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Interleukin‐1β, Interleukin‐18, and the Interleukin‐1β Converting Enzymea

Interleukin‐1β, Interleukin‐18, and the Interleukin‐1β Converting Enzymea 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annals of the New York Academy of Sciences Wiley

Interleukin‐1β, Interleukin‐18, and the Interleukin‐1β Converting Enzymea

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References (91)

Publisher
Wiley
Copyright
Copyright © 1998 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0077-8923
eISSN
1749-6632
DOI
10.1111/j.1749-6632.1998.tb08307.x
Publisher site
See Article on Publisher Site

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.

Journal

Annals of the New York Academy of Sciences – Wiley

Published: Sep 1, 1998

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