Activation of interleukin-1 beta by a co-induced protease.
The proteolytic generation of mature interleukin-1 beta (IL-1 beta) from its inactive precursor does not proceed by a conventional pathway for hormonal processing. Pro-IL-1 beta is found dispersed in the cytoplasm, and there are no basic amino acid residues or other commonly recognized processing sites adjoining the mature N-terminus. Processing appears to occur during release of the hormone. In the present study, we have identified a specific protease that generates mature IL-1 beta from the precursor. This enzyme is co-induced with the hormone, and it differs in its cleavage specificity and inhibitor sensitivity from all known proteases.
Black
R A
RA
Department of Protein Chemistry, Immunex Corporation, Seattle, WA 98101.
Kronheim
S R
SR
Sleath
P R
PR
D015153:Blotting, Western; D002460:Cell Line; D003593:Cytoplasm / Q000378:metabolism; D005033:Ethylmaleimide / Q000494:pharmacology; D007375:Interleukin-1 / Q000502:physiology*; D007461:Iodoacetates / Q000494:pharmacology; D019807:Iodoacetic Acid; D009000:Monocytes / Q000201:enzymology; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology; D011498:Protein Precursors / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D013379:Substrate Specificity
D007375:Interleukin-1; D007461:Iodoacetates; D011480:Protease Inhibitors; D011498:Protein Precursors; D011994:Recombinant Proteins; D010447:Peptide Hydrolases; D005033:Ethylmaleimide; D019807:Iodoacetic Acid