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Pleiotropic regulation of mitochondrial function by adipose triglyceride lipase-mediated lipolysis()
Lipolysis is defined as the catabolism of triacylglycerols (TGs) stored in cellular lipid droplets. Recent discoveries of essential lipolytic enzymes and characterization of numerous regulatory proteins and mechanisms have fundamentally changed our perception of lipolysis and its impact on cellular...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Editions Scientifiques Elsevier
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3859496/ https://www.ncbi.nlm.nih.gov/pubmed/23827855 http://dx.doi.org/10.1016/j.biochi.2013.06.023 |
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author | Kratky, Dagmar Obrowsky, Sascha Kolb, Dagmar Radovic, Branislav |
author_facet | Kratky, Dagmar Obrowsky, Sascha Kolb, Dagmar Radovic, Branislav |
author_sort | Kratky, Dagmar |
collection | PubMed |
description | Lipolysis is defined as the catabolism of triacylglycerols (TGs) stored in cellular lipid droplets. Recent discoveries of essential lipolytic enzymes and characterization of numerous regulatory proteins and mechanisms have fundamentally changed our perception of lipolysis and its impact on cellular metabolism. Adipose triglyceride lipase (ATGL) is the rate-limiting enzyme for TG catabolism in most cells and tissues. This review focuses on recent advances in understanding the (patho)physiological impact due to defective lipolysis by ATGL deficiency on mitochondrial (dys)function. Depending on the type of cells and tissues investigated, absence of ATGL has pleiotropic roles in mitochondrial function. |
format | Online Article Text |
id | pubmed-3859496 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Editions Scientifiques Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-38594962014-01-01 Pleiotropic regulation of mitochondrial function by adipose triglyceride lipase-mediated lipolysis() Kratky, Dagmar Obrowsky, Sascha Kolb, Dagmar Radovic, Branislav Biochimie Mini-Review Lipolysis is defined as the catabolism of triacylglycerols (TGs) stored in cellular lipid droplets. Recent discoveries of essential lipolytic enzymes and characterization of numerous regulatory proteins and mechanisms have fundamentally changed our perception of lipolysis and its impact on cellular metabolism. Adipose triglyceride lipase (ATGL) is the rate-limiting enzyme for TG catabolism in most cells and tissues. This review focuses on recent advances in understanding the (patho)physiological impact due to defective lipolysis by ATGL deficiency on mitochondrial (dys)function. Depending on the type of cells and tissues investigated, absence of ATGL has pleiotropic roles in mitochondrial function. Editions Scientifiques Elsevier 2014-01 /pmc/articles/PMC3859496/ /pubmed/23827855 http://dx.doi.org/10.1016/j.biochi.2013.06.023 Text en © 2013 The Authors https://creativecommons.org/licenses/by-nc-nd/3.0/ Open Access under CC BY-NC-ND 3.0 (https://creativecommons.org/licenses/by-nc-nd/3.0/) license |
spellingShingle | Mini-Review Kratky, Dagmar Obrowsky, Sascha Kolb, Dagmar Radovic, Branislav Pleiotropic regulation of mitochondrial function by adipose triglyceride lipase-mediated lipolysis() |
title | Pleiotropic regulation of mitochondrial function by adipose triglyceride lipase-mediated lipolysis() |
title_full | Pleiotropic regulation of mitochondrial function by adipose triglyceride lipase-mediated lipolysis() |
title_fullStr | Pleiotropic regulation of mitochondrial function by adipose triglyceride lipase-mediated lipolysis() |
title_full_unstemmed | Pleiotropic regulation of mitochondrial function by adipose triglyceride lipase-mediated lipolysis() |
title_short | Pleiotropic regulation of mitochondrial function by adipose triglyceride lipase-mediated lipolysis() |
title_sort | pleiotropic regulation of mitochondrial function by adipose triglyceride lipase-mediated lipolysis() |
topic | Mini-Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3859496/ https://www.ncbi.nlm.nih.gov/pubmed/23827855 http://dx.doi.org/10.1016/j.biochi.2013.06.023 |
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