Snake venom proteins related to "vascular endothelial growth factor": new tools for therapeutic angiogenesis

• Published in: Archives de l'Institut Pasteur de Tunis Vol. 90; no. 1-4; pp. 23 - 37
• Main Authors: Aloui, Z, Essafi-Benkhadir, K, Karoui, H, Gasmi, A
• Format: Journal Article
• Language: French
• Published: Tunisia 2013
• Subjects: Humans; Neovascularization, Physiologic - drug effects; Snake Venoms - therapeutic use; Vascular Endothelial Growth Factor A - physiology; Vascular Endothelial Growth Factor A - therapeutic use
• ISSN: 0020-2509

The Vascular Endothelial Growth Factor "VEGF" plays a pivotal role in the stimulation of angiogenesis. The VEGF isoforms (A-D) and PlGF act in a coordinate fashion to develop the vascular network. Numerous proteins closely related in structure and function to VEGF-A have been reported and were grouped in the VEGF family. Some predators make use of VEGF-like molecules with devastating results for their prey. VEGF-E, investigated in 1994, is encoded by the parapoxvirus (Orf virus). VEGF-F is a common term designating molecules which were isolated from snake venom (also known as svVEGF). These proteins are disulphide-linked homodimers of 110 amino acids each and have a molecular weight of approximately 25 kDa. Their primary structures show approximately 50% identity to VEGF-A. However, unlike VEGF-A, they do not contain any N-linked glycosylation sites. They interact with heparin but have a different binding domain from that of VEGF-A. Among species, these svVEGFs vary extensively in amino acid sequences and in receptor-binding specificities towards endogenous VEGF receptors. Understanding the properties that determine the specificity of these interactions could improve our knowledge of the VEGF-receptor interactions. This knowledge is essential to the development of new drugs in angiogenesis. This knowledge is essential to the development of new drugs in angiogenesis.