| + |
MMP2 | down-regulates quantity by destabilization 
cleavage
|
A2M |
0.636 |
| 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 |
| + |
MMP25 | up-regulates activity 
cleavage
|
MMP2 |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256345 |
Asn109 |
CGNPDVAnYNFFPRK |
in vitro |
|
| pmid |
sentence |
| 14583471 |
Direct activation of pro-matrix metalloproteinase-2 by leukolysin/membrane-type 6 matrix metalloproteinase/matrix metalloproteinase 25 at the asn(109)-Tyr bond. Leukolysin Cleaves ProMMP-2 at Asn66-Leu and Asn109-Tyr. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256346 |
Asn66 |
GCPKESCnLFVLKDT |
in vitro |
|
| pmid |
sentence |
| 14583471 |
Direct activation of pro-matrix metalloproteinase-2 by leukolysin/membrane-type 6 matrix metalloproteinase/matrix metalloproteinase 25 at the asn(109)-Tyr bond. Leukolysin Cleaves ProMMP-2 at Asn66-Leu and Asn109-Tyr. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
MMP2 | down-regulates quantity by destabilization
cleavage
|
DCN |
0.697 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256349 |
Glu30 |
GLFDFMLeDEASGIG |
in vitro |
|
| pmid |
sentence |
| 9148753 |
Degradation of decorin by matrix metalloproteinases. These data indicate proteolytic degradation of DCN by MMP-2, MMP-3 and MMP-7, and suggest the possibility that, under pathophysiological conditions, the digestion by the MMPs may induce tissue reactions mediated by TGF-beta1 released from DCN in the connective tissues. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256350 |
Ser240 |
ISRVDAAsLKGLNNL |
in vitro |
|
| pmid |
sentence |
| 9148753 |
Degradation of decorin by matrix metalloproteinases. These data indicate proteolytic degradation of DCN by MMP-2, MMP-3 and MMP-7, and suggest the possibility that, under pathophysiological conditions, the digestion by the MMPs may induce tissue reactions mediated by TGF-beta1 released from DCN in the connective tissues. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
MMP2 | down-regulates quantity by destabilization
cleavage
|
HAPLN1 |
0.338 |
| 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 |
| + |
MMP2 | down-regulates quantity by destabilization
cleavage
|
PZP |
0.328 |
| 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 |
| + |
MMP2 | down-regulates 
|
ECM |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272387 |
|
|
|
|
| pmid |
sentence |
| 17318226 |
Historically, MMPs were thought to function mainly as enzymes that degrade structural components of the ECM. |
|
| Publications: |
1 |
| + |
NODAL | up-regulates quantity by expression 
transcriptional regulation
|
MMP2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251940 |
|
|
Homo sapiens |
GBM-8401 Cell |
| pmid |
sentence |
| 20383200 |
Ectopic expression of Nodal or activation of Nodal signaling by addition of rNodal increased MMP-2 protein level and cell invasion. the expression level of Nodal correlates well with MMP-2 expression and cell invasion. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MMP2 | up-regulates
|
ECM_disassembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272364 |
|
|
|
|
| pmid |
sentence |
| 17318226 |
Historically, MMPs were thought to function mainly as enzymes that degrade structural components of the ECM. |
|
| Publications: |
1 |
| + |
MMP2 | up-regulates activity
cleavage
|
LAMC2 |
0.474 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253240 |
|
|
|
|
| pmid |
sentence |
| 9211848 |
Induction of Cell Migration by Matrix Metalloprotease-2 Cleavage of Laminin-5|MMP2 cleaved the Ln-5 gamma2 subunit at residue 587, exposing a putative cryptic promigratory site on Ln-5 that triggers cell motility. This altered form of Ln-5 is found in tumors and in tissues undergoing remodeling, but not in quiescent tissues. Cleavage of Ln-5 by MMP2 and the resulting activation of the Ln-5 cryptic site may provide new targets for modulation of tumor cell invasion and tissue remodeling. |
|
| Publications: |
1 |
| + |
MMP2 | up-regulates
cleavage
|
TGFB1 |
0.554 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-74384 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10652271 |
We also demonstrate that mmp-9, as well as its relative, mmp-2, cleave latent transforming growth factor-beta (tgf-beta), which constitutes a novel mechanism of tgf-beta activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TWIST1 | up-regulates quantity by expression
transcriptional regulation
|
MMP2 |
0.377 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255525 |
|
|
Homo sapiens |
GBM-8401 Cell |
| pmid |
sentence |
| 20646316 |
Individual genes upregulated by TWIST1 known to promote EMT and/or GBM invasion included SNAI2, MMP2, HGF, FAP and FN1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TP53 | up-regulates quantity by expression
transcriptional regulation
|
MMP2 |
0.447 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255432 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10029407 |
p53 transcriptionally activates expression of the genes encoding epidermal growth factor receptor, matrix metalloproteinase (MMP)-2, cathepsin D, and thrombospondin-1 but represses expression of the genes encoding basic fibroblast growth factor and multidrug resistance-1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MMP2 | up-regulates quantity
binding
|
LRP2 |
0.343 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265255 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 28659595 |
We show that megalin/LRP-2 acts as an endocytic receptor for proMMP-2:TIMP-2 complex. We found that RAP, an antagonist of the LDL receptor family18, competed with binding of proMMP-2:TIMP-2 complex onto rat BN16 epithelial cells. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PZP | down-regulates activity
binding
|
MMP2 |
0.328 |
| 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 |
| + |
RUNX2 | up-regulates quantity by expression
transcriptional regulation
|
MMP2 |
0.329 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255082 |
|
|
Homo sapiens |
Thyroid Cancer Cell Line |
| pmid |
sentence |
| 22641097 |
Effective silencing of Runx2 by short interfering RNA (siRNA) demonstrated downregulation of EMT-related molecules (SNAI2, SNAI3 and TWIST1), MMP2 and vasculogenic factors (VEGFA and VEGFC) in thyroid carcinoma cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NME1 | down-regulates quantity by repression
transcriptional regulation
|
MMP2 |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255165 |
|
|
Homo sapiens |
MDA-MB-435 Cell |
| pmid |
sentence |
| 17671192 |
To elucidate the molecular mechanism of Nm23-H1 motility suppression, expression microarray analysis of an MDA-MB-435 cancer cell line overexpressing wild-type Nm23-H1 was done and cross-compared with expression profiles from lines expressing the P96S and S120G mutants. Nine genes, MET, PTN, SMO, FZD1, L1CAM, MMP2, NETO2, CTGF, and EDG2, were down-regulated by wild-type but not by mutant Nm23-H1 expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
A2M | down-regulates activity
binding
|
MMP2 |
0.636 |
| 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 |
| + |
MMP2 | up-regulates activity
cleavage
|
Laminin-5 |
0.464 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253239 |
|
|
|
|
| pmid |
sentence |
| 9211848 |
Induction of Cell Migration by Matrix Metalloprotease-2 Cleavage of Laminin-5|MMP2 cleaved the Ln-5 gamma2 subunit at residue 587, exposing a putative cryptic promigratory site on Ln-5 that triggers cell motility. This altered form of Ln-5 is found in tumors and in tissues undergoing remodeling, but not in quiescent tissues. Cleavage of Ln-5 by MMP2 and the resulting activation of the Ln-5 cryptic site may provide new targets for modulation of tumor cell invasion and tissue remodeling. |
|
| Publications: |
1 |
4.0
MMP2
- 
- 