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The interleukin-1 superfamily has 11 members, which have similar gene structure, although originally it contained only four members IL-1α, IL-1β, IL-1Ra and IL-18. After discovery of another 5 members the updated nomenclature was generally accepted which included all members of IL-1 cytokine family. The old IL-1 members were renamed to IL-1F1 ...
Interleukin-1 beta (IL-1β) also known as leukocytic pyrogen, leukocytic endogenous mediator, mononuclear cell factor, lymphocyte activating factor and other names, is a cytokine protein that in humans is encoded by the IL1B gene.
Interleukin 8 is a chemokine produced by macrophages and other cell types such as epithelial cells, airway smooth muscle cells [25] and endothelial cells. Endothelial cells store IL-8 in their storage vesicles, the Weibel-Palade bodies .
Interleukin-1 alpha (IL-1 alpha) also known as hematopoietin 1 is a cytokine of the interleukin 1 family that in humans is encoded by the IL1A gene. [5] [6] In general, Interleukin 1 is responsible for the production of inflammation, as well as the promotion of fever and sepsis. IL-1α inhibitors are being developed to interrupt those processes ...
Interleukin-1 receptor (IL-1R) is a cytokine receptor which binds interleukin 1. [1] Two forms of the receptor exist. The type I receptor is primarily responsible for transmitting the inflammatory effects of interleukin-1 (IL-1) while type II receptors may act as a suppressor of IL-1 activity by competing for IL-1 binding. [1]
Members of the very wide interleukin-1 receptor (IL-1R) family are characterized by extracellular immunoglobulin-like domains and intracellular Toll/Interleukin-1R (TIR) domain. It is a group of structurally homologous proteins, conserved throughout the species as it was identified from plants to mammals.
Interleukin 1 is a cytokine that acts locally and systemically in the innate immune system. IL-1a and IL-1ß are known for causing inflammation, but can also cause induction of other proinflammatory cytokines, and fever.
Caspase-1 Zymogen. Caspase-1/Interleukin-1 converting enzyme (ICE) is an evolutionarily conserved enzyme that proteolytically cleaves other proteins, such as the precursors of the inflammatory cytokines interleukin 1β and interleukin 18 as well as the pyroptosis inducer Gasdermin D, into active mature peptides.