Proteomics

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Quantitative analysis of the succinylome in the thyroid tissue of high fat diet induced hypothyroxinemia in rats


ABSTRACT: Background Hypothyroidism is a common disease, and its molecular mechanism still needs further investigation. Succinylation, as a newly identified protein posttranslational modification, is found to be involved in various metabolisms and cellular processes. In the present study, we performed quantitative analysis of the lysine succinylome in the thyroid of rats with hypothyroxinemia. Methods Hypothyroxinemia was induced in rats through the administration of a high-fat diet and then the thyroid tissues were taken out for further analysis. Affinity enrichment and liquid chromatography-tandem mass spectrometry techniques were applied for the quantitative proteome and succinylome analyses, respectively. Bioinformatic analyses were performed to decipher the differentially expressed proteins and succinylated sites, including the gene ontology (GO) annotation-based classification, Wolfpsort-based subcellular localization prediction, Kyoto Encyclopedia of Genes and Genomes (KEGG)-based functional pathway enrichment, and conserved domains of protein and succinylation sites prediction. Finally, the mitochondrial oxygen consumption rates of human normal thyroid epithelial cells were measured to further verify the role of lysine succinylation in vitro. Results Overall, 3869 proteins were identified, among which 129 differentially expressed proteins were quantified. Downregulated expressed proteins were enriched in the thyroid hormone synthesis and thyroid hormone signaling pathways and were mainly localized to the mitochondria and ATPase complex. In addition, 685 lysine succinylation sites on 250 proteins were identified, of which 172 lysine succinylation sites on 104 proteins were obvious changed (7 upregulated on 5 proteins and 165 downregulated on 99 proteins). Decreased succinylated proteins were involved in diverse metabolic pathways and biological processes, including the tricarboxylic acid cycle (TCA cycle), cellular respiration, energy derivation by oxidation of organic compounds and aerobic respiration. Moreover, these decreased succinylated proteins were primarily localized to the mitochondria. Finally, OCRs related to basal respiration, ATP production and maximal respiration were markedly blunted in the normal thyroid epithelial cells treated with palmitic acid (all p < 0.05), and the changes were reversed when the cells were treated with palmitic acid and desuccinylase inhibitor together (all p < 0.05). Conclusions The thyroid differentially expressed proteins and changed succinylation levels played a potential role in the mitochondria-mediated energy metabolism in the HFD-induced hypothyroxinemia rat model.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Rattus Norvegicus (rat)

SUBMITTER: lihuan Qin  

LAB HEAD: Ling Gao

PROVIDER: PXD012814 | Pride | 2021-09-08

REPOSITORIES: Pride

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Publications

Quantitative Analysis of the Proteome and the Succinylome in the Thyroid Tissue of High-Fat Diet-Induced Hypothyroxinemia in Rats.

Hu Baoxiang B   Zhao Meng M   Luo Dandan D   Yu Chunxiao C   Shao Shanshan S   Zhao Lifang L   Yang Yashuang Y   Zhang Xiaohan X   Zhao Jiajun J   Gao Ling L  

International journal of endocrinology 20200723


Hypothyroidism is a common disease, and its molecular mechanism still needs further investigation. Lysine succinylation is found to be involved in various metabolic processes associated with hypothyroidism. We performed quantitative analysis on lysine succinylome in thyroids of rats with hypothyroxinemia, which was induced through the administration of a high-fat diet. Overall, 129 differentially expressed proteins were quantified. Downregulated proteins were enriched in the thyroid hormone synt  ...[more]

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