| + |
MMP2 | down-regulates quantity by destabilization 
cleavage
|
A2M |
0.62 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261739 |
Arg719 |
VMGRGHArLVHVEEP |
in vitro |
|
| pmid |
sentence |
| 9344465 |
The complex formation was confirmed by the use of 125I-labeled matrix metalloproteinase-2. The cleavage sites in the "bait" regions following formation of high-molecular-weight complexes of matrix metalloproteinases with the alpha-macroglobulins were determined by protein sequence analysis. Pregnancy zone protein was cleaved at Thr693-Tyr694 and alpha2-macroglobulin at Gly679-Leu680 and Arg696-Leu697 by matrix metalloproteinase-2. Matrix metalloproteinase-9 cleaved alpha2-macroglobulin at the same site as matrix metalloproteinase-2, but cleavage of pregnancy zone protein was at Leu753-Ser754.|MMP-2 and MMP-9 cause a significant degradation of these bands and the background, a degradation which is prevented by both a2M and PZP. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261780 |
Gly702 |
YEMHGPEgLRVGFYE |
in vitro |
|
| pmid |
sentence |
| 9344465 |
The complex formation was confirmed by the use of 125I-labeled matrix metalloproteinase-2. The cleavage sites in the "bait" regions following formation of high-molecular-weight complexes of matrix metalloproteinases with the alpha-macroglobulins were determined by protein sequence analysis. Pregnancy zone protein was cleaved at Thr693-Tyr694 and alpha2-macroglobulin at Gly679-Leu680 and Arg696-Leu697 by matrix metalloproteinase-2. Matrix metalloproteinase-9 cleaved alpha2-macroglobulin at the same site as matrix metalloproteinase-2, but cleavage of pregnancy zone protein was at Leu753-Ser754.|MMP-2 and MMP-9 cause a significant degradation of these bands and the background, a degradation which is prevented by both a2M and PZP. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
MMP9 | down-regulates quantity by destabilization
cleavage
|
A2M |
0.471 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261740 |
Arg719 |
VMGRGHArLVHVEEP |
in vitro |
|
| pmid |
sentence |
| 9344465 |
The complex formation was confirmed by the use of 125I-labeled matrix metalloproteinase-2. The cleavage sites in the "bait" regions following formation of high-molecular-weight complexes of matrix metalloproteinases with the alpha-macroglobulins were determined by protein sequence analysis. Pregnancy zone protein was cleaved at Thr693-Tyr694 and alpha2-macroglobulin at Gly679-Leu680 and Arg696-Leu697 by matrix metalloproteinase-2. Matrix metalloproteinase-9 cleaved alpha2-macroglobulin at the same site as matrix metalloproteinase-2, but cleavage of pregnancy zone protein was at Leu753-Ser754.|MMP-2 and MMP-9 cause a significant degradation of these bands and the background, a degradation which is prevented by both a2M and PZP. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261781 |
Gly702 |
YEMHGPEgLRVGFYE |
in vitro |
|
| pmid |
sentence |
| 9344465 |
The complex formation was confirmed by the use of 125I-labeled matrix metalloproteinase-2. The cleavage sites in the "bait" regions following formation of high-molecular-weight complexes of matrix metalloproteinases with the alpha-macroglobulins were determined by protein sequence analysis. Pregnancy zone protein was cleaved at Thr693-Tyr694 and alpha2-macroglobulin at Gly679-Leu680 and Arg696-Leu697 by matrix metalloproteinase-2. Matrix metalloproteinase-9 cleaved alpha2-macroglobulin at the same site as matrix metalloproteinase-2, but cleavage of pregnancy zone protein was at Leu753-Ser754.|MMP-2 and MMP-9 cause a significant degradation of these bands and the background, a degradation which is prevented by both a2M and PZP. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CTSE | down-regulates quantity by destabilization
cleavage
|
A2M |
0.388 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266977 |
Phe834 |
QLEASPAfLAVPVEK |
in vitro |
|
| pmid |
sentence |
| 12631277 |
Disruption of structural and functional integrity of alpha 2-macroglobulin by cathepsin E|Analysis of the N-terminal amino-acid sequences of these proteins revealed that alpha 2M was selectively cleaved at the Phe811-Leu812 bond in about 100mer downstream of the bait region. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
A2M | down-regulates activity
binding
|
MMP2 |
0.62 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261803 |
|
|
in vitro |
|
| pmid |
sentence |
| 9344465 |
Both PZP and a2M collagenase complexes incubated with gelatin demonstrated a significant inhibition of the catalytic activity| MMP-2 and MMP-9 cause a significant degradation of these bands and the background, a degradation which is prevented by both a2M and PZP. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
A2M | down-regulates activity
binding
|
MMP9 |
0.471 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261801 |
|
|
in vitro |
|
| pmid |
sentence |
| 9344465 |
Both PZP and a2M collagenase complexes incubated with gelatin demonstrated a significant inhibition of the catalytic activity| MMP-2 and MMP-9 cause a significant degradation of these bands and the background, a degradation which is prevented by both a2M and PZP. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
A2M
- 
- 