Vascular endothelial growth factor (VEGF) is a hypoxia-inducible factor that promotes angiogenesis and vascular permeability. It is highly expressed in perinecrotic palisading cells in human glioblastomas. Hypoxia significantly enhances VEGF gene expression in vitro, and current evidence suggests that hypoxia is the main driver of VEGF expression in glioblastoma cells in vivo, promoting tumor angiogenesis and edema. The authors focus on disrupting the VEGF/VEGF receptor signaling pathway to inhibit tumor angiogenesis and edema in glioblastoma patients. VEGF is an endothelial cell-specific mitogen that induces angiogenesis and vascular permeability. It is important for embryonic development and tumor angiogenesis, and may induce peritumoral edema. VEGF and its receptors, VEGFR-1 and -2, have been identified in various human tumors, with extensive studies in malignant gliomas. Overexpression of VEGF and its receptors is associated with angiogenesis, vascular permeability, and edema in gliomas. Inhibiting the VEGF/receptor system may be an effective treatment for malignant gliomas. VEGF is a disulfide-linked dimeric glycoprotein with a N-terminal signal sequence and a heparin-binding domain. Four VEGF isoforms have been identified in humans: VEGF121, VEGF165, VEGF189, and VEGF206. VEGF165 is the most abundant and well-characterized isoform. VEGF is mitogenic for endothelial cells in vitro and angiogenic in vivo. It plays a role in developmental angiogenesis, as evidenced by its expression in the developing brain. VEGF is also a vascular permeability factor (VPF), inducing vascular permeability. VEGF induces vascular permeability through various mechanisms, including cytoskeletal changes and vesicular-vacuolar organelle activity. VEGF can induce fenestration in endothelial cells, which is important for capillary transport in organs like the kidney. VEGF exerts its function via two high-affinity tyrosine kinase receptors, VEGFR-1 and VEGFR-2. These receptors are involved in vasculogenesis and angiogenesis. VEGFR-1 is expressed in the endothelial cell lineage in the mouse embryo and is downregulated in the adult brain. The function of VEGFR-1 is not fully understood.Vascular endothelial growth factor (VEGF) is a hypoxia-inducible factor that promotes angiogenesis and vascular permeability. It is highly expressed in perinecrotic palisading cells in human glioblastomas. Hypoxia significantly enhances VEGF gene expression in vitro, and current evidence suggests that hypoxia is the main driver of VEGF expression in glioblastoma cells in vivo, promoting tumor angiogenesis and edema. The authors focus on disrupting the VEGF/VEGF receptor signaling pathway to inhibit tumor angiogenesis and edema in glioblastoma patients. VEGF is an endothelial cell-specific mitogen that induces angiogenesis and vascular permeability. It is important for embryonic development and tumor angiogenesis, and may induce peritumoral edema. VEGF and its receptors, VEGFR-1 and -2, have been identified in various human tumors, with extensive studies in malignant gliomas. Overexpression of VEGF and its receptors is associated with angiogenesis, vascular permeability, and edema in gliomas. Inhibiting the VEGF/receptor system may be an effective treatment for malignant gliomas. VEGF is a disulfide-linked dimeric glycoprotein with a N-terminal signal sequence and a heparin-binding domain. Four VEGF isoforms have been identified in humans: VEGF121, VEGF165, VEGF189, and VEGF206. VEGF165 is the most abundant and well-characterized isoform. VEGF is mitogenic for endothelial cells in vitro and angiogenic in vivo. It plays a role in developmental angiogenesis, as evidenced by its expression in the developing brain. VEGF is also a vascular permeability factor (VPF), inducing vascular permeability. VEGF induces vascular permeability through various mechanisms, including cytoskeletal changes and vesicular-vacuolar organelle activity. VEGF can induce fenestration in endothelial cells, which is important for capillary transport in organs like the kidney. VEGF exerts its function via two high-affinity tyrosine kinase receptors, VEGFR-1 and VEGFR-2. These receptors are involved in vasculogenesis and angiogenesis. VEGFR-1 is expressed in the endothelial cell lineage in the mouse embryo and is downregulated in the adult brain. The function of VEGFR-1 is not fully understood.