Posttranslational modifications in psoriatic arthritis: A systematic literature review

Autores organización

• Omar Javier Calixto Castaño

  Autor

• Maria Consuelo Romero Sanchez

  Autor

• 

  Sandra Janneth Perdomo Lara

  Autor

Autores

• Meneses-Toro M.-A.
• Vera-Parra E.-C.
• Bello-Gualtero J.-M.

Grupos de investigación

• Grupo de Inmunología celular y molecular Universidad El Bosque (InmuBo)

  Investigador

  Maria Consuelo Romero Sanchez

Resumen

Background and aims: Psoriatic arthritis (PsA) is an inflammatory complex condition. Posttranslational modifications influence almost all aspects of normal cell biology and pathogenesis. The aim of this systematic review was to collect all published evidence regarding posttranslational modifications in PsA, and the main outcome was to evaluate an association between disease outcomes and specific posttranslational modifications in PsA. Methods: A systematic electronic search was performed in Medline, PubMed, Cochrane, Virtual Health Library, and Embase databases. A total of 587 articles were identified; 59 were evaluated after removing duplicates and scanning, of which 47 were included. A descriptive analysis was conducted, with results grouped according to the type of posttranslational modification evaluated. The protocol was registered at the PROSPERO database. Results: Seven posttranslational modifications were identified: citrullination, carbamylation, phosphorylation, glycosylation, acetylation, methylation, and oxidative stress. Anti-citrullinated peptide and anti-carbamylated protein have been evaluated in rheumatoid arthritis. There is now information suggesting that these antibodies may be helpful in improving the diagnosis of PsA and that they may demonstrate a correlation with worse disease progression (erosions, polyarticular involvement, and poor treatment response). Glycosylation was associated with increased inflammation and phosphorylation products related to the expression of SIRT2 and pSTAT3 or the presence of Th17 and cytokine interleukin-22, suggesting a possible therapeutic target. Conclusions: Posttranslational modifications often play a key role in modulating protein function in PsA and correlate with disease outcomes. Citrullination, carbamylation, phosphorylation, glycosylation, acetylation, methylation, and oxidative stress were identified as associated with diagnosis and prognosis. © 2023 The Author(s)

Keywords

• Arthritis, Psoriatic; Arthritis, Rheumatoid; Citrullination; Glycosylation; Humans; Protein Processing, Post-Translational; alpha 1 antitrypsin; C reactive protein; ccp2 antibody; ccp3 antibody; CD14 antigen; CD16 antigen; citrullinated filaggrin peptide 1; citrullinated filaggrin peptide 2; citrullinated filaggrin peptide 3; citrulline; collagen type 1; collagen type 2; concanavalin A; corticosteroid; cyclic citrullinated peptide antibody; cytokine; disease modifying antirheumatic drug; etanercept; fibrin; fibrinogen; filaggrin; free radical; gelatinase B; glycosylated protein; high density lipoprotein; histone H3; histone H4; HLA antigen; HLA DRB1 antigen; homocitrulline; hydroperoxide; I kappa B kinase alpha; immunoglobulin A; immunoglobulin enhancer binding protein; immunoglobulin G; immunoglobulin M; interleukin 22; interleukin 23p19; interleukin 6; interstitial collagenase; Janus kinase 1; low density lipoprotein; mammalian target of rapamycin; methotrexate; mitogen activated pro