Quantitative Proteomic Profiling of Human Articular Cartilage Degradation in Osteoarthritis

Osteoarthritis (OA) is the most common rheumatic pathology and is characterized primarily by articular cartilage degradation. Despite its high prevalence, there is no effective therapy to slow disease progression or regenerate the damaged tissue. Therefore, new diagnostic and monitoring tests for OA...

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Bibliographic Details
Published in:Journal of proteome research 2014-12, Vol.13 (12), p.6096-6106
Main Authors: Lourido, Lucía, Calamia, Valentina, Mateos, Jesús, Fernández-Puente, Patricia, Fernández-Tajes, Juan, Blanco, Francisco J, Ruiz-Romero, Cristina
Format: Article
Language:English
Subjects:
Aged
Aged, 80 and over
Biomarkers - metabolism
Blotting, Western
Cartilage, Articular - metabolism
Cartilage, Articular - pathology
Cell Adhesion Molecules - genetics
Cell Adhesion Molecules - metabolism
Cell Adhesion Molecules - secretion
Chromatography, Liquid
Female
Humans
Male
Middle Aged
Multivariate Analysis
Osteoarthritis - diagnosis
Osteoarthritis - genetics
Osteoarthritis - metabolism
Osteoprotegerin - genetics
Osteoprotegerin - metabolism
Osteoprotegerin - secretion
Proteome - genetics
Proteome - metabolism
Proteome - secretion
Proteomics - methods
Reverse Transcriptase Polymerase Chain Reaction
Signal Transduction
Synovial Fluid - metabolism
Tandem Mass Spectrometry
Tissue Culture Techniques
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Summary:Osteoarthritis (OA) is the most common rheumatic pathology and is characterized primarily by articular cartilage degradation. Despite its high prevalence, there is no effective therapy to slow disease progression or regenerate the damaged tissue. Therefore, new diagnostic and monitoring tests for OA are urgently needed, which would also promote the development of alternative therapeutic strategies. In the present study, we have performed an iTRAQ-based quantitative proteomic analysis of secretomes from healthy human articular cartilage explants, comparing their protein profile to those from unwounded (early disease) and wounded (advanced disease) zones of osteoarthritic tissue. This strategy allowed us to identify a panel of 76 proteins that are distinctively released by the diseased tissue. Clustering analysis allowed the classification of proteins according to their different profile of release from cartilage. Among these proteins, the altered release of osteoprotegerin (decreased in OA) and periostin (increased in OA), both involved in bone remodelling processes, was verified in further analyses. Moreover, periostin was also increased in the synovial fluid of OA patients. Altogether, the present work provides a novel insight into the mechanisms of human cartilage degradation and a number of new cartilage-characteristic proteins with possible biomarker value for early diagnosis and prognosis of OA.
ISSN:1535-3893
1535-3907
DOI:10.1021/pr501024p