{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRNASE3, also known as eosinophil cationic protein (ECP), is a highly cationic member of the RNase A superfamily secreted primarily by activated eosinophils (and, under certain conditions, by neutrophils). It exerts potent antimicrobial and cytotoxic functions by binding directly to microbial surface components—such as lipopolysaccharides, lipid A, and peptidoglycans—and by integrating into and destabilizing lipid bilayers. Detailed structure–function studies have mapped its key membrane‐active regions, including an N‐terminal domain that contributes to membrane aggregation and disruption. Moreover, RNASE3 interacts with cell surface glycosaminoglycans, permitting its endocytic uptake, which further promotes its cytotoxic effects on target cells."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRNASE3 also plays a critical immunomodulatory role in the inflammatory milieu. Its levels in biological fluids serve as sensitive biomarkers of eosinophil activation in a wide spectrum of conditions including asthma, allergic rhinitis, coronary artery disease, and even parasitic infections. In addition, several studies have linked RNASE3 gene polymorphisms and post‐translational heterogeneity to alterations in its cytotoxic and immunoregulatory functions, thereby influencing disease susceptibility and progression. For example, RNASE3 can promote fibroblast activation and collagen gel contraction via stimulation of TGF‑β release, a mechanism that may contribute to airway remodeling and tissue fibrosis. Furthermore, its local production by cells such as neutrophils—via IgE‐dependent mechanisms—further expands its role as both an effector molecule and a clinical marker in allergic and inflammatory pathologies."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRecent structure–function analyses have further revealed that intrinsic genetic variation and post‐translational modifications contribute to RNASE3’s molecular heterogeneity and, by extension, its functional versatility. Comparative studies using native protein variants have demonstrated that single amino acid substitutions (for example, an arginine-to-threonine shift) can markedly impair the protein’s cytotoxic potential while sparing its ribonuclease activity. In experimental models, administration of RNASE3 has been shown to trigger significant tissue responses—including localized lesions following intradermal injection—underscoring its dual capacity as an effector molecule in host defense and a mediator of tissue injury. Such insights continue to inform the development of novel therapeutic agents based on RNASE3-derived peptides."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "33", "end_ref": "36"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Esther Carreras, Ester Boix, Susanna Navarro, et al. 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