Get access to all handy features included in the IVIS website
- Get unlimited access to books, proceedings and journals.
- Get access to a global catalogue of meetings, on-site and online courses, webinars and educational videos.
- Bookmark your favorite articles in My Library for future reading.
- Save future meetings and courses in My Calendar and My e-Learning.
- Ask authors questions and read what others have to say.
Comprehensive protein profiling of synovial fluid in osteoarthritis
Peffers, M., Riggs, C., McDermott...
Get access to all handy features included in the IVIS website
- Get unlimited access to books, proceedings and journals.
- Get access to a global catalogue of meetings, on-site and online courses, webinars and educational videos.
- Bookmark your favorite articles in My Library for future reading.
- Save future meetings and courses in My Calendar and My e-Learning.
- Ask authors questions and read what others have to say.
Read
Reasons for performing study:
Synovial fluid (SF) is located in joint cavities, tendon sheaths and bursae. In joints it comprises a serum filtrate with additional contributions from articular cartilage, synovium and bone. It represents a potential source of disease specific proteins that could aid in the understanding of the pathogenesis of joint disease and be used in the early diagnosis of disease.
Objectives:
To comprehensively profile the protein complement of SF in health and osteoarthritis (OA) using liquid chromatography mass spectrometry (LC-MS/MS) and identify potential OA biomarkers. Study design: SF was used from the metacarpophalangeal joints of 9 normal and 9 OA Thoroughbred horses following macroscopic, microscopic and synovitis scoring.
Methods:
Samples were analysed with LC-MS/MS using a NanoAcquity LC coupled to a LTQ Orbitrap Velos. Progenesis™ LC-MS software was used for label-free quantification with data searched using Mascot in the Ensembl database for horse. Adjusted ANOVA values of P2-fold were regarded as significant.
Results:
754 proteins were identified in SF. Thus Proteominer™ beads concentrated the lower abundance proteins enabling the most comprehensive SF proteome to date. Proteins identified included those relating to matrix proteins, inflammatory factors, complement activation proteins and proteases. A subset of 10 proteins was identified which were differentially expressed in OA SF.
Conclusions:
A number of proteins were identified for the first time in SF which may be involved in the pathogenesis of OA. We identified a distinct set of proteins that may act as potential biomarkers to distinguish between normal and OA joints. S100-A10, a calcium binding protein has upregulated in OA. This may have a role in the synthesis and activation of matrix degrading proteases. CD109 is a TGF-β co-receptor, released from the chondrocyte cell surface that inhibits TGF-β signalling. Its contribution to the disregulation of TGF-β is unknown
Get access to all handy features included in the IVIS website
- Get unlimited access to books, proceedings and journals.
- Get access to a global catalogue of meetings, on-site and online courses, webinars and educational videos.
- Bookmark your favorite articles in My Library for future reading.
- Save future meetings and courses in My Calendar and My e-Learning.
- Ask authors questions and read what others have to say.
About
Affiliation of the authors at the time of publication
Institute of Ageing and Chronic Disease, University of Liverpool, Liverpool, UK
Comments (0)
Ask the author
0 comments