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Literature summary for 3.4.24.18 extracted from

  • Herzog, C.; Haun, R.S.; Kaushal, V.; Mayeux, P.R.; Shah, S.V.; Kaushal, G.P.
    Meprin A and meprin alpha generate biologically functional IL-1beta from pro-IL-1beta (2009), Biochem. Biophys. Res. Commun., 379, 904-908.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.18

Application

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(Commentary)

Cloned (Comment) Organism
meprin alpha subunit Mus musculus
meprin alpha subunit Rattus norvegicus

Inhibitors

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

Organism UniProt Comment Textmining
Mus musculus
-
-
-
Rattus norvegicus Q64230
-
-

Purification (Commentary)

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

Source Tissue Comment Organism Textmining
kidney kidney cortex Rattus norvegicus
-

Substrates and Products (Substrate)

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 ?