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VEGF-165 is the most abundant and potent isoform of human vascular endothelial growth factor A (VEGFA), a secreted glycoprotein that plays a central role in angiogenesis and vasculogenesis. It consists of two glycosylated polypeptide chains of 165 amino acids each forming a disulfide-linked homodimer. VEGF-165 binds to receptor tyrosine kinases on endothelial cells—primarily VEGFR1 (FLT1) and VEGFR2 (KDR/FLK1)—to stimulate proliferation, migration, survival of endothelial cells and increase vascular permeability. Its expression is induced by hypoxia and various cytokines. Pathologically, it is implicated in tumor angiogenesis as well as diseases involving abnormal blood vessel growth such as cancer and autoimmune disorders. Recombinant forms are used for research; gene therapy using plasmid encoding vegf-165 (e.g., pCMV-vefgf65) has been developed for therapeutic angiogenesis in peripheral artery disease under the brand name Neovasculgen[1][2][4][5][7][8].
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