{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPLAC8 is emerging as a multifaceted regulator in cancer biology, where its expression and function are highly context‐dependent. In several epithelial malignancies—including colon, pancreatic exocrine, lung, breast, prostate, and cervical cancers—enhanced PLAC8 expression has been linked to aggressive phenotypes. For instance, in colon cancer, PLAC8 localizes to the apical domain of intestinal epithelium and promotes epithelial‐to‐mesenchymal transition (EMT) by reconfiguring cadherin profiles, upregulating markers such as vimentin and ZEB1, and activating ERK2 through inhibition of its phosphatase DUSP6. Similarly, in prostate cancer bone metastasis, increased PLAC8 stimulates tumor growth and invasion, while in lung and cervical cancers, PLAC8 overexpression couples with deregulated signaling (including via KLF4 repression and SOX4-mediated AKT activation) and with the activation of the Wnt/β‐catenin pathway to promote cell proliferation and EMT. In breast cancer, abnormal PLAC8 signaling is also associated with chemoresistance and enhanced migration."}, {"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": "\nIn addition to its roles in regulating cellular adhesion and motility, PLAC8 is a central mediator of autophagic processes, which in turn influence tumor cell survival and therapeutic responses. In pancreatic ductal adenocarcinoma, for example, PLAC8 facilitates lysosome–autophagosome fusion, thereby linking oncogenic mutations to metabolic reprogramming and sustained autophagy. In nasopharyngeal carcinoma, loss of PLAC8 activates autophagy via suppression of the AKT/mTOR pathway, which is associated with reduced proliferation and enhanced apoptosis. Furthermore, in breast cancer, PLAC8 contributes to chemoresistance against agents such as adriamycin by inhibiting autophagic flux through mechanisms involving p62 accumulation. Similar autophagy‐promoting roles of PLAC8 have also been documented in trophoblast cells, where increased PLAC8 enhances invasion and migration under hypoxic conditions, and in inflammatory settings such as Adult Still Disease, where it appears to limit the production of pro‐inflammatory cytokines through augmented autophagy."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its oncogenic and autophagy‐related functions, PLAC8 plays diverse roles in developmental and other pathological contexts. In normal physiology, PLAC8 is expressed in oocytes, trophoblast cells, and embryos where it is implicated in processes such as cellular differentiation and implantation. In hematologic malignancies, for instance, a downregulation of PLAC8 is necessary for promyelocytic cells to undergo terminal differentiation, whereas forward genetics screens have revealed that, depending on the cellular context, PLAC8 can either inhibit or promote apoptosis. Its altered expression has also been observed in hepatocellular carcinoma and clear cell renal cell carcinoma, and increased PLAC8 levels have been linked with altered endothelial progenitor cell function in neonates exposed to gestational diabetes. Additional studies have associated elevated PLAC8 with the promotion of stemness characteristics and radiotherapy resistance in lung adenocarcinoma, with osteosarcoma metastasis linked to mutant p53, and with pancreatic neuroendocrine tumor development. Notably, PLAC8 has recently emerged as a critical host factor that facilitates SARS‑CoV‑2 entry and, in gallbladder carcinoma, as a mediator of chemoresistance via PD‑L1 upregulation. Even in non‑cancerous states such as interstitial cystitis, PLAC8 is being explored as a potential biomarker."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Hisanori Uehara, Tetsuyuki Takahashi, Keisuke Izumi "}, {"type": "b", "children": [{"type": "t", "text": "Induction of retinol-binding protein 4 and placenta-specific 8 expression in human prostate cancer cells remaining in bone following osteolytic tumor growth inhibition by osteoprotegerin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Int J Oncol (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3892/ijo.2013.1954"}], "href": "https://doi.org/10.3892/ijo.2013.1954"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23708710"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23708710"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Cunxi Li, Haiting Ma, Yang Wang, et al. 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