Interleukin-13 receptor subunit alpha-2 (IL-13RA2) (IL-13RA2)

Interleukin-13 receptor subunit alpha-2 (IL-13RA2) is a high-affinity cell-surface protein that binds the cytokine interleukin-13 (IL-13). Historically characterized as a decoy receptor because it lacks the cytoplasmic signaling motifs found in IL-13RA1, it primarily functions to sequester IL-13 and limit its bioavailability for the signaling-competent IL-13RA1/IL-4RA complex (UniProt Q14627; PubMed: 10449777). Beyond its decoy role, IL-13RA2 is implicated in promoting tumor cell invasion and metastasis through alternative signaling pathways, such as the activation of AP-1 (PubMed: 16143774). The receptor is highly overexpressed in various cancers, particularly glioblastoma multiforme (GBM), while showing minimal expression in healthy tissues, making it a prime candidate for targeted immunotherapy (PubMed: 28024237). Current therapeutic approaches include the development of chimeric antigen receptor (CAR) T-cells, such as MB-101, and immunotoxins like Cintredekin besudotox, which exploit the receptor's high affinity for IL-13 to selectively destroy malignant cells (ClinicalTrials.gov NCT02208362; PubMed: 17606715). This target's role in fibrosis and its potential as a biomarker for disease progression further underscore its clinical significance (PubMed: 25132446).

Other names

IL13RA2CD213A2Interleukin-13 receptor alpha-2IL-13R-alpha-2Cancer/testis antigen 19CT19

Chimeric antigen receptor (CAR) T-cell mediated lysis, immunotoxin-induced protein synthesis inhibition, and competitive ligand sequestration to inhibit signaling.