Abstract
VEGF is an approximately 45 kDa homodimeric glycoprotein in the VEGF family, which includes more than seven proteins. Five of the polypeptides are encoded by distinct genes in the human genome: VEGF-A (VEGF), VEGF-B, VEGF-C, VEGF-D, and PGF (placenta growth factor) (Carmeliet, Oncology 69:4–10, 2005; Shibuya, Vascular permeability/vascular endothelial growth factor. In: Figg WD, Folkman J (eds) Angiogenesis. Springer, New York, pp 89–98, 2008). VEGF is considered to play a key role in regulating angiogenesis both in normal and malignant cells. VEGF-A exists in many different isoforms as a result of alternative exon splicing; the most frequent subtypes are VEGF121, VEGF165, VEGF189, and VEGF206. The shorter amino acid sequence isoform VEGF121 is soluble, in contrast to VEGF165, VEGF189, and VEGF206, which are heparin bound with varying affinity. VEGF121 and VEGF165, which also have the propensity to be unbound, are believed to have a central role in tumor angiogenesis (Kerbel and Ellis, Angiogenesis. In: DeVita, Hellman, Rosenberg (eds) Cancer. LWW, Philadelphia, pp 101–112, 2011).
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Ulahannan, S. (2017). VEGF. In: Marshall, J. (eds) Cancer Therapeutic Targets. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-0717-2_71
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DOI: https://doi.org/10.1007/978-1-4419-0717-2_71
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