+ |
MMP9 | down-regulates quantity by destabilization
cleavage
|
PZP |
0.355 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261785 |
Leu778 |
WKAGAFClSEDAGLG |
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: |
1 |
Organism: |
In Vitro |
+ |
MMP2 | down-regulates quantity by destabilization
cleavage
|
PZP |
0.335 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261796 |
Thr718 |
PYVPQLGtYNVIPLN |
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: |
1 |
Organism: |
In Vitro |
+ |
PZP | down-regulates activity
binding
|
MMP2 |
0.335 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261804 |
|
|
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 |
+ |
PZP | down-regulates activity
binding
|
MMP9 |
0.355 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261802 |
|
|
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 |