proteinases in the joint clinical relevance of proteinases in joint destruction蛋白酶联合临床意义的蛋白酶在关节破坏.pdfVIP

Available online /content/9/5/221 Review Proteinases in the joint: clinical relevance of proteinases in joint destruction Yvonne Rengel, Caroline Ospelt and Steffen Gay Center of Experimental Rheumatology, University Hospital Zürich, Gloriastrasse, CH-8091 Zurich, Switzerland Corresponding author: Steffen Gay, steffengay@usz.ch Published: 31 October 2007 Arthritis Research Therapy 2007, 9:221 (doi:10.1186/ar2304) This article is online at /content/9/5/221 © 2007 BioMed Central Ltd Abstract General features of proteinases Proteinases are involved in essential steps in cartilage and bone Proteases selectively hydrolyze a peptide bond in a poly- homeostasis. Consequently, efforts have been made to establish peptide chain of a target molecule. Depending on the their potential role in the pathology of rheumatic conditions such as position of the peptide bond, proteases are referred to as rheumatoid arthritis, osteoarthritis and spondyloarthritis. Matrix exopeptidases or endopeptidases. Exopeptidases specifically metalloproteinases (MMPs) are sensitive markers of disease cleave substrates at the amino-terminal or carboxyl-terminal severity and response to treatment, and therefore they have poten- positions of polypeptides, and therefore can be subdivided tial in the assessment of rheumatic diseases. Despite disappointing early results with synthetic inhibitors of MMPs, there is still much into aminopeptidases and carboxypeptidases [5,6]. Endo- s