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Literature summary for 3.4.22.52 extracted from
- Suppression of cancer cell migration and invasion by protein phosphatase 2A through dephosphorylation of micro- and m-calpains (2006), J. Biol. Chem., 281, 35567-35575.
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | protein phosphatase 2A functions as a physiological calpain phosphatase to directly dephosphorylate mu-calpain, which leads to decreased calpain activity and suppression of migration and invasion of human lung cancer cells. Therapeutic activation of protein phosphatase 2A to dephosphorylate calpain by enhancing ceramide production may have clinical relevance for the treatment of cancer metastasis | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | protein phosphatase 2A functions as a physiological calpain phosphatase to directly dephosphorylate mu-calpain, which leads to decreased calpain activity and suppression of migration and invasion of human lung cancer cells | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| A-549 cell | protein phosphatase 2A functions as a physiological calpain phosphatase to directly dephosphorylate mu-calpain, which leads to decreased calpain activity and suppression of migration and invasion of human lung cancer cells | Homo sapiens | - |
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