| + |
MMP7 | down-regulates quantity by destabilization 
cleavage
|
DCN |
0.593 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256352 |
Glu273 |
ANTPHLReLHLDNNK |
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-256351 |
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. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
MMP2 | down-regulates quantity by destabilization
cleavage
|
DCN |
0.682 |
| 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 |
| + |
MMP3 | down-regulates quantity by destabilization
cleavage
|
DCN |
0.659 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256353 |
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: |
1 |
Organism: |
In Vitro |
| + |
DCN | up-regulates quantity by expression 
transcriptional regulation
|
FBN1 |
0.578 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251893 |
|
|
Rattus norvegicus |
NRK Cell |
| pmid |
sentence |
| 17200203 |
Decorin Induces Fibrillin-1 Protein Expression in NRK Cells via IGF-IR. we report a novel mechanism of action that involves two key molecules: decorin, a small leucine-rich proteoglycan, and the IGF-IR. These two players, together with the downstream signaling pathway evoked by decorin-mediated activation of the receptor, lead to an enhanced translation of fibrillin-1 and its deposition in the extracellular environment both in vitro and in vivo. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
3.0
DCN
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