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, ,

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

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

https://doi.org/10.18632/aging.205406
How to Cite

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.

Abbreviations

APGN: acute proliferative glomerulonephritides; C1GALT1: core1 b1,3-galactosyltransferase; CREB: cAMP response element binding protein; DHA: docosahexaenoic acid; EMT: Eepithelial-to-mesenchymal transition; FSGS: focal segmental glomerulosclerosis; Gd-IgA1: galactose-deficient IgA1; GM130: Golgi matric protein 130; GMCs: glomerular mesangial cells; HECT: homologous to E6-AP C-terminus; HRP: horseradish peroxidase; ICAM-1: intercellular adhesion molecule 1; IgAN: Immunoglobulin A nephropathy; LPS: lipopolysaccharide; NLRP3: Nod-like receptor pyrin domain-containing-3; PBMCs: peripheral blood mononuclear cells; PCNA: proliferation cell nuclear antigen; PI3K: phosphatidyl inositol-3-kinase; PPARγ: Peroxisome proliferator-activated receptors-γ; PTM: Post-translational modification; RING: really interesting new gene; SUMO: small ubiquitin-like modifier; ST6GALNAC2: ST6 N-Acetylgalactosaminide Alpha-2,6-Sialyltransferase 2; TMCs: tonsillar mononuclear cells; TLR4: Toll-like receptor 4; UCH-L1: ubiquitin carboxyl-terminal hydrolase L1; UPS: ubiquitin proteasome system.