Comprehensive Profiling of Proteome and Ubiquitome Changes in Human Lens Epithelial Cell Line after Ultraviolet-B Irradiation

被引：16

作者：

Chen, Xiaojuan ^{[1
]}

Li, Pengfei ^{[1
]}

Zhang, Guowei ^{[1
]}

Kang, Lihua ^{[1
]}

Qin, Bai ^{[1
]}

Mao, Xinmu ^{[1
]}

Qin, Miaomiao ^{[1
]}

Cao, Yu ^{[1
]}

Wang, Ying ^{[1
]}

Guan, Huaijin ^{[1
]}

机构：

[1] Nantong Univ, Eye Inst, Affiliated Hosp, Nantong 226000, Jiangsu, Peoples R China

来源：

ACS OMEGA | 2020年 / 5卷 / 50期

基金：

中国国家自然科学基金;

关键词：

NUCLEOTIDE EXCISION-REPAIR; AGE-RELATED CATARACT; DNA GLYCOSYLASE 1; PATHOGENESIS; METHYLATION; PROTEASOME; EXPRESSION; PROTEINS;

D O I：

10.1021/acsomega.0c03088

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Ultraviolet-B (UVB) is a recognized risk factor for age-related cataract (ARC) and can cause various changes, including ubiquitination, in lens epithelial cells (LECs). However, the relationship between ubiquitination and ARC is unclear. Herein, we used UVB-irradiated human lens epithelial cell line (SRA01/04) representing the cell model of ARC to investigate the profile changes in the proteome and ubiquitome. A total of 552 differentially expressed proteins (DEPs) and 871 differentially ubiquitinated proteins (DUPs) were identified, and 9 ubiquitination motifs were found. Bioinformatics analysis revealed diverse pathways and biological processes of differential proteins and several DNA damage repair proteins that were potentially mediated via ubiquitin-proteasome pathway. We validated the decreased protein expression of DNA-directed RNA polymerase II subunit RPB2 (POLR2B) in both human cataract capsule tissues and UVB-treated SRA01/04 cells and found that treatment with proteasome inhibitor (MG-132) could reverse the protein level of POLR2B in UVB-irradiated SRA01/04 cells. Our data provide novel information regarding protein expressions and ubiquitination modifications in UVB-induced oxidative damage model. This study might offer a cell-level reference to further investigate the pathogenesis of ARC.

引用

页码：32171 / 32182

页数：12

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