The DOI matches its Crossref record; 75 of the 75 references it cites were found in a registry or an index.
Interleukin‐1β, Interleukin‐18, and the Interleukin‐1β Converting Enzymea
Abstract
ABSTRACT: When injected intravenously into humans and animals, interleukin‐1β (IL‐1β) is perhaps the most potent of the endogenous pyrogens. However, IL‐1β is initially synthesized as a relatively inactive precursor molecule (proIL‐1β) which lacks a signal peptide and hence remains inside the cell. To be active as a fever‐producing molecule, proIL‐1β must first be processed to an active mature molecule and secreted. Although several enzymes associated with inflammatory tissues are capable of processing proIL‐1β into an active molecule in the extracellular compartment, the IL‐1β converting enzyme (ICE, also called caspase‐1) cuts intracellular proIL‐1β after the aspartic acid residue in position 116, resulting in a highly active mature IL‐1β that is secreted into the extracellular space. IL‐18 is also initially synthesized as an inactive precursor molecule (proIL‐18) lacking a signal peptide. IL‐18 is a member of the IL‐1 family, and like IL‐1β, proIL‐18 is cleaved by ICE to yield an active molecule. However, unlike IL‐1β, IL‐18 is not an endogenous pyrogen following intraperitoneal injection into mice. Nevertheless, IL‐18 may contribute to inflammation and fever because IL‐18 is a potent inducer of tumor necrosis factor, chemokines, and interferon‐γ production.
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1 retracted
Preliminary report: effects of interleukin-1 on platelet counts
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RetractedCloning of a new cytokine that induces IFN-γ production by T cells
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A novel heterodimeric cysteine protease is required for interleukin-1βprocessing in monocytes
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Human ICE/CED-3 Protease Nomenclature
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Altered Cytokine Export and Apoptosis in Mice Deficient in Interleukin-1β Converting Enzyme
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Activation of Interferon-γ Inducing Factor Mediated by Interleukin-1β Converting Enzyme
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Structure and mechanism of interleukin-lβ converting enzyme
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Cited by
Martinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066
Allergic Rhinitis and Its Impact on Asthma
Bousquet, J., van Cauwenberge, P., & Khaltaev, N. (2001) · Journal of Allergy and Clinical Immunology · doi:10.1067/mai.2001.118891 · Cited by 3,588
Hornung, V., Bauernfeind, F., Halle, A., Samstad, E. O., Kono, H., Rock, K. L., Fitzgerald, K. A., & Latz, E. (2008) · Nature Immunology · doi:10.1038/ni.1631 · Cited by 3,065
Ghiringhelli, F., Apetoh, L., Tesniere, A., Aymeric, L., Ma, Y., Ortiz, C., Vermaelen, K., Panaretakis, T., Mignot, G., Ullrich, E., et al. (2009) · Nature Medicine · doi:10.1038/nm.2028 · Cited by 1,898
Agostini, L., Martinon, F., Burns, K., McDermott, M. F., Hawkins, P. N., & Tschopp, J. (2004) · Immunity · doi:10.1016/s1074-7613(04)00046-9 · Cited by 1,768
Metadata
- Authors
- DINARELLO, C. A.
- Venue
- Annals of the New York Academy of Sciences
- Publisher
- Wiley
- Published
- 1998-09
- Volume
- 856
- Issue
- 1
- Pages
- 1-11
- ISSN
- 0077-8923 (ISSN-L)
- 1749-6632
- OpenAlex
- W1921587687
- Cited by
- 498
- References
- 75
- FWCI
- 5.18
- Type
- journal article
- Language
- en
- Open access
- closed
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- DINARELLO, C. A. (1998). Interleukin‐1β, Interleukin‐18, and the Interleukin‐1β Converting Enzymea. Annals of the New York Academy of Sciences. https://doi.org/10.1111/j.1749-6632.1998.tb08307.x
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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