| + |
MMP2 | down-regulates quantity by destabilization 
cleavage
|
HAPLN1 |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256327 |
His31 |
LDHDRAIhIQAENGP |
in vitro |
|
| pmid |
sentence |
| 7694569 |
Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein. Sequencing studies of modified link protein components revealed that stromelysins-1 and -2, gelatinases A and B and collagenase cleaved specifically between His16 and Ile17, and matrilysin, stromelysin-2 and gelatinase A cleaved between Leu25 and Leu26. Based on previously determined in situ cleavage sites it is evident that matrix metalloproteinases are not solely responsible for the accumulation of link protein degradation products in adult human cartilage, indicating that additional proteolytic agents are involved in the normal catabolism of human cartilage matrix. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256333 |
Leu40 |
QAENGPHlLVEAEQA |
in vitro |
|
| pmid |
sentence |
| 7694569 |
Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein. Sequencing studies of modified link protein components revealed that stromelysins-1 and -2, gelatinases A and B and collagenase cleaved specifically between His16 and Ile17, and matrilysin, stromelysin-2 and gelatinase A cleaved between Leu25 and Leu26. Based on previously determined in situ cleavage sites it is evident that matrix metalloproteinases are not solely responsible for the accumulation of link protein degradation products in adult human cartilage, indicating that additional proteolytic agents are involved in the normal catabolism of human cartilage matrix. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
MMP3 | down-regulates quantity by destabilization
cleavage
|
HAPLN1 |
0.392 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256330 |
His31 |
LDHDRAIhIQAENGP |
in vitro |
|
| pmid |
sentence |
| 7694569 |
Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein. Sequencing studies of modified link protein components revealed that stromelysins-1 and -2, gelatinases A and B and collagenase cleaved specifically between His16 and Ile17, and matrilysin, stromelysin-2 and gelatinase A cleaved between Leu25 and Leu26. Based on previously determined in situ cleavage sites it is evident that matrix metalloproteinases are not solely responsible for the accumulation of link protein degradation products in adult human cartilage, indicating that additional proteolytic agents are involved in the normal catabolism of human cartilage matrix. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MMP10 | down-regulates quantity by destabilization
cleavage
|
HAPLN1 |
0.329 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256331 |
His31 |
LDHDRAIhIQAENGP |
in vitro |
|
| pmid |
sentence |
| 7694569 |
Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein. Sequencing studies of modified link protein components revealed that stromelysins-1 and -2, gelatinases A and B and collagenase cleaved specifically between His16 and Ile17, and matrilysin, stromelysin-2 and gelatinase A cleaved between Leu25 and Leu26. Based on previously determined in situ cleavage sites it is evident that matrix metalloproteinases are not solely responsible for the accumulation of link protein degradation products in adult human cartilage, indicating that additional proteolytic agents are involved in the normal catabolism of human cartilage matrix. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256332 |
Leu40 |
QAENGPHlLVEAEQA |
in vitro |
|
| pmid |
sentence |
| 7694569 |
Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein. Sequencing studies of modified link protein components revealed that stromelysins-1 and -2, gelatinases A and B and collagenase cleaved specifically between His16 and Ile17, and matrilysin, stromelysin-2 and gelatinase A cleaved between Leu25 and Leu26. Based on previously determined in situ cleavage sites it is evident that matrix metalloproteinases are not solely responsible for the accumulation of link protein degradation products in adult human cartilage, indicating that additional proteolytic agents are involved in the normal catabolism of human cartilage matrix. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
MMP9 | down-regulates quantity by destabilization
cleavage
|
HAPLN1 |
0.348 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256328 |
His31 |
LDHDRAIhIQAENGP |
in vitro |
|
| pmid |
sentence |
| 7694569 |
Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein. Sequencing studies of modified link protein components revealed that stromelysins-1 and -2, gelatinases A and B and collagenase cleaved specifically between His16 and Ile17, and matrilysin, stromelysin-2 and gelatinase A cleaved between Leu25 and Leu26. Based on previously determined in situ cleavage sites it is evident that matrix metalloproteinases are not solely responsible for the accumulation of link protein degradation products in adult human cartilage, indicating that additional proteolytic agents are involved in the normal catabolism of human cartilage matrix. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MMP7 | down-regulates quantity by destabilization
cleavage
|
HAPLN1 |
0.327 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256329 |
Leu40 |
QAENGPHlLVEAEQA |
in vitro |
|
| pmid |
sentence |
| 7694569 |
Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein. Sequencing studies of modified link protein components revealed that stromelysins-1 and -2, gelatinases A and B and collagenase cleaved specifically between His16 and Ile17, and matrilysin, stromelysin-2 and gelatinase A cleaved between Leu25 and Leu26. Based on previously determined in situ cleavage sites it is evident that matrix metalloproteinases are not solely responsible for the accumulation of link protein degradation products in adult human cartilage, indicating that additional proteolytic agents are involved in the normal catabolism of human cartilage matrix. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
HAPLN1
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- 