ADAMTS proteinases: a multi-domain, multi-functional family with roles in extracellular matrix turnover and arthritis

• Published in: Arthritis research & therapy Vol. 7; no. 4; pp. 160 - 169
• Main Authors: Jones, Gavin C, Riley, Graham P
• Format: Journal Article
• Language: English
• Published: England BioMed Central Ltd 01-01-2005; BioMed Central
• Subjects: ADAM Proteins - chemistry; ADAM Proteins - genetics; ADAM Proteins - physiology; Animals; Arthritis, Rheumatoid - enzymology; Arthritis, Rheumatoid - genetics; Extracellular Matrix - enzymology; Extracellular Matrix - genetics; Humans; Multigene Family; Protein Structure, Tertiary; Review
• ISSN: 1478-6354; 1478-6362
• DOI: 10.1186/ar1783

Members of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) family are known to influence development, angiogenesis, coagulation and progression of arthritis. As proteinases their substrates include the von Willebrand factor precursor and extracellular matrix components such as procollagen, hyalectans (hyaluronan-binding proteoglycans including aggrecan), decorin, fibromodulin and cartilage oligomeric matrix protein. ADAMTS levels and activities are regulated at multiple levels through the control of gene expression, mRNA splicing, protein processing and inhibition by TIMP (tissue inhibitor of metalloproteinases). A recent screen of human cartilage has shown that multiple members of the ADAMTS family may be important in connective tissue homeostasis and pathology.