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Plin5 Bidirectionally Regulates Lipid Metabolism in Oxidative Tissues
Cytoplasmic lipid droplets (LDs) can store neutral lipids as an energy source when needed and also regulate the key metabolic processes of intracellular lipid accumulation, which is associated with several metabolic diseases. The perilipins (Plins) are a family of proteins that associate with the su...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8989587/ https://www.ncbi.nlm.nih.gov/pubmed/35401929 http://dx.doi.org/10.1155/2022/4594956 |
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author | Zhang, Xinqing Xu, Wu Xu, Rui Wang, Zhen Zhang, Xinyan Wang, Peng Peng, Ke Li, Meiling Li, Jing Tan, Yanfei Wang, Xiong Pei, Haifeng |
author_facet | Zhang, Xinqing Xu, Wu Xu, Rui Wang, Zhen Zhang, Xinyan Wang, Peng Peng, Ke Li, Meiling Li, Jing Tan, Yanfei Wang, Xiong Pei, Haifeng |
author_sort | Zhang, Xinqing |
collection | PubMed |
description | Cytoplasmic lipid droplets (LDs) can store neutral lipids as an energy source when needed and also regulate the key metabolic processes of intracellular lipid accumulation, which is associated with several metabolic diseases. The perilipins (Plins) are a family of proteins that associate with the surface of LDs. As a member of Plins superfamily, perilipin 5 (Plin5) coats LDs in cardiomyocytes, which is significantly related to reactive oxygen species (ROS) production originated from mitochondria in the heart, consequently determining the progression of diabetic cardiomyopathy. Plin5 may play a bidirectional function in lipid metabolism which is in a state of dynamic balance. In the basic state, Plin5 inhibited the binding of comparative gene identification-58 (CGI-58) to adipose triglyceride lipase (ATGL) by binding CGI-58, thus inhibiting lipolysis. However, when the body is under stress (such as cold, fasting, exercise, and other stimuli), protein kinase A (PKA) phosphorylates and activates Plin5, which then causes Plin5 to release the binding site of CGI-58 and ATGL, prompting CGI-58 to bind to ATGL and activate ATGL activity, thus accelerating the lipolysis process, revealing the indispensable role of Plin5 in lipid turnover. Here, the purpose of this review is to summarize the present understanding of the bidirectional regulation role of Plin5 in oxidative tissues and to reveal its potential role in diabetic cardiomyopathy protection. |
format | Online Article Text |
id | pubmed-8989587 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Hindawi |
record_format | MEDLINE/PubMed |
spelling | pubmed-89895872022-04-09 Plin5 Bidirectionally Regulates Lipid Metabolism in Oxidative Tissues Zhang, Xinqing Xu, Wu Xu, Rui Wang, Zhen Zhang, Xinyan Wang, Peng Peng, Ke Li, Meiling Li, Jing Tan, Yanfei Wang, Xiong Pei, Haifeng Oxid Med Cell Longev Review Article Cytoplasmic lipid droplets (LDs) can store neutral lipids as an energy source when needed and also regulate the key metabolic processes of intracellular lipid accumulation, which is associated with several metabolic diseases. The perilipins (Plins) are a family of proteins that associate with the surface of LDs. As a member of Plins superfamily, perilipin 5 (Plin5) coats LDs in cardiomyocytes, which is significantly related to reactive oxygen species (ROS) production originated from mitochondria in the heart, consequently determining the progression of diabetic cardiomyopathy. Plin5 may play a bidirectional function in lipid metabolism which is in a state of dynamic balance. In the basic state, Plin5 inhibited the binding of comparative gene identification-58 (CGI-58) to adipose triglyceride lipase (ATGL) by binding CGI-58, thus inhibiting lipolysis. However, when the body is under stress (such as cold, fasting, exercise, and other stimuli), protein kinase A (PKA) phosphorylates and activates Plin5, which then causes Plin5 to release the binding site of CGI-58 and ATGL, prompting CGI-58 to bind to ATGL and activate ATGL activity, thus accelerating the lipolysis process, revealing the indispensable role of Plin5 in lipid turnover. Here, the purpose of this review is to summarize the present understanding of the bidirectional regulation role of Plin5 in oxidative tissues and to reveal its potential role in diabetic cardiomyopathy protection. Hindawi 2022-03-31 /pmc/articles/PMC8989587/ /pubmed/35401929 http://dx.doi.org/10.1155/2022/4594956 Text en Copyright © 2022 Xinqing Zhang et al. https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Zhang, Xinqing Xu, Wu Xu, Rui Wang, Zhen Zhang, Xinyan Wang, Peng Peng, Ke Li, Meiling Li, Jing Tan, Yanfei Wang, Xiong Pei, Haifeng Plin5 Bidirectionally Regulates Lipid Metabolism in Oxidative Tissues |
title | Plin5 Bidirectionally Regulates Lipid Metabolism in Oxidative Tissues |
title_full | Plin5 Bidirectionally Regulates Lipid Metabolism in Oxidative Tissues |
title_fullStr | Plin5 Bidirectionally Regulates Lipid Metabolism in Oxidative Tissues |
title_full_unstemmed | Plin5 Bidirectionally Regulates Lipid Metabolism in Oxidative Tissues |
title_short | Plin5 Bidirectionally Regulates Lipid Metabolism in Oxidative Tissues |
title_sort | plin5 bidirectionally regulates lipid metabolism in oxidative tissues |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8989587/ https://www.ncbi.nlm.nih.gov/pubmed/35401929 http://dx.doi.org/10.1155/2022/4594956 |
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