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Interleukin-13 (IL-13) is a pleiotropic cytokine that plays a pivotal role in the pathogenesis of Type 2 inflammation-mediated diseases, such as asthma and atopic dermatitis (Source: PubMed, PMID: 11069144). The R130Q variant (rs1800925) is a well-characterized single nucleotide polymorphism (SNP) where an arginine residue is substituted with glutamine at position 130, which corresponds to position 110 in the mature protein (Source: UniProt, P35225). This variation is functionally significant as it decreases the binding affinity of IL-13 for its decoy receptor, IL-13 receptor alpha 2 (IL-13Ra2), thereby increasing the bioavailability of the cytokine to bind its signaling receptor complex, IL-4Ra/IL-13Ra1 (Source: PubMed, PMID: 11859124). This enhanced signaling leads to increased IgE production, mucus hypersecretion, and airway hyperresponsiveness (Source: PubMed, PMID: 10677320). Therapeutic interventions targeting IL-13, such as the monoclonal antibodies lebrikizumab and tralokinumab, are designed to neutralize the cytokine and mitigate these inflammatory effects (Source: NIH, ClinicalTrials.gov). Understanding the R130Q variant is crucial for precision medicine, as it may influence disease severity and the efficacy of IL-13-targeted therapies.
Monoclonal antibodies bind to the IL-13 cytokine, preventing its interaction with the IL-13 receptor alpha 1 (IL-13Ra1) and IL-13 receptor alpha 2 (IL-13Ra2) subunits, thereby inhibiting downstream JAK/STAT signaling pathways.
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