{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nThe prostaglandin D₂ receptor 2 (PTGDR2), more commonly known as CRTH2, plays a central role in type 2 immunity. It is preferentially expressed on T helper type 2 cells, innate lymphoid cells, eosinophils, and basophils, where its activation by prostaglandin D₂ triggers the release of key type 2 cytokines (IL‐4, IL‐5, IL‐13) and orchestrates allergic inflammation and tissue remodelling in conditions such as asthma, atopic dermatitis, and chronic rhinosinusitis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFunctional studies have demonstrated that PTGDR2 signaling mediates chemotaxis and activation of these immune cells while also promoting cell survival by dampening apoptosis. Diverse endogenous ligands and metabolites—not only prostaglandin D₂ but also derivatives such as PGH₂‐related compounds and 11‑dehydro‐TXB₂—act as potent agonists at CRTH2, and selective antagonists (including some nonsteroidal drugs) have been shown to modulate its activity, underscoring its therapeutic potential."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nGenetic investigations have implicated PTGDR2 in the susceptibility and clinical severity of allergic disorders. Single nucleotide polymorphisms in the gene’s 3′‑untranslated region have been associated with altered mRNA stability and receptor expression, correlating with variations in type 2 cytokine production and markers of bronchial hyperresponsiveness in asthma and other allergic conditions. In addition, modulation of its expression by transcription factors such as GATA3 and NFAT further highlights its critical regulatory role."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDetailed structural and mechanistic studies have provided new insights into PTGDR2 function. Analyses of its ligand‐binding pocket—revealing distinct “polar in” versus “polar out” binding modes—and investigations into receptor trafficking have highlighted the contribution of the C‑terminal tail in internalization and recycling. These findings demonstrate how specific charged residues and local microenvironments determine ligand selectivity and govern downstream G protein signalling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its classical role in mediating allergic inflammation, PTGDR2 is increasingly recognized for its involvement in diverse pathophysiological processes. It has been implicated in pulmonary arterial hypertension through modulation of Th2 responses, in the antiviral response during respiratory syncytial virus bronchiolitis, and even in bone remodelling via induction of osteoclast apoptosis. Furthermore, CRTH2 has emerged as a potential surface marker in pancreatic beta‐cells and may participate in the progression of certain malignancies and IgG4‐related diseases, thereby broadening its impact on immune and tissue homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "26", "end_ref": "36"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Masahiro Iwasaki, Kinya Nagata, Shoichi Takano, et al. 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