Proteome analysis of lysine crotonylation modification in patients with psoriasis.

Lysine crotonylation, particularly on histones, has recently emerged as a prominent focus in post-translational modification research. While it has been extensively studied in oncology, its role in skin diseases remains largely unexplored. To address this gap, we enrolled 45 psoriasis patients from outpatient clinics and compared crotonylation profiles between lesional and non-lesional skin tissues. Although many modifications were conserved across both tissue types, several differences were observed. We identified 100 upregulated and 76 downregulated lysine crotonylation sites in psoriatic lesions. The most significantly upregulated site was detected in COL6A3 (ratio = 3.07, p = 1.73 × 10-2), while the most significantly downregulated site was found in S100A9 (ratio = 0.14, p = 3.61 × 10-5). Bioinformatics analysis further suggested enrichment of crotonylated proteins in the ribosome pathway within psoriatic lesions. Overall, this study offers preliminary evidence of altered lysine crotonylation in psoriatic skin and suggests its potential involvement in psoriasis pathogenesis.