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Protein citrullination and NET formation do not contribute to the pathology of A20/TNFAIP3 mutant mice. | LitMetric

AI Article Synopsis

  • * Research using mouse models has shown that A20's deubiquitinase (DUB) function, when genetically disrupted, does not lead to autoimmune diseases, suggesting its role is not as straightforward as previously thought.
  • * Additionally, the absence of PAD4, which is responsible for a specific protein modification, does not prevent autoimmunity in A20-deficient mice, indicating that the pathways related to PAD4 and protein citrullination may not be crucial for the autoimmune processes in these models.

Article Abstract

A20 serves as a critical brake on NF-κB-dependent inflammation. In humans, polymorphisms in or near the TNFAIP3/A20 gene have been linked to various inflammatory disorders, including systemic lupus erythematosus (SLE) and rheumatoid arthritis (RA). Experimental gene knockout studies in mice have confirmed A20 as a susceptibility gene for SLE and RA. Here, we examine the significance of protein citrullination and NET formation in the autoimmune pathology of A20 mutant mice because autoimmunity directed against citrullinated antigens released by neutrophil extracellular traps (NETs) is central to the pathogenesis of RA and SLE. Furthermore, genetic variants impairing the deubiquitinase (DUB) function of A20 have been shown to contribute to autoimmune susceptibility. Our findings demonstrate that genetic disruption of A20 DUB function in A20 C103R knockin mice does not result in autoimmune pathology. Moreover, we show that PAD4 deficiency, which abolishes protein citrullination and NET formation, does not prevent the development of autoimmunity in A20 deficient mice. Collectively, these findings provide experimental confirmation that PAD4-dependent protein citrullination and NET formation do not serve as pathogenic mechanisms in the development of RA and SLE pathology in mice with A20 mutations.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10590390PMC
http://dx.doi.org/10.1038/s41598-023-45324-8DOI Listing

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