{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nE‐selectin, the protein product of SELE, is a pivotal endothelial adhesion molecule that orchestrates the early phases of the inflammatory response. Induced by proinflammatory cytokines such as tumor necrosis factor‐α, E‐selectin promotes leukocyte tethering and rolling by interacting with a broad repertoire of glycosylated ligands—including PSGL‐1, CD44, L‐selectin and HCELL—thereby triggering intracellular signaling cascades (via NF‐κB, p38 MAPK, Src, and phospholipase Cγ) that culminate in the activation of β₂‐integrins for stable adhesion and subsequent diapedesis. The receptor’s localization within cholesterol‐rich lipid rafts further facilitates its unique catch‐bond behavior under shear stress, ensuring efficient leukocyte recruitment."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAberrant regulation of E‐selectin is closely linked to a spectrum of vascular and metabolic disorders. In pathological conditions such as Fabry disease, oscillating hyperglycemia, and exposure to uremic toxins, enhanced oxidative stress drives up‐regulation of E‐selectin, which contributes to endothelial dysfunction. In parallel, genetic variations within the SELE locus have been associated with an array of cardiovascular risk factors—including atherosclerosis, myocardial infarction and elements of the metabolic syndrome—while elevated circulating (soluble) E‐selectin levels serve as valuable biomarkers of type 2 diabetes and vascular inflammation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "23"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its classical role in inflammation, E‐selectin significantly contributes to cancer metastasis. Tumor cells co‐opt E‐selectin interactions by employing alternative glycoprotein ligands—such as carcinoembryonic antigen (CEA), MUC16, podocalyxin‐like protein, and HCELL—to secure rolling adhesion along the endothelium, thereby facilitating extravasation into distant tissues. Moreover, certain malignancies, including squamous cell carcinomas, exhibit down‐regulation of endothelial E‐selectin to impair immune cell recruitment and foster an immunosuppressive tumor milieu."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "24", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nTherapeutic strategies targeting E‐selectin offer considerable promise in mitigating pathological leukocyte adhesion and aberrant angiogenesis. Glycomimetic inhibitors (such as rivipansel) effectively disrupt E‐selectin catch‐bond formation and impede downstream integrin activation, thereby attenuating leukocyte recruitment during inflammatory episodes. In addition, modalities including low‐dose radiotherapy and unfractionated heparin have been demonstrated to down‐regulate E‐selectin expression on activated endothelium, providing potential interventions against sepsis, tumor dissemination, and other disorders of endothelial activation. Furthermore, constitutive, basal expression of E‐selectin in noninflamed tissues contributes to immunosurveillance by enabling T‐cell recruitment for tissue homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "32", "end_ref": "42"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Alexander Zarbock, Klaus Ley, Rodger P McEver, et al. 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