Proteomic analysis of human osteoarthritis synovial fluid

Clinical Proteomics

Akhilesh Pandey⁹  Subramanian Shankar²  Harsha Gowda⁵  Sujatha Mohan⁶  TS Keshava Prasad³  Nandini A Sahasrabuddhe⁵  YL Ramachandra⁴  Vivek Vasdev⁷  Ramesh Jois¹  Shantal Gupta Tankala²  Mukesh Dhillon²  Navjyot Kaur²  Joji Kurian Thomas^1,10  Renu Goel⁴  Rajesh Raju⁵  Yashwanth Subbannayya^1,11  Dhanashree S Kelkar^1,10  Santosh Renuse^1,10  Srikanth S Manda⁸  Mitali Bhattacharjee^1,10  Sartaj Ahmad³  Raja Sekhar Nirujogi⁸  Lavanya Balakrishnan⁴ 

[1] Department of Rheumatology, Fortis Hospitals, Bangalore, Karnataka 560076, India;Department of Internal Medicine, Armed Forces Medical College, Pune, Maharashtra 411040, India;Manipal University, Madhava Nagar, Manipal, Karnataka 576104, India;Department of Biotechnology, Kuvempu University, Shankaraghatta, Shimoga, Karnataka 577451, India;Institute of Bioinformatics, International Technology Park, Bangalore, Karnataka 560066, India;Laboratory for Integrated Bioinformatics, RIKEN Center for Integrative Medical Sciences (IMS-RCAI), Yokohama Institute, Yokohama, Kanagawa 230-0045, Japan;Department of Rheumatology, Command Airforce Hospital, Bangalore 560008, India;Centre for Excellence in Bioinformatics, School of Life Sciences, Pondicherry University, Pondicherry, Puducherry 605014, India;Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA;Amrita School of Biotechnology, Amrita University, Kollam, Kerala 690525, India;Rajiv Gandhi University of Health Sciences, Bangalore, Karnataka 560041, India

关键词: Glycosylation;    Joint destruction;    Cartilage;    Body fluid;   

Others  :  803008
DOI  :  10.1186/1559-0275-11-6

 received in 2013-08-06, accepted in 2014-01-06,  发布年份 2014

【 摘 要 】

Background

Osteoarthritis is a chronic musculoskeletal disorder characterized mainly by progressive degradation of the hyaline cartilage. Patients with osteoarthritis often postpone seeking medical help, which results in the diagnosis being made at an advanced stage of cartilage destruction. Sustained efforts are needed to identify specific markers that might help in early diagnosis, monitoring disease progression and in improving therapeutic outcomes. We employed a multipronged proteomic approach, which included multiple fractionation strategies followed by high resolution mass spectrometry analysis to explore the proteome of synovial fluid obtained from osteoarthritis patients. In addition to the total proteome, we also enriched glycoproteins from synovial fluid using lectin affinity chromatography.

Results

We identified 677 proteins from synovial fluid of patients with osteoarthritis of which 545 proteins have not been previously reported. These novel proteins included ADAM-like decysin 1 (ADAMDEC1), alanyl (membrane) aminopeptidase (ANPEP), CD84, fibulin 1 (FBLN1), matrix remodelling associated 5 (MXRA5), secreted phosphoprotein 2 (SPP2) and spondin 2 (SPON2). We identified 300 proteins using lectin affinity chromatography, including the glycoproteins afamin (AFM), attractin (ATRN), fibrillin 1 (FBN1), transferrin (TF), tissue inhibitor of metalloproteinase 1 (TIMP1) and vasorin (VSN). Gene ontology analysis confirmed that a majority of the identified proteins were extracellular and are mostly involved in cell communication and signaling. We also confirmed the expression of ANPEP, dickkopf WNT signaling pathway inhibitor 3 (DKK3) and osteoglycin (OGN) by multiple reaction monitoring (MRM) analysis of osteoarthritis synovial fluid samples.

Conclusions

We present an in-depth analysis of the synovial fluid proteome from patients with osteoarthritis. We believe that the catalog of proteins generated in this study will further enhance our knowledge regarding the pathophysiology of osteoarthritis and should assist in identifying better biomarkers for early diagnosis.

【 授权许可】

   
2014 Balakrishnan et al.; licensee BioMed Central Ltd.

【 图 表 】

Figure 1.

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