| + |
CAPN1 | up-regulates activity 
cleavage
|
F2R |
0.383 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263559 |
Lys32 |
RARRPESkATNATLD |
in vitro |
|
| pmid |
sentence |
| 10978167 |
PAR1E and PAR2E (10 microM) were incubated in the presence of the different proteases | The enzymes were used at the following concentrations: 0.5 unit/mL thrombin, 2.5 nM trypsin, 20 nM plasmin, 20 nM cathepsin G, 20 nM elastase, 20 nM proteinase 3, and 2 units/mL calpain I and II|Protease-activated receptors (PARs) mediate cell activation after proteolytic cleavage of their extracellular amino terminus.|Protease-activated receptors (PARs) mediate cell activation after proteolytic cleavage of their extracellular amino terminus.|Protease-activated receptors (PARs) mediate cell activation after proteolytic cleavage of their extracellular amino terminus |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CAPN1 | down-regulates activity 
cleavage
|
F2R |
0.383 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263560 |
Lys76 |
YRLVSINkSSPLQKQ |
in vitro |
|
| pmid |
sentence |
| 10978167 |
PAR1E and PAR2E (10 microM) were incubated in the presence of the different proteases | The enzymes were used at the following concentrations: 0.5 unit/mL thrombin, 2.5 nM trypsin, 20 nM plasmin, 20 nM cathepsin G, 20 nM elastase, 20 nM proteinase 3, and 2 units/mL calpain I and II|Protease-activated receptors (PARs) mediate cell activation after proteolytic cleavage of their extracellular amino terminus.|Protease-activated receptors (PARs) mediate cell activation after proteolytic cleavage of their extracellular amino terminus.|Plasmin, calpain and leukocyte elastase, cathepsin G, and proteinase 3 cleaved at multiple sites and would be expected to disable PAR1 by cleaving COOH-terminal to the activation site. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CAPN1 | down-regulates activity
cleavage
|
F2RL1 |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263580 |
Phe59 |
GVTVETVfSVDEFSA |
in vitro |
|
| pmid |
sentence |
| 10978167 |
PAR1E and PAR2E (10 microM) were incubated in the presence of the different proteases | The enzymes were used at the following concentrations: 0.5 unit/mL thrombin, 2.5 nM trypsin, 20 nM plasmin, 20 nM cathepsin G, 20 nM elastase, 20 nM proteinase 3, and 2 units/mL calpain I and II|Protease-activated receptors (PARs) mediate cell activation after proteolytic cleavage of their extracellular amino terminus.|Mass spectrometry studies of PAR2E predicted activation of PAR2 by trypsin through cleavage at the Arg36-Ser37 site, no effect of thrombin, and inactivation of the receptor by plasmin, calpain and leukocyte elastase, cathepsin G, and proteinase 3 |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CAPN1 | down-regulates activity
cleavage
|
MAPT |
0.341 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251584 |
|
|
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 25969760 |
Besides tau phosphorylation, calpain activation might play a role in tau-mediated neurodegeneration by inducing tau cleavage. In vitro studies have shown that both fetal and adult tau isoforms are rapidly proteolyzed by calpains |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
| + |
CAPN1 | up-regulates activity
cleavage
|
CDK5/CDK5R1 |
0.559 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251581 |
|
|
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 25969760 |
Calpains also modulate the activity of CDK5. Physiologically, CDK 5 is activated by p35 and its cleaved product p25. The latter has a longer half life than p35 and therefore it is a more potent activator of CDK5. The cleavage of p35 to p25 is mediated by calpain |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
| + |
CAST | down-regulates activity
binding
|
CAPN1 |
0.913 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251582 |
|
|
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 25969760 |
In addition to Ca2+, calpastatin has a key role in the regulation of calpain. Calpastatin, a heat-stable protein ranging from ~70 to ~140 kDa of apparent molecular weight depending on the cell type, is considered a specific endogenous inhibitor of calpains|The calpastatin molecule contains four inhibitory units [75–77]. Each of these units binds to one calpain molecule [75–77]. Therefore, the ratio calpain/calpastatin plays a key role in the regulation of calpain activity [78–80]. The inhibitory effect of calpastatin requires Ca2+-dependent high-affinity binding to three sites of calpain |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
| + |
CAPN1 | up-regulates activity
cleavage
|
CDK5R1 |
0.552 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251583 |
|
|
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 25969760 |
Calpains also modulate the activity of CDK5. Physiologically, CDK 5 is activated by p35 and its cleaved product p25. The latter has a longer half life than p35 and therefore it is a more potent activator of CDK5. The cleavage of p35 to p25 is mediated by calpain |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
| + |
CAPN1 | up-regulates activity
cleavage
|
GSK3B |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251586 |
|
|
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 25969760 |
Thus, it has been shown that calpain cleaves the inhibitory domain of GSK3 generating two fragments of 40 and 30 kDa. This cleavage enhanced activity of the kinase |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
| + |
calcium(2+) | up-regulates activity
chemical activation
|
CAPN1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251580 |
|
|
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 25969760 |
The data obtained from those studies suggest that the mechanisms leading to the formation of the hallmark lesions of AD might be linked. One of such mechanisms seems to be the dysregulation of calcium homeostasis that results in the abnormal activation of calpains. Calpains are a family of Ca2+-dependent cysteine proteases that play a key role in multiple cell functions including cell development, differentiation and proliferation, axonal guidance, growth cone motility, and cell death, among others. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAPN1 | up-regulates activity
cleavage
|
GSK3A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251585 |
|
|
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 25969760 |
Thus, it has been shown that calpain cleaves the inhibitory domain of GSK3 generating two fragments of 40 and 30 kDa. This cleavage enhanced activity of the kinase |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
3.0
CAPN1
- 
- 