Posttranslational modifications in psoriatic arthritis: A systematic literature review

• Published in: Autoimmunity reviews Vol. 22; no. 9; p. 103393
• Main Authors: Calixto, Omar-Javier, Meneses-Toro, Maria-Alejandra, Vera-Parra, Edward-Camilo, Bello-Gualtero, Juan-Manuel, Romero-Sanchez, Consuelo, Perdomo, Sandra J.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.09.2023
• Subjects: Allergy and Immunology; Arthritis, Psoriatic - diagnosis; Arthritis, Rheumatoid; Carbamylation; Citrullination; Glycosylation; Humans; Phosphorylation; Posttranslational modifications; Protein Processing, Post-Translational; Psoriatic arthritis; DLQI; anti-CCP2; anti-CCP; MDA; ACPA; PsO; TNF; anti-Carp; CIMT; PsO-QoL; PI3K; mTOR; CIA; anti-MCV; US; Citrullination; Carbamylation; CFFCP; PASI; AIP; MeSH; Glycosylation; DAS44; MAPK; SIRT2; Psoriatic arthritis; RA; SF-36; RF; ca-LDL; HLA; ELISA; CRP; Phosphorylation; IgA; IgG; DMARDs; IgM; OA; SF; AHCPA; DAPSA; 4-ONE; DAS28; OR; ESR; SpA; PRISMA; GS; NIH; PBMCs; PTMs; DeCS; STAT; Posttranslational modifications; PD; NAPSI; HC; PsA; Disease modifying antirheumatic drugs; Disease activity score 44; Preferred Reporting Items for Systematic Review and Meta-analysis; National Institutes of Health; Spondyloarthritis; Phosphoinositide 3 kinase; Carbamylated low-density lipoprotein; Psoriatic Arthritis Quality of Life; Malondialdehyde; Healthy controls; Anti-citrullinated protein antibodies; Tumor necrosis factor; Mammalian target of rapamycin; Disease activity score 28; Nail Psoriasis Severity Index; Psoriasis Area Severity Index; Autoantibodies carbamylated peptides; Signal Transducer and Activator of Transcription; Synovial fluid; Peripheral blood mononuclear cells; Chemiluminescence immunoassay; Medical Subject Headings; Disease Activity in Psoriatic Arthritis; Second-generation anti-CCP; Chimeric fibrin and citrullinated filaggrin peptide; Atherogenic index of plasma; Rheumatoid factor; Homocitrullinated/carbamylated peptide; Dermatology Life Quality Index; Carotid intima-media thickness; Short Form Health Survey; C-reactive protein; Human leukocyte antigen; Erythrocyte sedimentation rate; Anti-citrullinated peptide; Mitogen-activated protein kinases; Rheumatoid arthritis; Osteoarthrosis; Immunoglobulin M; Power Doppler; Descriptores en Ciencias de la Salud; Immunoglobulin G; Gray-scale; Immunoglobulin A; 4-oxononenal; Ultrasound; Enzyme-linked immunosorbent assay; Sirtuin-2; Psoriasis; Vimentin antibodies; Odds ratio
• ISSN: 1568-9972; 1568-9972; 1873-0183
• DOI: 10.1016/j.autrev.2023.103393

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. 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. 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. 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. •Posttranslational modifications in PsA: Citrullination, carbamylation, phosphorylation, glycosylation, acetylation, methylation, and oxidative stress modulate protein function.•Diagnostic & prognostic implications: Antibodies targeting citrullinated peptides & carbamylated proteins improve PsA diagnosis & correlate with worse disease progression.•Role of glycosylation: Increased inflammation suggests it is a therapeutic target in PsA.•Phosphorylation & PsA pathogenesis: pSTAT3, SIRT2, Th17, and IL-22 relate to PsA, offering potential research targets.•Understanding PsA complexity: Posttranslational modifications associate with diagnosis, prognosis, and disease outcomes, guiding future research and therapies.