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Interleukin-36 Receptor Antagonist (IL-36Ra) is a member of the interleukin-36 family of cytokines, which also includes three agonists: interleukin-36 alpha, interleukin-36 beta, and interleukin-36 gamma. These cytokines are part of the larger interleukin-1 superfamily . The primary function of IL-36Ra is to inhibit the pro-inflammatory effects of the interleukin-36 cytokines by competing with their receptor, interleukin-36 receptor (IL-36R), thereby preventing the recruitment of the accessory protein interleukin-1 receptor accessory protein (IL-1RAcP) .
IL-36Ra is a protein coding gene known as IL36RN. It is expressed in various tissues, including the skin, lungs, intestines, joints, and brain . The receptor activation follows a two-step mechanism: the agonist first binds to IL-36R, forming a binary complex that recruits IL-1RAcP. This assembled ternary complex brings together intracellular Toll/Interleukin-1 receptor (TIR) domains of receptors, which activate downstream nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) and mitogen-activated protein kinase (MAPK) signaling .
Mutations in the IL36RN gene can lead to a decrease or production of defective IL-36Ra protein, which has been associated with several inflammatory skin diseases, including generalized pustular psoriasis, acrodermatitis continua suppurativa Hallopeau, and acute generalized exanthematous pustulosis . Dysregulation of IL-36Ra can stimulate keratinocyte and immune cells, enhancing the T-helper 17/T-helper 23 axis and inducing psoriatic-like skin disorders .
Recombinant IL-36Ra, particularly the human recombinant form with a His tag, is produced using recombinant DNA technology. The His tag is a sequence of histidine residues added to the protein to facilitate purification through affinity chromatography. This recombinant form is used in research to study the protein’s function, signaling pathways, and potential therapeutic applications.