In:
Frontiers in Genetics, Frontiers Media SA, Vol. 12 ( 2021-11-25)
Abstract:
Diabetic nephropathy is considered one of the most common microvascular complications of diabetes and the pathophysiology involves multiple factors. Progressive diabetic nephropathy is believed to be related to the structure and function of the tubular epithelial cells in the kidney. However, the role of lysine acetylation in lesions of the renal tubular epithelial cells arising from hyperglycemia is poorly understood. Consequently, in this study, we cultured mouse renal tubular epithelial cells in vitro under high glucose conditions and analyzed the acetylation levels of proteins by liquid chromatography-high-resolution mass spectrometry. We identified 48 upregulated proteins and downregulated 86 proteins. In addition, we identified 113 sites with higher acetylation levels and 374 sites with lower acetylation levels. Subcellular localization analysis showed that the majority of the acetylated proteins were located in the mitochondria (43.17%), nucleus (28.57%) and cytoplasm (16.19%). Enrichment analysis indicated that these acetylated proteins are primarily associated with oxidative phosphorylation, the citrate cycle (TCA cycle), metabolic pathways and carbon metabolism. In addition, we used the MCODE plug-in and the cytoHubba plug-in in Cytoscape software to analyze the PPI network and displayed the first four most compact MOCDEs and the top 10 hub genes from the differentially expressed proteins between global and acetylated proteomes. Finally, we extracted 37 conserved motifs from 4915 acetylated peptides. Collectively, this comprehensive analysis of the proteome reveals novel insights into the role of lysine acetylation in tubular epithelial cells and may make a valuable contribution towards the identification of the pathological mechanisms of diabetic nephropathy.
Type of Medium:
Online Resource
ISSN:
1664-8021
DOI:
10.3389/fgene.2021.767135
DOI:
10.3389/fgene.2021.767135.s001
DOI:
10.3389/fgene.2021.767135.s002
DOI:
10.3389/fgene.2021.767135.s003
DOI:
10.3389/fgene.2021.767135.s004
DOI:
10.3389/fgene.2021.767135.s005
DOI:
10.3389/fgene.2021.767135.s006
DOI:
10.3389/fgene.2021.767135.s007
DOI:
10.3389/fgene.2021.767135.s008
DOI:
10.3389/fgene.2021.767135.s009
DOI:
10.3389/fgene.2021.767135.s010
DOI:
10.3389/fgene.2021.767135.s011
DOI:
10.3389/fgene.2021.767135.s012
DOI:
10.3389/fgene.2021.767135.s013
Language:
Unknown
Publisher:
Frontiers Media SA
Publication Date:
2021
detail.hit.zdb_id:
2606823-0
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