Review|Volume 16, Issue 1|pp 964—982

Deciphering roles of protein post-translational modifications in IgA nephropathy progression and potential therapy

Mengying Sun¹, Guojuan Shi¹, Xiaohan Zhang¹, Chao Kan¹, Shimin Xie¹, Weixiang Peng¹, Wenjun Liu², Peter Wang², Rui Zhang¹

¹Department of Nephrology, Zhuhai People’s Hospital, Zhuhai Clinical Medical College of Jinan University, Zhuhai, Guangdong 519000, China
²Department of Medicine, Zhejiang Zhongwei Medical Research Center, Hangzhou, Zhejiang 310018, China

Received: September 5, 2023Accepted: November 16, 2023Published: January 3, 2024

https://doi.org/10.18632/aging.205406

Copyright: © 2024 Sun et al. This is an open access article distributed under the terms of the Creative Commons Attribution License (CC BY 4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

Immunoglobulin A nephropathy (IgAN), one type of glomerulonephritis, displays the accumulation of glycosylated IgA in the mesangium. Studies have demonstrated that both genetics and epigenetics play a pivotal role in the occurrence and progression of IgAN. Post-translational modification (PTM) has been revealed to critically participate in IgAN development and progression because PTM dysregulation results in impaired degradation of proteins that regulate IgAN pathogenesis. A growing number of studies identify that PTMs, including sialylation, o-glycosylation, galactosylation, phosphorylation, ubiquitination and deubiquitination, modulate the initiation and progression of IgAN. Hence, in this review, we discuss the functions and mechanisms of PTMs in regulation of IgAN. Moreover, we outline numerous compounds that govern PTMs and attenuate IgAN progression. Targeting PTMs might be a useful strategy to ameliorate IgAN.