Periostin Is a Biomarker for Anterior Shoulder Instability: Proteomic Analysis of Synovial Fluid

滑液 蛋白质组 生物标志物 医学 骨关节炎 骨膜炎 串联质谱法 不稳定性 病理 内科学 化学 质谱法 色谱法 生物化学 细胞外基质 替代医学 物理 机械
作者
Joseph W. Galvin,Rachel J. Milam,Brendan M. Patterson,James V. Nepola,Joseph A. Buckwalter,Brian R. Wolf,Felicity M. Say,K. Free,Elizabeth Yohannes
出处
期刊:American Journal of Sports Medicine [SAGE Publishing]
卷期号:52 (7): 1719-1727
标识
DOI:10.1177/03635465241246258
摘要

Background: The incremental biological changes in the synovial microenvironment of the shoulder in acute and chronic instability that may contribute to joint degeneration are poorly understood. Proteomic analysis of synovial fluid in patients with shoulder instability may improve our understanding of proteins that are shed into shoulder synovial fluid after an injury. Hypothesis: Injury-specific factors such as the direction of instability and the severity of glenoid and humeral bone loss are associated with the proteome of synovial fluid in patients with shoulder instability. Study Design: Descriptive laboratory study. Methods: Synovial fluid lavage samples were compared between patients with anterior (n = 12) and posterior (n = 8) instability and those without instability (n = 5). Synovial proteins were identified with liquid chromatography–tandem mass spectrometry. Orthogonal validation of protein targets found to be significant on tandem mass spectrometry was performed in a separate set of prospective patients with Western blotting. Data were processed and analyzed, and P values were adjusted with the Benjamini-Hochberg method for multiple comparisons. Results: A total of 25 patients were included. Tandem mass spectrometry identified 720 protein groups in synovial fluid of patients with shoulder instability. There were 4 synovial proteins that were significantly expressed in patients with anterior instability relative to posterior instability: periostin (POSTN) (adjusted P value = .03; log fold change [logFc] = 4.7), transforming growth factor beta–induced protein ig-h3 (adjusted P value = .05; logFc = 1.7), collagen type VI alpha-3 chain (adjusted P value = .04; logFc = 2.6), and coagulation factor V (adjusted P value = .04; logFc = −3.3). Among these targets, POSTN showed a moderate correlation with the Hill-Sachs lesion size ( r = 0.7). Prospective validation with Western blotting confirmed a significantly higher level of POSTN in synovial fluid of patients with anterior instability ( P = .00025; logFc = 5.1). Conclusion: Proteomic analysis enriched our understanding of proteins that were secreted into shoulder synovial fluid of patients with shoulder instability. The identification of POSTN, a proinflammatory catabolic protein involved with tissue remodeling and repair, as a significant target in anterior shoulder instability is a novel finding. Therefore, further study is warranted to determine the role that POSTN may play in the progression of bone loss and posttraumatic osteoarthritis. Clinical Relevance: Proteomic analysis of synovial fluid in patients with shoulder instability improved our understanding of this abnormality after an injury.
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