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Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP)
Author(s) -
Stracke Jan O.,
Fosang Amanda J.,
Last Karena,
Mercuri Francesca A.,
Pendás Alberto M.,
Llano Elena,
Perris Roberto,
Di Cesare Paul E.,
Murphy Gillian,
Knäuper Vera
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01819-6
Subject(s) - aggrecan , cartilage oligomeric matrix protein , matrix metalloproteinase , extracellular matrix , cartilage , aggrecanase , cleave , matrix metalloproteinase 3 , chemistry , type ii collagen , cleavage (geology) , microbiology and biotechnology , blot , proteolytic enzymes , metalloproteinase , proteoglycan , matrix (chemical analysis) , adamts , biochemistry , enzyme , biology , osteoarthritis , anatomy , pathology , medicine , thrombospondin , articular cartilage , gene , alternative medicine , fracture (geology) , paleontology , chromatography
Matrix metalloproteinase (MMP)‐19 and MMP‐20 (enamelysin) are two recently discovered members of the MMP family. These enzymes are involved in the degradation of the various components of the extracellular matrix (ECM) during development, haemostasis and pathological conditions. Whereas MMP‐19 mRNA is found widely expressed in body tissues, including the synovium of normal and rheumatoid arthritic patients, MMP‐20 expression is restricted to the enamel organ. In this study we investigated the ability of MMP‐19 and MMP‐20 to cleave two of the macromolecules characterising the cartilage ECM, namely aggrecan and the cartilage oligomeric matrix protein (COMP). Both MMPs hydrolysed aggrecan efficiently at the well‐described MMP cleavage site between residues Asn 341 and Phe 342 , as shown by Western blotting using neo‐epitope antibodies. Furthermore, the two enzymes cleaved COMP in a distinctive manner, generating a major proteolytic product of 60 kDa. Our results suggest that MMP‐19 may participate in the degradation of aggrecan and COMP in arthritic disease, whereas MMP‐20, due to its unique expression pattern, may primarily be involved in the turnover of these molecules during tooth development.