Expression of vascular endothelial growth factor (VEGF) in human osteosarcoma cells transfected with adeno-associated virus-antisense VEGF.
- Author:
Weiguo XU
1
;
Anmin CHEN
;
Yibei ZHANG
;
Chengla YI
Author Information
1. Department of Orthopaedics, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, China.
- Publication Type:Journal Article
- MeSH:
Bone Neoplasms;
metabolism;
pathology;
Dependovirus;
genetics;
Gene Transfer Techniques;
Genetic Vectors;
Humans;
Oligodeoxyribonucleotides, Antisense;
pharmacology;
Osteosarcoma;
metabolism;
pathology;
Transfection;
Tumor Cells, Cultured;
Vascular Endothelial Growth Factor A;
antagonists & inhibitors;
biosynthesis;
genetics
- From:
Journal of Huazhong University of Science and Technology (Medical Sciences)
2004;24(3):279-283
- CountryChina
- Language:English
-
Abstract:
The expression of protein vascular endothelial growth factor (VEGF) in osteosarcoma cells transfected with adeno-associated virus (rAAV)-antisense VEGF was studied to provide the foundation of osteosarcoma treatment through antivascularization. The rAAV-antisense VEGF at different doses (0, 20, 50, 100, 200, 240 microl) was transfected into osteosarcoma MG-63 cell. The cells and culture supernatants were collected before and after tansfection. The expression of VEGF protein was detected by using immunohistochemical staining (SP) and Western blot. SP and Western-blot tests revealed that the MG-63 Cells transfected with rAAV-antisense VEGF had less staining than those without transfection with rAAV-antisense VEGF, and the staining intensity was negatively correlated with the doses of genes. The corresponding A values of transfected genes with different doses of rAAV-antisense VEGF (0, 20, 50, 100, 200, 240 microl) were 86614 +/- 13776, 73245 +/- 15414, 61078 +/- 12124, 54657 +/- 10953, 39802 +/- 11308, 32014 +/- 15057 respectively, with the difference being significant (P<0.05). It was concluded that the expression of VEGF protein in MG-63 cells could be inhibited by rAAV-antisense VEGF.
