The effect of soluble form of VEGF8-109 on vein endothelial cells

Vascular endothelial growth factor (VEGF) is a primarily endothelial cell-specific mitogen that plays a pivotal role in both vasculogenesis and angiogenesis. As a key regulator of neovascularization, it promotes embryonic development, wound healing and female reproductive functions. The function of VEGF is associated with various medical disorders, including tumor growth and metastasis, proliferative retinopathies and inflammatory conditions such as rheumatoid arthritis and psoriasis. VEGF elicits cellular responses through binding to the receptor tyrosine kinases, VEGFR1 and VEGFR2. VEGF is a dimeric molecule, each polypeptide chain contains multiple intrachain disulfide bonds, forming a cysteine knot motif. Soluble expression of receptor binding domain (RBD) of VEGF-A (residues 8-109) in SHuffle strain was optimized by recruiting of taguchi software.SHuffle strain is genetically engineered E. coli that is capable of oxidizing cysteines within proteins to form disulfide bonds. The quantification of expressed VEGF-A8-109 was performed by ELISA. The angiogenic potency of expressed VEGF-A8-109 was investigated by the proliferation assay on human umbilical vein endothelial cells (HUVEC). The results revealed that the recombinant protein can induce proliferation of HUVECand showed a significant increase in proliferation rate compared to control.

کلیدواژه ها:

VEGF ، Angiogenesis ، SHuffle strain ، HUVEC proliferation assay