Proteomic analysis of synovial fluid in osteoarthritis using SWATH‑mass spectrometry

Liao, Weixiong; Li, Zhongli; Li, Tanshi; Zhang, Qiang; Zhang, Heng; Wang, Xinzheng

doi:10.3892/mmr.2017.8250

Cited by 26 publications

(35 citation statements)

References 29 publications

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“…Previous studies supporting inflammation as a driving force of OA were not discovery based and only explored specific inflammatory molecules in bio fluids such as blood or plasma. 46 The lack of a robust inflammatory signature in our findings matches previous reports using discovery based proteomics 13,[15][16][17] . Furthermore, clinical trials that targeted inflammation such as IL antagonist therapies and anti-cytokine therapeutic drugs failed to reverse OA 49 .…”

Section: Discussionsupporting

confidence: 88%

“…In contrast, the global crosstalk between molecules could be very informative in order to explore and gain deeper insights into the molecular pathogenesis of OA 12 . While a number of different omics studies have been carried out [13][14][15][16][17][18][19] , they were limited by the technologies used or availability of biological samples. Therefore, the aim of this study was to explore disease stages of OA using a global discovery approach based on state-of-the-art mass spectrometry (MS) instrumentation and methodology.…”

Section: Introductionmentioning

confidence: 99%

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Proteomics profiling of human synovial fluid suggests global increased protein interplay in early-osteoarthritis (OA) and lost in late-stage OA

Ali

Turkiewicz

Hughes

et al. 2020

Preprint

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The underlying molecular mechanisms in osteoarthritis (OA) development are largely unknown. This study explores the proteome and the pairwise interplay of proteins on a global level in synovial fluid from patients with late-stage knee OA (arthroplasty), early knee OA (arthroscopy due to degenerative meniscal tear) and from controls without knee OA. Synovial fluid samples were analyzed using state-of-the-art mass spectrometry with data-independent acquisition. The differential expression of the proteins detected was clustered and evaluated with data mining strategies and a multilevel model. Group-specific slopes of associations were estimated between expressions of each pair of identified proteins to assess the co-expression (i.e. interplay) between the proteins in each group. The differential expression revealed more proteins to be increased in early-OA vs controls than late-stage OA vs controls. For most of these proteins, the fold changes between late-stage OA vs controls and early-stage OA vs controls were remarkably similar suggesting potential involvement in the OA process. Further, for the first time, this study illustrated distinct patterns in protein co-expression suggesting that the global interplay between the protein machinery is increased in early-OA and lost in late-stage OA. Further efforts should probably focus on earlier stages of the disease than previously considered.

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Section: Discussionsupporting

confidence: 88%

Section: Introductionmentioning

confidence: 99%

Proteomics profiling of human synovial fluid suggests global increased protein interplay in early-osteoarthritis (OA) and lost in late-stage OA

Ali

Turkiewicz

Hughes

et al. 2020

Preprint

View full text Add to dashboard Cite

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“…Many studies have noted that the defect area in the talus cartilage is an important factor, and choice of treatment is based on the defect area of the cartilage. Currently, however, research is insufficient on the effect of the depth of talus cartilage defects on repair outcome [ 5 , 6 ].…”

Section: Introductionmentioning

confidence: 99%

Finite Element Analysis of the Effect of Talar Osteochondral Defects of Different Depths on Ankle Joint Stability

Wei

2020

Med Sci Monit

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Background Talus cartilage injury leads to changes in biomechanics of the ankle joint and ultimately affects ankle joint function, but which talus cartilage defects require surgery is still uncertain. This research used a finite element method to simulate the effect of different depth of talus cartilage defects on the stress and stability of the ankle joint in a certain area. Material/Methods A three-dimensional finite element model with different depths of osteochondral defects was created to simulate and calculate joint stress and displacement of the articular surface of the distal tibia and the proximal talus while the ankle joint was in the push-off, midstance, and heel-strike phases. Results The equivalent stress of the proximal talus did not change significantly at a defect depth of 1 mm, whereas the equivalent stress of the upper talus increased significantly at a defect depth of ≥3 mm or more, reaching a maximum value at a defect depth of 10 mm. The equivalent stress of the tibial cartilage and the equivalent stress and displacement in the corresponding forces in the midstance phase and heel-strike phase were significantly different from those in the normal group, but the difference in stress in each defect group was not obvious. Conclusions The effect of cartilage defects of the talus on biomechanics of the ankle is clear, especially in the midstance and push-off phases. When the defect reaches the subchondral bone (at a depth of 3 mm), the most obvious change in ankle joint stability occurs, and it does not increase linearly with the increase in depth of the defect.

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“…In the last decade, many proteomic studies in the area of rheumatic diseases have been published [10][11][12][13][14], largely with the aim of diagnosing disease and evaluating disease activity/severity and therapeutic response [11,12]. Different rheumatic disease samples with complicated pathologic structure, such as blood, SF, synovial tissue, and urine, have been investigated for system-wide discovery and validation of rheumatoid arthritis biomarkers [15].…”

mentioning

confidence: 99%

Proteomic analysis of human synovial fluid reveals potential diagnostic biomarkers for ankylosing spondylitis

et al. 2020

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Background: Ankylosing spondylitis (AS) is a chronic inflammatory rheumatic disease affecting the axial skeleton and peripheral joints. The etiology of this disease remains poorly understood, but interactions between genetic and environmental factors have been implicated. The present study identified differentially expressed proteins in the synovial fluid (SF) of AS patients to elucidate the underlying cause of AS. Methods: A cohort of 40 SF samples from 10 AS and 10 each of rheumatoid arthritis (RA), gout, and osteoarthritis (OA) patients were analyzed by liquid chromatography tandem mass spectrometry (LC-MS/MS) to identify differentially expressed proteins specific to AS. The label-free LC-MS/MS results were verified by western blotting. Results: We identified 8 proteins that were > 1.5-fold upregulated in the SF of AS patients compared to that of the disease control groups, including HP, MMP1, MMP3, serum amyloid P-component (APCS), complement factor H-related protein 5 (CFHR5), mannose-binding lectin 2 (MBL2), complement component C9 (C9), and complement C4-A (C4A). CFHR5 and C9 were previously found in serum from AS patients, while APCS was previously found in SF as well as in serum. However, the present study has identified C4A, and MBL2 as potential AS biomarkers for the first time. The expression levels of MMP3, C9, and CFHR5 were verified in AS SF using western blotting. Conclusion: We performed quantitative comparative proteomic analysis using by LC-MS/MS of the SF from four disease states: RA, gout, and OA. This systematic comparison revealed novel differentially expressed proteins in AS SF, as well as two previously reported candidate biomarkers. We further verified the expression of MMP3, C9 and CFHR5 by western blot. These proteins may serve as diagnostic or prognostic biomarkers in patients with AS, and may thus improve the clinical outcomes of this serious disease.

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Proteomic analysis of synovial fluid in osteoarthritis using SWATH‑mass spectrometry

Cited by 26 publications

References 29 publications

Proteomics profiling of human synovial fluid suggests global increased protein interplay in early-osteoarthritis (OA) and lost in late-stage OA

Proteomics profiling of human synovial fluid suggests global increased protein interplay in early-osteoarthritis (OA) and lost in late-stage OA

Finite Element Analysis of the Effect of Talar Osteochondral Defects of Different Depths on Ankle Joint Stability

Proteomic analysis of human synovial fluid reveals potential diagnostic biomarkers for ankylosing spondylitis

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