| + |
MMP19 | down-regulates quantity by destabilization 
cleavage
|
ACAN |
0.411 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266978 |
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-266980 |
|
|
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 |
| + |
MMP3 | down-regulates quantity by destabilization
cleavage
|
ACAN |
0.729 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266986 |
Asn360 |
DFVDIPEnFFGVGGE |
Homo sapiens |
|
| pmid |
sentence |
| 9202061 |
Aggrecan Degradation in Human Cartilage Evidence for both Matrix Metalloproteinase and Aggrecanase Activity in Normal, Osteoarthritic, and Rheumatoid Joints|Stromelysin-1 (MMP-3), as well as other MMPs, cleave aggrecan in the interglobular domain between Asn341 and Phe342 to generate a G1 fragment with the COOH terminus VDIPEN341 (11–13). This fragment has been isolated and identified by NH2-terminal sequence analysis from human OA cartilage (11). A second proteolytic activity identified as “aggrecanase” also cleaves aggrecan in the interglobular domain, but between Glu373 and Ala374 (19–24), generating a G1 fragment with a COOH terminus of NITEGE374 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Cartilage |
| + |
MMP20 | down-regulates quantity by destabilization
cleavage
|
ACAN |
0.495 |
| 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 |
| + |
ADAMTS4 | down-regulates quantity by destabilization
cleavage
|
ACAN |
0.76 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266984 |
Glu392 |
PRNITEGeARGSVIL |
Homo sapiens |
|
| pmid |
sentence |
| 9202061 |
Aggrecan Degradation in Human Cartilage Evidence for both Matrix Metalloproteinase and Aggrecanase Activity in Normal, Osteoarthritic, and Rheumatoid Joints|Stromelysin-1 (MMP-3), as well as other MMPs, cleave aggrecan in the interglobular domain between Asn341 and Phe342 to generate a G1 fragment with the COOH terminus VDIPEN341 (11–13). This fragment has been isolated and identified by NH2-terminal sequence analysis from human OA cartilage (11). A second proteolytic activity identified as “aggrecanase” also cleaves aggrecan in the interglobular domain, but between Glu373 and Ala374 (19–24), generating a G1 fragment with a COOH terminus of NITEGE373 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ADAMTS5 | down-regulates quantity by destabilization
cleavage
|
ACAN |
0.758 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266985 |
Glu392 |
PRNITEGeARGSVIL |
Homo sapiens |
|
| pmid |
sentence |
| 9202061 |
Aggrecan Degradation in Human Cartilage Evidence for both Matrix Metalloproteinase and Aggrecanase Activity in Normal, Osteoarthritic, and Rheumatoid Joints|Stromelysin-1 (MMP-3), as well as other MMPs, cleave aggrecan in the interglobular domain between Asn341 and Phe342 to generate a G1 fragment with the COOH terminus VDIPEN341 (11–13). This fragment has been isolated and identified by NH2-terminal sequence analysis from human OA cartilage (11). A second proteolytic activity identified as “aggrecanase” also cleaves aggrecan in the interglobular domain, but between Glu373 and Ala374 (19–24), generating a G1 fragment with a COOH terminus of NITEGE374 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACAN | up-regulates 
|
ECM_synthesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266982 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10922468 |
Degradation of aggrecan, the major proteoglycan of the cartilage ECM responsible for the load-bearing and elastic properties of this tissue, is one of the earliest detectable events in arthritic cartilage degeneration. MMPs have been implicated in proteolysis and the subsequent loss of aggrecan from cartilage during arthritis |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266983 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16051604 |
Cartilage oligomeric matrix protein/thrombospondin 5 (COMP/TSP5) is a major component of the extracellular matrix of the musculoskeletal system. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SIRT1 | up-regulates quantity by expression 
transcriptional regulation
|
ACAN |
0.326 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255142 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21337390 |
The inhibition of SIRT1 by siRNA induced OA-like gene expression changes, namely the significant down-regulation of aggrecan and up-regulation of COL10A1 and ADAMTS-5. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACAN | up-regulates activity
binding
|
A5/b1 integrin |
0.329 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266988 |
|
|
Homo sapiens |
Chondrocyte Cell Line |
| pmid |
sentence |
| 16051604 |
Cartilage Oligomeric Matrix Protein/Thrombospondin 5 Supports Chondrocyte Attachment through Interaction with Integrins|We show that COMP/TSP5 can support chondrocyte attachment and that the RGD sequence in COMP/TSP5 and the integrin receptors alpha5beta1 and alphaVbeta3 on the chondrocytes are involved in mediating this attachment. The interactions of COMP/TSP5 with the integrins are dependent on COMP/TSP5 conformation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACAN | up-regulates activity
binding
|
Av/b3 integrin |
0.269 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266987 |
|
|
Homo sapiens |
Chondrocyte Cell Line |
| pmid |
sentence |
| 16051604 |
Cartilage Oligomeric Matrix Protein/Thrombospondin 5 Supports Chondrocyte Attachment through Interaction with Integrins|We show that COMP/TSP5 can support chondrocyte attachment and that the RGD sequence in COMP/TSP5 and the integrin receptors alpha5beta1 and alphaVbeta3 on the chondrocytes are involved in mediating this attachment. The interactions of COMP/TSP5 with the integrins are dependent on COMP/TSP5 conformation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ACAN
- 
- 