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Vascular endothelial growth factor A isoform 165 (VEGF-A165) is the predominant and most biologically active isoform of the VEGFA gene product, arising through alternative splicing[1][2][7][5]. VEGF-A165 is a secreted, disulfide-linked homodimeric glycoprotein with distinct N-terminal receptor-binding and C-terminal heparin-binding domains, mediating both interaction with endothelial cell VEGF receptors (primarily VEGFR2) and retention in the extracellular matrix[1][9]. It acts as a potent pro-angiogenic cytokine, promoting endothelial cell proliferation, migration, survival, and vascular permeability, and plays a crucial role in physiological and pathological angiogenesis, including embryonic development, tumor growth, retinal neovascularization, and various vascular conditions[3][5][7]. VEGF-A165 is a central therapeutic target for anti-angiogenic drugs approved for cancer and ocular diseases, and circulating levels have biomarker utility in oncology and vascular complications[3][4].
Monoclonal antibodies binding VEGF-A165 to prevent receptor activation (e.g., bevacizumab); Aptamer binding to VEGF-A165, blocking interaction with VEGFR-1 and VEGFR-2 (e.g., pegaptanib); Fusion protein trapping VEGF-A165, preventing receptor binding (e.g., aflibercept)
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