The pathophysiological mechanism of adhesive arachnoiditis (AA) is complex, involving the interaction of multiple proteins. In recent years, the development of quantitative proteomics technology has provided a new perspective to reveal its pathological mechanism. The main objective of this study was to reveal the changes of protein expression profiles in arachnoid tissue of patients with AA. Proteomic analysis of arachnoid tissue samples was performed by high-throughput mass spectrometry. Bioinformatics tools were used to process and analyze the data and screen out 712 differentially expressed proteins (DEPs). Specially, 2 hub DEPs (TNC and RANBP1) were found as potential diagnostic markers. The expression levels of TNC and RANBP1 proteins were significantly up-regulated in patients with AA. TNC protein played a key role in inflammation and extracellular matrix remodeling, while RANBP1 was involved in cytoplasmic transport and cell cycle regulation. The abnormal expression and modification of these two proteins were closely related to the pathophysiological process of the disease. Immunoinfiltration analysis found the pathological process of AA were related to the infiltration of memory B cells, activated NK cells and CD8(+) T cells. Additonally, weighted gene co-expression network analysis (WGCNA) showed the organization of the arachnoid proteome into a network of 28 biologically meaningful modules of co-expressed proteins. Of these, 2 modules were positively correlated to AA phenotypes. This study shows a distinct proteomic landscape of AA and non-adhesive arachnoiditis (nAA). These findings also provide valuable insights into the molecular changes associated with potential mechanisms underlying AA.
Keywords: Adhesive arachnoiditis; Clinical significance; Pathophysiology; Quantitative proteomics; RANBP1; Structure and mechanism; TNC.
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