{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nOLFM4, an olfactomedin‐related glycoprotein, is widely recognized for its roles in normal tissue function and homeostasis. Initially identified as a gene highly induced in myeloid stem cells and later shown to colocalize with specific granule proteins in neutrophils, OLFM4 is expressed in only a discrete subset of these cells—reflecting a sophisticated post‐transcriptional regulation. In addition, as a secreted extracellular matrix protein that binds cell‐surface lectins and cadherins, OLFM4 promotes cell adhesion and has emerged as a robust marker of intestinal stem cells."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nOLFM4 has been extensively implicated in cancer biology, where its expression and function appear to be highly context dependent. In gastrointestinal malignancies such as colorectal and gastric cancers, OLFM4 is markedly upregulated in early-stage lesions—serving as a potential diagnostic marker—but often declines during tumor progression. Functional studies indicate that OLFM4 can negatively regulate oncogenic pathways (including Wnt/β‑catenin, NF‑κB, and hedgehog signaling) and modulate cellular processes such as proliferation, apoptosis, and migration. In prostate, endometrial, ovarian, cervical, lung, and pancreatic cancers, genetic alterations and/or epigenetic silencing of OLFM4 correlate with enhanced invasiveness and metastasis; microRNAs (for example, miR‑103 and miR‑486‑5p) have also been shown to regulate its expression. Moreover, its secreted nature has spurred investigation into its utility as a circulating biomarker for early detection and prognostication across diverse tumor types."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "34"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the context of innate immunity and inflammatory disorders, OLFM4 modulates neutrophil function by interacting with cathepsin C and thereby inhibiting downstream serine protease activity—a regulatory mechanism that compromises bacterial killing. 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