Usurped SLRPs novel arthritis biomarkers exposed by catabolism of small leucine-rich proteoglycans 英文参考文献.docVIP

Available online /content/8/2/106 Commentary Usurped SLRPs: novel arthritis biomarkers exposed by catabolism of small leucine-rich proteoglycans? Carl R Flannery Wyeth Research, Cambridge, MA, USA Corresponding author: Carl R Flannery, cflannery@ Published: 13 March 2006 Arthritis Research Therapy 2006, 8:106 (doi:10.1186/ar1925) This article is online at /content/8/2/106 ? 2006 BioMed Central Ltd See related research by Monfort et al. in issue 8.1 [/content/8/1/R26] and Young et al. in issue 7.4 [/content/7/4/R852] Abstract during active progression of OA, thus concomitantly advocating the utility of monitoring SLRP catabolites as a promising biomarker strategy for evaluating OA disease status. Proteolytic degradation of articular cartilage macromolecules, including the large aggregating cartilage proteoglycan (aggrecan) and small leucine-rich proteoglycans (SLRPs), is a prominent pathophysiological feature of arthritic diseases such as osteo- arthritis (OA). Molecular profiling and monitoring of soluble/ circulating proteoglycan catabolites that may be released from the cartilage matrix therefore represents an attractive strategy for evaluating OA disease progression and intervention. The recent identification of discrete metalloproteinase-sensitive SLRP cleavage sites, and complementary neoepitope-bearing SLRP catabolites, Members of the SLRP gene family play vital roles in a variety of tissues and extracellular matrices, comprising binding and regulation of collagen fibrils, as well as modulation of cellular responses [3]. As exemplified by knockout mice [4], SLRP deficiencies in vivo lead to the development of corneal, dermatological and musculoskeletal diseases (including OA), indicating that the connate functions of SLRPs could be profoundly impacted by post-translational (i.e. proteolytic) processing events. Indeed, and with pertin