| + |
DPP3 | down-regulates quantity by destabilization 
cleavage
|
Angiotensin-2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268463 |
|
|
in vitro |
|
| pmid |
sentence |
| 34770898 |
Human dipeptidyl-peptidase III (hDPP III) is capable of specifically cleaving dipeptides from the N-terminal of small peptides with biological activity such as angiotensin II (Ang II, DRVYIHPF), and participates in blood pressure regulation, pain modulation, and the development of cancers in human biological activities. The binding of Ang II to hDPP III may lead to changes in the shape and size of subsite S1, an important catalytic site, so as to promote the decomposition of the substrate. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
DPP3 | down-regulates quantity by destabilization
cleavage
|
KEAP1 |
0.621 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268464 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 35278345 |
The influence of DPP3 on the Keap1-Nrf2/ARE signal pathway suggest a direct involvement of DPP3 in the oxidative stress response [8,14,31,53,99,100]. It was shown that DPP3 competes with Nrf2 through the ETGE motif to bind to Keap1 and consequently enhances the translocation of Nrf2 to the nucleus, thereby driving the expression of an array of genes encoding antioxidative enzymes [99]. More specifically, binding of DPP3 to Keap1 releases Nrf2, and thus, prevents its degradation through the 26S proteasome |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
DPP3
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