Vascular endothelial growth factor (VEGF) is a key signaling molecule that plays a crucial role in the formation of new blood vessels. While its effects have been extensively studied on vascular endothelial cells, VEGF also influences various other cell types, including monocytes, macrophages, neurons, cancer cells, and kidney epithelial cells. VEGF contributes to increased vascular permeability, stimulates the formation of new blood vessels (vasculogenesis) and the production of endothelial cells, encourages cell migration, and hinders programmed cell death (apoptosis). In laboratory settings, VEGF has been observed to promote both the division and movement of endothelial cells. Additionally, VEGF acts as a vasodilator, widening blood vessels, and enhances the permeability of small blood vessels. It was initially known as vascular permeability factor. VEGF is present in healthy cartilage; however, only cartilage affected by osteoarthritis expresses the VEGF receptors NP1, VEGFR1, and VEGFR2. Notably, the concentration of VEGF in the culture medium of chondrocytes derived from osteoarthritic cartilage was found to be over three times higher compared to the medium from normal chondrocytes.
Vascular Endothelial Growth Factor (VEGF) is a critical signaling protein involved in the formation of blood vessels, a process known as angiogenesis. It plays a pivotal role in both physiological and pathological conditions, including embryonic development, wound healing, and tumor growth . Human recombinant VEGF is a bioengineered form of this protein, produced using recombinant DNA technology to study its functions and therapeutic potential.
VEGF is a heparin-binding glycoprotein that typically exists as a homodimer. The human VEGF gene undergoes alternative splicing to produce several isoforms, including VEGF121, VEGF145, VEGF165, VEGF189, and VEGF206 . Among these, VEGF165 is the most studied and widely used in research and therapeutic applications .
VEGF primarily acts on endothelial cells, promoting their proliferation, migration, and new blood vessel formation. It binds to specific receptors on the surface of these cells, namely VEGFR-1 and VEGFR-2, triggering a cascade of signaling pathways essential for angiogenesis . VEGF also increases vascular permeability, which is crucial in both normal and pathological conditions.
The production of human recombinant VEGF involves cloning the VEGF gene into an expression vector, which is then introduced into a host cell, commonly Escherichia coli (E. coli). The host cells are cultured, and the recombinant protein is expressed, extracted, and purified using techniques such as nickel affinity chromatography . This process ensures a high yield of biologically active VEGF, which can be used for various research and therapeutic purposes.
Recombinant VEGF has shown promise in treating conditions that require enhanced angiogenesis, such as ischemic heart disease and peripheral artery disease . It is also being explored in cancer therapy, where inhibiting VEGF can reduce tumor vascularization and growth . However, the therapeutic use of VEGF must be carefully controlled due to its potent effects on blood vessel formation and permeability.