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Beschreibung

Interleukin-1 alpha (UniProt: P01583, also known as IL-1 alpha, Hematopoietin-1) is encoded by the IL1A (also known as IL1F1) gene (Gene ID: 3552) in human. IL-1a is constitutively expressed in several healthy tissues in a steady state and its expression can be increased in response to a number of stimuli. Absolute amounts of IL-1a vary among cell types, but barrier cells, such as endothelial and epithelial cells, express higher amounts at steady state. IL-1a is synthesized with a propeptide (aa 1-112) and is post-translationally modified by phosphorylation at serine 90, myristoylation on lysine 82, and acetylation on lysine 82. After synthesis, pro-IL-1a is localized into the nucleus, cytosol or lysosomal compartment or is displayed on the outer leaflet of the plasma membrane. Its intracellular localization can change in response to specific stimuli. Pro-IL-1a can also be cleaved by calpain to generate IL-1 -N-terminal domain (NTP) and a mature C-terminal IL-1a form. The C-terminal domain is catalytically active and is capable of signaling via IL-1R. Both IL-1a -NTP and pro-IL-1a contains a functional NLS signal and bind HAX1 to allow translocation into the nucleus. In the nucleus, IL-1a -NTP binds transcription regulation factors and activates expression of proinflammatory cytokines and chemokines independently of IL-1R1 signaling. The biological functions of IL-1a also involve stimulation of thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. (Ref.: Malik, A., and Kanneganti, TD. (2018). Immunol. Rev. 281(1), 124-137, Di Paolo, NC., and Shayakhmetov, DM (2016). Nat. Commun. 17(8), 906-913).