| + |
MMP9 | down-regulates quantity by destabilization 
cleavage
|
A2M |
0.49 |
| 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 |
| + |
MMP9 | down-regulates quantity by destabilization
cleavage
|
HAPLN1 |
0.342 |
| 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 |
| + |
MMP9 | down-regulates quantity by destabilization
cleavage
|
PZP |
0.35 |
| 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 |
| + |
ETS1 | up-regulates quantity by expression 
transcriptional regulation
|
MMP9 |
0.378 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254083 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22270366 |
VEGF-induced MMP-9 and MMP-13 promoter activities were down-regulated in ETS-1 siRNA-transfected cells. it is hypothesized that the activation of PI3K/AKT and p38 MAPK by VEGF results in ETS-1 gene expression, which activates MMP-9 and MMP-13, leading to the invasion and scattering of SKOV-3 cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
A2M | down-regulates activity
binding
|
MMP9 |
0.49 |
| 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 |
| + |
MMP9 | down-regulates 
|
ECM |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272399 |
|
|
|
|
| pmid |
sentence |
| 17318226 |
Historically, MMPs were thought to function mainly as enzymes that degrade structural components of the ECM. |
|
| Publications: |
1 |
| + |
SPRY4 | down-regulates activity
|
MMP9 |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253037 |
|
|
Homo sapiens |
Non-small Cell Lung Cancer Cell |
| pmid |
sentence |
| 20501643 |
When Spry4 was stably transfected into H157 and H2122 NSCLC cell lines, decreased migration and invasion were observed. Matrix metalloproteinase-9 activity was decreased, and the expression of matrix metalloproteinase inhibitors TIMP1 and CD82 were increased. Stable expression of Spry4 led to reduced cell growth and reduced anchorage-independent growth in NSCLC cell lines, along with upregulation of tumor suppressors p53 and p21. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SPDEF | down-regulates quantity by repression
transcriptional regulation
|
MMP9 |
0.361 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255218 |
|
|
Homo sapiens |
PrEC Cell |
| pmid |
sentence |
| 22761428 |
Transcriptional analysis of several genes associated with tumor metastasis, invasion, and the epithelial-mesenchymal transition demonstrated that SPDEF expression selectively down-regulated MMP9 and MMP13 in prostate cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MMP9 | up-regulates 
cleavage
|
TGFB1 |
0.595 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-74461 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10652271 |
We also demonstrate that mmp-9, as well as its relative, mmp-2, cleave latent transforming growth factor-_ (tgf-_), which constitutes a novel mechanism of tgf-_ activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
USP6 | up-regulates quantity by expression
transcriptional regulation
|
MMP9 |
0.328 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164946 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20418905 |
In this study we show that tre17 is sufficient to induce expression of mmp-9 and mmp-10, in a manner requiring its usp activity, but not its ability to bind arf6. Tre17 induces transcription of mmp-9 through activation of nuclear factor-kappab (nf-kappab), mediated in part by the gtpase rhoa and its effector kinase, rock. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NfKb-p65/p50 | up-regulates quantity by expression
transcriptional regulation
|
MMP9 |
0.419 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254798 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15536164 |
Biglycan, NGAL, and MMP-9 are transcriptionally up-regulated by NF-kappaB, a transcription factor that is activated in FAP nerves and SG. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CCR6 | up-regulates activity
|
MMP9 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278042 |
|
|
Homo sapiens |
Pancreatic Cancer Cell |
| pmid |
sentence |
| 15652956 |
We hypothesized that MIP-3alpha promotes pancreatic cancer invasion through the up-regulation of MMP-9, a Type 4 collagenase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PZP | down-regulates activity
binding
|
MMP9 |
0.35 |
| 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 |
| + |
TIMP1 | down-regulates activity
binding
|
MMP9 |
0.807 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278116 |
|
|
Homo sapiens |
Peripheral Blood Cell |
| pmid |
sentence |
| 36935521 |
Tissue inhibitor of metalloproteinase (TIMP-1) is an inhibitor of MMP-9 that binds to MMP-9 precursors and to the active form. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277734 |
|
|
Homo sapiens |
Pancreatic Cancer Cell |
| pmid |
sentence |
| 38339310 |
Given that MMP-9 is able to degrade the ECM, which is an essential step in tumor cell extravasation and metastasis, and it is highly expressed in PDAC, CXCL12 may be playing a similar role in upregulating MMPs in PDAC |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MMP9 | up-regulates
|
ECM_disassembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272376 |
|
|
|
|
| pmid |
sentence |
| 17318226 |
Historically, MMPs were thought to function mainly as enzymes that degrade structural components of the ECM. |
|
| Publications: |
1 |
| + |
SNAI2 | up-regulates quantity by expression
transcriptional regulation
|
MMP9 |
0.453 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255170 |
|
|
Homo sapiens |
Prostate Cancer Cell Line |
| pmid |
sentence |
| 22074556 |
We demonstrated that forced expression of SLUG elevated CXCR4 and CXCL12 expression in human prostate cancer cell lines PC3, DU145, 22RV1, and LNCaP; conversely, reduced expression of SLUG by shRNA downregulated CXCR4 and CXCL12 expression at RNA and protein levels in prostate cancer cells. Furthermore, ectopic expression of SLUG increased MMP9 expression and activity in PC3, 22RV1, and DU-145 cells, and SLUG knockdown by shRNA downregulated MMP9 expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
MMP9
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- 