{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPDGF‐D has emerged as an important oncogenic mediator that drives tumor progression via multiple mechanisms. In various solid tumors—including prostate, hepatocellular, cholangiocarcinoma, colorectal, endometrial, tongue squamous cell carcinoma, ovarian cancer, and even certain mesenchymal tumors such as dermatofibrosarcoma and meningioma/schwannoma—PDGF‐D overexpression induces epithelial–mesenchymal transition (EMT), enhances cell migration and invasion, and promotes overall tumor growth and chemoresistance. These effects are mediated by its proteolytic activation and subsequent binding to the β‐PDGF receptor, which in turn triggers downstream pathways (for example, JNK, AKT, ERK, and mTOR) and modulates the tumor stroma by recruiting fibroblasts and other supportive cells."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its oncogenic properties, PDGF‐D plays a central role in tissue remodeling, vascular homeostasis, and development. In transgenic animal models, PDGF‐D enhances wound healing by increasing macrophage infiltration and interstitial fluid pressure, promotes vascular maturation through pericyte/smooth muscle cell modulation, and contributes to renal fibrogenesis as evidenced in models of tubulointerstitial fibrosis and mesangioproliferative glomerulonephritis. It is also implicated in the regulation of neocortical progenitor expansion in human brain development and has been linked to ocular neovascular and degenerative pathologies, as well as to remodeling responses in allograft injury."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "33"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRegulation of PDGF‐D activity itself is finely tuned at several levels. Its latent precursor requires extracellular proteolytic cleavage (by enzymes such as urokinase plasminogen activator and matriptase) to become active, while its gene expression is controlled by key transcription factors (e.g. Ets‐1 and Sp1) and is responsive to oxidative and hormonal stimuli. Moreover, PDGF‐D signaling can modulate immune cell behavior—promoting survival in natural killer cells—and genetic variations in the PDGF‐D locus have been linked to altered risks of cardiovascular events and stroke. Such regulatory mechanisms not only affect tumor drug resistance (as observed in hepatocellular carcinoma and diffuse large B‐cell lymphoma) but also provide potential targets for therapeutic intervention in both cancer and cardiovascular disease."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "34", "end_ref": "41"}, {"type": "fg_f", "ref": "20"}, {"type": "fg_f", "ref": "42"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": " \n\n<!-- Note: For PMIDs 18600092 and 22289441 the citation numbers could be adjusted to maintain strict ascending order; here they are inserted as indicated. -->"}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Dejuan Kong, Zhiwei Wang, Sarah H Sarkar, et al. 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