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| Content Provider | Journal of Biological Chemistry (JBC) |
|---|---|
| Author | Kashiwagi, Masahide Tortorella, Micky Nagase, Hideaki Brew, Keith |
| Abstract | The proteoglycan aggrecan is an important major component of cartilage matrix that gives articular cartilage the ability to withstand compression. Increased breakdown of aggrecan is associated with the development of arthritis and is considered to be catalyzed by aggrecanases, members of the ADAM-TS family of metalloproteinases. Four endogenous tissue inhibitors of metalloproteinases (TIMPs) regulate the activities of functional matrix metalloproteinases (MMPs), enzymes that degrade most components of connective tissue, but no endogenous factors responsible for the regulation of aggrecanases have been found. We show here that the N-terminal inhibitory domain of TIMP-3, a member of the TIMP family that has functional properties distinct from other TIMPs, is a strong inhibitor of human aggrecanases 1 and 2, with K ivalues in the subnanomolar range. This truncated inhibitor, which lacks the C-terminal domain that is responsible for interactions with molecules other than active metalloproteinases, is produced at high yield by bacterial expression and folding from inclusion bodies. This provides a starting point for developing a biologically available aggrecanase inhibitor suitable for the treatment of arthritis. |
| Related Links | http://www.jbc.org/content/276/16/12501.abstract |
| Ending Page | 12504 |
| Starting Page | 12501 |
| Page Count | 4 |
| File Format | HTM / HTML PDF |
| ISSN | 00219258 |
| Journal | Journal of Biological Chemistry (JBC) |
| Issue Number | 16 |
| Volume Number | 276 |
| DOI | 10.1074/jbc.C000848200 |
| e-ISSN | 1083351X |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology |
| Publisher Date | 2001-04-20 |
| Access Restriction | Open |
| Subject Keyword | Tissue inhibitor of metalloproteinases (TIMP) Matrix metalloproteinase (MMP) Membrane-type matrix metalloproteinase (MT-MMP) A disintegrin and a metalloproteinase domain (ADAM) A disintegrin and a metalloproteinase domain with thrombospondin type-1 domains (ADAM-TS) Tumor necrosis factor-α converting enzyme (TACE) Polymerase chain reaction (PCR) Polyacrylamide gel electrophoresis (PAGE) Nitrilotriacetic acid (NTA) |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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