+ |
MMP20 | down-regulates quantity by destabilization
cleavage
|
ACAN |
0.491 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266979 |
Asn360 |
DFVDIPEnFFGVGGE |
in vitro |
|
pmid |
sentence |
10922468 |
Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP)|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. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266981 |
|
|
in vitro |
|
pmid |
sentence |
10922468 |
Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP)|It has been suggested that MMPs play a role in the hydrolysis of COMP and, therefore, compromise the integrity of the cartilage ECM structure leading to the ultimate loss of joint function |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
MMP20 | down-regulates
|
ECM |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272388 |
|
|
|
|
pmid |
sentence |
17318226 |
Historically, MMPs were thought to function mainly as enzymes that degrade structural components of the ECM. |
|
Publications: |
1 |
+ |
MMP20 | up-regulates
|
ECM_disassembly |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272365 |
|
|
|
|
pmid |
sentence |
17318226 |
Historically, MMPs were thought to function mainly as enzymes that degrade structural components of the ECM. |
|
Publications: |
1 |