Cargando…
Non-Histone Lysine Crotonylation Is Involved in the Regulation of White Fat Browning
Lysine crotonylation modification is a novel acylation modification that is similar to acetylation modification. Studies have found that protein acetylation plays an important regulatory part in the occurrence and prevention of obesity and is involved in the regulation of glucose metabolism, tricarb...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9658748/ https://www.ncbi.nlm.nih.gov/pubmed/36361522 http://dx.doi.org/10.3390/ijms232112733 |
_version_ | 1784830028290195456 |
---|---|
author | Liu, Yuexia Li, Yizhou Liang, Juntong Sun, Zhuwen Sun, Chao |
author_facet | Liu, Yuexia Li, Yizhou Liang, Juntong Sun, Zhuwen Sun, Chao |
author_sort | Liu, Yuexia |
collection | PubMed |
description | Lysine crotonylation modification is a novel acylation modification that is similar to acetylation modification. Studies have found that protein acetylation plays an important regulatory part in the occurrence and prevention of obesity and is involved in the regulation of glucose metabolism, tricarboxylic acid cycle, white fat browning and fatty acid metabolism. Therefore, we speculate that protein crotonylation may also play a more vital role in regulating the browning of white fat. To verify this conjecture, we identified 7254 crotonyl modification sites and 1629 modified proteins in iWAT of white fat browning model mice by affinity enrichment and liquid chromatography–mass spectrometry (LC-MS/MS). We selected five representative proteins in the metabolic process, namely glycerol-3-phosphate dehydrogenase 1 (GPD1), fatty acid binding protein 4 (FABP4), adenylate kinase 2 (AK2), triosephosphate isomerase 1 (TPI1) and NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 8 (NDUFA8). Through qPCR, Western blotting, immunofluorescence staining, Oil Red O staining and HE staining, we demonstrated that GPD1 and FABP4 inhibited white fat browning, while AK2, TPI1 and NDUFA8 promoted white fat browning. GPD1 and FABP4 proteins were downregulated by crotonylation modification, while AK2, TPI1 and NDUFA8 proteins were upregulated by crotonylation modification. Further detection found that the crotonylation modification of GPD1, FABP4, AK2, TPI1 and NDUFA8 promoted white fat browning, which was consistent with the sequencing results. These results indicate that the protein crotonylation is involved in regulating white fat browning, which is of great significance for controlling obesity and treating obesity-related diseases. |
format | Online Article Text |
id | pubmed-9658748 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-96587482022-11-15 Non-Histone Lysine Crotonylation Is Involved in the Regulation of White Fat Browning Liu, Yuexia Li, Yizhou Liang, Juntong Sun, Zhuwen Sun, Chao Int J Mol Sci Article Lysine crotonylation modification is a novel acylation modification that is similar to acetylation modification. Studies have found that protein acetylation plays an important regulatory part in the occurrence and prevention of obesity and is involved in the regulation of glucose metabolism, tricarboxylic acid cycle, white fat browning and fatty acid metabolism. Therefore, we speculate that protein crotonylation may also play a more vital role in regulating the browning of white fat. To verify this conjecture, we identified 7254 crotonyl modification sites and 1629 modified proteins in iWAT of white fat browning model mice by affinity enrichment and liquid chromatography–mass spectrometry (LC-MS/MS). We selected five representative proteins in the metabolic process, namely glycerol-3-phosphate dehydrogenase 1 (GPD1), fatty acid binding protein 4 (FABP4), adenylate kinase 2 (AK2), triosephosphate isomerase 1 (TPI1) and NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 8 (NDUFA8). Through qPCR, Western blotting, immunofluorescence staining, Oil Red O staining and HE staining, we demonstrated that GPD1 and FABP4 inhibited white fat browning, while AK2, TPI1 and NDUFA8 promoted white fat browning. GPD1 and FABP4 proteins were downregulated by crotonylation modification, while AK2, TPI1 and NDUFA8 proteins were upregulated by crotonylation modification. Further detection found that the crotonylation modification of GPD1, FABP4, AK2, TPI1 and NDUFA8 promoted white fat browning, which was consistent with the sequencing results. These results indicate that the protein crotonylation is involved in regulating white fat browning, which is of great significance for controlling obesity and treating obesity-related diseases. MDPI 2022-10-22 /pmc/articles/PMC9658748/ /pubmed/36361522 http://dx.doi.org/10.3390/ijms232112733 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Liu, Yuexia Li, Yizhou Liang, Juntong Sun, Zhuwen Sun, Chao Non-Histone Lysine Crotonylation Is Involved in the Regulation of White Fat Browning |
title | Non-Histone Lysine Crotonylation Is Involved in the Regulation of White Fat Browning |
title_full | Non-Histone Lysine Crotonylation Is Involved in the Regulation of White Fat Browning |
title_fullStr | Non-Histone Lysine Crotonylation Is Involved in the Regulation of White Fat Browning |
title_full_unstemmed | Non-Histone Lysine Crotonylation Is Involved in the Regulation of White Fat Browning |
title_short | Non-Histone Lysine Crotonylation Is Involved in the Regulation of White Fat Browning |
title_sort | non-histone lysine crotonylation is involved in the regulation of white fat browning |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9658748/ https://www.ncbi.nlm.nih.gov/pubmed/36361522 http://dx.doi.org/10.3390/ijms232112733 |
work_keys_str_mv | AT liuyuexia nonhistonelysinecrotonylationisinvolvedintheregulationofwhitefatbrowning AT liyizhou nonhistonelysinecrotonylationisinvolvedintheregulationofwhitefatbrowning AT liangjuntong nonhistonelysinecrotonylationisinvolvedintheregulationofwhitefatbrowning AT sunzhuwen nonhistonelysinecrotonylationisinvolvedintheregulationofwhitefatbrowning AT sunchao nonhistonelysinecrotonylationisinvolvedintheregulationofwhitefatbrowning |