ABSTRACT
Osteoarthritis (OA) is one of the most common diseases worldwide caused by chronic degeneration of the joints. Its high prevalence and the involvement of several tissues define OA as a highly heterogeneous disease. New biological markers to evaluate the progression of the pathology and improve its prognosis are needed. Among all the different -omic strategies applied to OA, solution phase bottom-up proteomics has made an extensive contribution to the field of biomarker research. However, new technologies for protein analysis should be considered for a better understanding of the disease. This review focuses on complementary proteomic methodologies and new technologies for translational research of OA and other rheumatic pathologies, especially mass spectrometry imaging and protein imaging methods not applied by the OA community yet.
Subject(s)
Osteoarthritis , Proteomics , Biomarkers , Humans , Mass Spectrometry , Osteoarthritis/diagnosis , ProteinsABSTRACT
Osteoarthritis (OA) is one of the most common musculoskeletal diseases, characterized by the progressive deterioration of articular cartilage. Although the disease has been well studied in the past few years, the endogenous metabolic composition and more importantly the spatial information of these molecules in cartilage is still poorly understood. Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry imaging (MSI) has been previously used for the investigation of the bimolecular distribution of proteins and lipids through the in situ analysis of cartilage tissue sections. MALDI-MSI as a tool to detect metabolites remains challenging, as these species have low abundance and degrade rapidly. In this work, we present a complete methodology, from sample preparation to data analysis for the detection of endogenous metabolites on cartilage by MSI. Our results demonstrate for the first time the ability to detect small molecules in fragile, challenging tissues through an optimized protocol, and render MSI as a tool towards a better understanding of OA.