Application | Comment | Organism |
---|---|---|
pharmacology | in a mouse model of sepsis induced by cecal ligation puncture that results in elevated levels of serum interleukin 1beta, meprin inhibitor actinonin significantly reduces levels of serum interleukin 1beta | Mus musculus |
Cloned (Comment) | Organism |
---|---|
meprin alpha subunit | Mus musculus |
meprin alpha subunit | Rattus norvegicus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
actinonin | in a mouse model of sepsis induced by cecal ligation puncture that results in elevated levels of serum interleukin 1beta, meprin inhibitor actinonin significantly reduces levels of serum interleukin 1beta | Mus musculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
- |
- |
Rattus norvegicus | Q64230 | - |
- |
Purification (Comment) | Organism |
---|---|
purification of oligomeric meprin A from kidney cortex | Mus musculus |
purification of oligomeric meprin A from kidney cortex | Rattus norvegicus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
kidney | kidney cortex | Rattus norvegicus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pro-interleukin 1beta + H2O | cleavage at the H115-D116 bond, which is one amino acid N-terminal to the caspase-1 cleavage site and five amino acids C-terminal to the meprin beta site. Both oligomeric meprin A and recombinant meprin alpha are capable of cleaving | Rattus norvegicus | interleukin 1beta + H2O | the biological activity of the pro-interleukin-1beta cleaved product produced by meprin A, is 3fold higher to that of the interleukin-1beta product produced by meprin b or caspase-1 | ? |