPs have a relevant...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8182305/ https://www.ncbi.nlm.nih.gov/pubmed/34090243 http://dx.doi.org/10.1016/j.redox.2021.102027 |
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author | Galli, Mauro Hameed, Ahsan Żbikowski, Arkadiusz Zabielski, Piotr |
author_facet | Galli, Mauro Hameed, Ahsan Żbikowski, Arkadiusz Zabielski, Piotr |
author_sort | Galli, Mauro |
collection | PubMed |
description | Aquaporins (AQPs) are part of the family of the integral membrane proteins. Their function is dedicated to the transport of water, glycerol, ammonia, urea, H(2)O(2), and other small molecules across the biological membranes. Although for many years they were scarcely considered, AQPs have a relevant role in the development of many diseases. Recent discoveries suggest, that AQPs may play an important role in the process of fat accumulation and regulation of oxidative stress, two crucial aspects of insulin resistance and type-2 diabetes (T2D). Insulin resistance (IR) and T2D are multi-faceted systemic diseases with multiple connections to obesity and other comorbidities such as hypertension, dyslipidemia and metabolic syndrome. Both IR and T2D transcends different tissues and organs, creating the maze of mutual relationships between adipose fat depots, skeletal muscle, liver and other insulin-sensitive organs. AQPs with their heterogenous properties, distinctive tissue distribution and documented involvement in both the lipid metabolism and regulation of the oxidative stress appear to be feasible candidates in the search for the explanation to this third-millennium plague. A lot of research has been assigned to adipose tissue AQP7 and liver tissue AQP9, clarifying their relationship and coordinated work in the induction of hepatic insulin resistance. Novel research points also to other aquaporins, such as AQP11 which may be associated with the induction of insulin resistance and T2D through its involvement in hydrogen peroxide transport. In this review we collected recent discoveries in the field of AQP's involvement in the insulin resistance and T2D. Novel paths which connect AQPs with metabolic disorders can give new fuel to the research on obesity, insulin resistance and T2D - one of the most worrying problems of the modern society. |
format | Online Article Text |
id | pubmed-8182305 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-81823052021-06-15 Aquaporins in insulin resistance and diabetes: More than channels! Galli, Mauro Hameed, Ahsan Żbikowski, Arkadiusz Zabielski, Piotr Redox Biol Review Article Aquaporins (AQPs) are part of the family of the integral membrane proteins. Their function is dedicated to the transport of water, glycerol, ammonia, urea, H(2)O(2), and other small molecules across the biological membranes. Although for many years they were scarcely considered, AQPs have a relevant role in the development of many diseases. Recent discoveries suggest, that AQPs may play an important role in the process of fat accumulation and regulation of oxidative stress, two crucial aspects of insulin resistance and type-2 diabetes (T2D). Insulin resistance (IR) and T2D are multi-faceted systemic diseases with multiple connections to obesity and other comorbidities such as hypertension, dyslipidemia and metabolic syndrome. Both IR and T2D transcends different tissues and organs, creating the maze of mutual relationships between adipose fat depots, skeletal muscle, liver and other insulin-sensitive organs. AQPs with their heterogenous properties, distinctive tissue distribution and documented involvement in both the lipid metabolism and regulation of the oxidative stress appear to be feasible candidates in the search for the explanation to this third-millennium plague. A lot of research has been assigned to adipose tissue AQP7 and liver tissue AQP9, clarifying their relationship and coordinated work in the induction of hepatic insulin resistance. Novel research points also to other aquaporins, such as AQP11 which may be associated with the induction of insulin resistance and T2D through its involvement in hydrogen peroxide transport. In this review we collected recent discoveries in the field of AQP's involvement in the insulin resistance and T2D. Novel paths which connect AQPs with metabolic disorders can give new fuel to the research on obesity, insulin resistance and T2D - one of the most worrying problems of the modern society. Elsevier 2021-05-27 /pmc/articles/PMC8182305/ /pubmed/34090243 http://dx.doi.org/10.1016/j.redox.2021.102027 Text en © 2021 Published by Elsevier B.V. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Review Article Galli, Mauro Hameed, Ahsan Żbikowski, Arkadiusz Zabielski, Piotr Aquaporins in insulin resistance and diabetes: More than channels! |
title | Aquaporins in insulin resistance and diabetes: More than channels! |
title_full | Aquaporins in insulin resistance and diabetes: More than channels! |
title_fullStr | Aquaporins in insulin resistance and diabetes: More than channels! |
title_full_unstemmed | Aquaporins in insulin resistance and diabetes: More than channels! |
title_short | Aquaporins in insulin resistance and diabetes: More than channels! |
title_sort | aquaporins in insulin resistance and diabetes: more than channels! |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8182305/ https://www.ncbi.nlm.nih.gov/pubmed/34090243 http://dx.doi.org/10.1016/j.redox.2021.102027 |
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