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The Relevance of the UPS in Fatty Liver Graft Preservation: A New Approach for IGL-1 and HTK Solutions
The 26S proteasome is the central proteolytic machinery of the ubiquitin proteasome system (UPS), which is involved in the degradation of ubiquitinated protein substrates. Recently, UPS inhibition has been shown to be a key factor in fatty liver graft preservation during organ cold storage using Uni...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5713257/ https://www.ncbi.nlm.nih.gov/pubmed/29088097 http://dx.doi.org/10.3390/ijms18112287 |
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author | Panisello-Roselló, Arnau Verde, Eva Amine Zaouali, Mohamed Flores, Marta Alva, Norma Lopez, Alexandre Folch-Puy, Emma Carbonell, Teresa Hotter, Georgina Adam, René Roselló-Catafau, Joan |
author_facet | Panisello-Roselló, Arnau Verde, Eva Amine Zaouali, Mohamed Flores, Marta Alva, Norma Lopez, Alexandre Folch-Puy, Emma Carbonell, Teresa Hotter, Georgina Adam, René Roselló-Catafau, Joan |
author_sort | Panisello-Roselló, Arnau |
collection | PubMed |
description | The 26S proteasome is the central proteolytic machinery of the ubiquitin proteasome system (UPS), which is involved in the degradation of ubiquitinated protein substrates. Recently, UPS inhibition has been shown to be a key factor in fatty liver graft preservation during organ cold storage using University of Wisconsin solution (UW) and Institute Georges Lopez (IGL-1) solutions. However, the merits of IGL-1 and histidine-tryptophan-ketoglutarate (HTK) solutions for fatty liver preservation have not been compared. Fatty liver grafts from obese Zücker rats were preserved for 24 h at 4 °C. Aspartate aminotransferase and alanine aminotransferase (AST/ALT), glutamate dehydrogenase (GLDH), ATP, adenosine monophosphate protein kinase (AMPK), e-NOS, proteasome activity and liver polyubiquitinated proteins were determined. IGL-1 solution prevented ATP breakdown during cold-storage preservation of steatotic livers to a greater extent than HTK solution. There were concomitant increases in AMPK activation, e-NOS (endothelial NOS (NO synthase)) expression and UPS inhibition. UPS activity is closely related to the composition of the solution used to preserve the organ. IGL-1 solution provided significantly better protection against ischemia-reperfusion for cold-stored fatty liver grafts than HTK solution. The effect is exerted through the activation of the protective AMPK signaling pathway, an increase in e-NOS expression and a dysregulation of the UPS. |
format | Online Article Text |
id | pubmed-5713257 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-57132572017-12-07 The Relevance of the UPS in Fatty Liver Graft Preservation: A New Approach for IGL-1 and HTK Solutions Panisello-Roselló, Arnau Verde, Eva Amine Zaouali, Mohamed Flores, Marta Alva, Norma Lopez, Alexandre Folch-Puy, Emma Carbonell, Teresa Hotter, Georgina Adam, René Roselló-Catafau, Joan Int J Mol Sci Article The 26S proteasome is the central proteolytic machinery of the ubiquitin proteasome system (UPS), which is involved in the degradation of ubiquitinated protein substrates. Recently, UPS inhibition has been shown to be a key factor in fatty liver graft preservation during organ cold storage using University of Wisconsin solution (UW) and Institute Georges Lopez (IGL-1) solutions. However, the merits of IGL-1 and histidine-tryptophan-ketoglutarate (HTK) solutions for fatty liver preservation have not been compared. Fatty liver grafts from obese Zücker rats were preserved for 24 h at 4 °C. Aspartate aminotransferase and alanine aminotransferase (AST/ALT), glutamate dehydrogenase (GLDH), ATP, adenosine monophosphate protein kinase (AMPK), e-NOS, proteasome activity and liver polyubiquitinated proteins were determined. IGL-1 solution prevented ATP breakdown during cold-storage preservation of steatotic livers to a greater extent than HTK solution. There were concomitant increases in AMPK activation, e-NOS (endothelial NOS (NO synthase)) expression and UPS inhibition. UPS activity is closely related to the composition of the solution used to preserve the organ. IGL-1 solution provided significantly better protection against ischemia-reperfusion for cold-stored fatty liver grafts than HTK solution. The effect is exerted through the activation of the protective AMPK signaling pathway, an increase in e-NOS expression and a dysregulation of the UPS. MDPI 2017-10-31 /pmc/articles/PMC5713257/ /pubmed/29088097 http://dx.doi.org/10.3390/ijms18112287 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Panisello-Roselló, Arnau Verde, Eva Amine Zaouali, Mohamed Flores, Marta Alva, Norma Lopez, Alexandre Folch-Puy, Emma Carbonell, Teresa Hotter, Georgina Adam, René Roselló-Catafau, Joan The Relevance of the UPS in Fatty Liver Graft Preservation: A New Approach for IGL-1 and HTK Solutions |
title | The Relevance of the UPS in Fatty Liver Graft Preservation: A New Approach for IGL-1 and HTK Solutions |
title_full | The Relevance of the UPS in Fatty Liver Graft Preservation: A New Approach for IGL-1 and HTK Solutions |
title_fullStr | The Relevance of the UPS in Fatty Liver Graft Preservation: A New Approach for IGL-1 and HTK Solutions |
title_full_unstemmed | The Relevance of the UPS in Fatty Liver Graft Preservation: A New Approach for IGL-1 and HTK Solutions |
title_short | The Relevance of the UPS in Fatty Liver Graft Preservation: A New Approach for IGL-1 and HTK Solutions |
title_sort | relevance of the ups in fatty liver graft preservation: a new approach for igl-1 and htk solutions |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5713257/ https://www.ncbi.nlm.nih.gov/pubmed/29088097 http://dx.doi.org/10.3390/ijms18112287 |
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