{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nS100A4 is a multifunctional, calcium‐binding protein that plays a central role in promoting cancer progression. Numerous studies have shown that S100A4 is overexpressed in a broad spectrum of malignancies—including pancreatic and colon carcinomas, medulloblastoma, prostate and thyroid cancers, lung and ovarian tumors, as well as hepatocellular and cholangiocarcinomas—and its elevated expression is frequently associated with poor differentiation, increased invasiveness and metastasis, and an overall adverse clinical outcome. In these settings, S100A4 regulates key aspects of tumor cell behavior, for example by controlling the expression and activity of matrix metalloproteinases and by modulating tumor cell–extracellular matrix interactions to enhance cell motility and dissemination."}, {"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": "\nIn addition to its intracellular actions, secreted S100A4 exerts profound paracrine effects within the tumor microenvironment. Extracellular S100A4 binds to receptors and partners such as annexin II and the receptor for advanced glycation end products (RAGE) to activate proteolytic cascades and induce inflammatory cytokine expression. In some tumors, signals mediated by integrin‐dependent pathways and NF‐κB activation further amplify S100A4 expression in stromal cells—including cancer‐associated fibroblasts and mesenchymal stem cells—thereby reinforcing a microenvironment that favors invasion and metastasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nS100A4 also modulates cytoskeletal organization and cellular motility through direct interactions with components of the contractile machinery. It localizes prominently to lamellipodia and binds to myosin‐IIA to regulate filament assembly and actin dynamics. Structural studies have revealed that Ca²⁺ binding induces large conformational changes in S100A4 that expose a hydrophobic cleft, permitting high‐affinity interactions with target sequences in proteins such as nonmuscle myosin. These biochemical and biophysical properties underlie its ability to influence cell shape and migration."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "21"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond effects on motility and invasion, S100A4 influences the epithelial–mesenchymal transition (EMT) and the maintenance of cancer stem cell properties. Intracellularly, S100A4 can directly bind to the tetramerization domain of p53, thereby modifying its oligomerization and functional activity in cell‐cycle control and apoptosis. Furthermore, S100A4 signaling has been linked to the activation of pathways (including Notch and PI3K/AKT) that sustain tumor‐initiating populations and promote EMT. Regulatory microRNAs that target S100A4 further modulate these processes, underscoring its complex role in connecting cell fate, differentiation, and metastatic potential."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "22"}, {"type": "fg_f", "ref": "8"}, {"type": "fg_f", "ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nApart from its oncogenic roles, S100A4 has been implicated in various non‐malignant pathologies. In the kidney, for example, S100A4 (often referred to as fibroblast‐specific protein 1) participates in processes linked to epithelial–mesenchymal transition that contribute to podocyte loss in diabetic nephropathy. In the nervous system, S100A4 released from stressed astrocytes exerts neuroprotective effects via activation of the Janus kinase/STAT pathway. Moreover, S100A4 is emerging as a mediator of inflammatory responses in conditions such as rheumatoid arthritis and pulmonary fibrosis, where its secretion by activated macrophages triggers cascades, including sphingosine‐1‐phosphate–dependent fibroblast activation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "26", "end_ref": "29"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Christophe Rosty, Takashi Ueki, Pedram Argani, et al. 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