Abstract
The effects of vascular endothelial growth factor (VEGF) on cytoskeletal actin networks, cell morphology and tyrosine phosphorylation of cellular proteins were studied in Balb/c3T3 A31-1-1 cells. VEGF induced the disorganization of actin stress fibers accompanied by drastic morphological rounding. A binding assay of [125I]VEGF demonstrated high and low affinity receptors for VEGF in the cells. Moreover, VEGF induced tyrosine phosphorylation of at least five cellular proteins in a dose and a time dependent manner. A tyrosine kinase inhibitor, genistein, inhibited the VEGF-induced morphological rounding. These results indicate that VEGF exerts the alteration of cytoskeletal organization resulting in morphological changes through inducing receptor-mediated tyrosine phosphorylation of cellular proteins.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
3T3 Cells
-
Actins / metabolism*
-
Animals
-
Baculoviridae / genetics
-
Binding Sites
-
Cells, Cultured
-
Endothelial Growth Factors / genetics
-
Endothelial Growth Factors / metabolism
-
Endothelial Growth Factors / pharmacology*
-
Genistein
-
Isoflavones / pharmacology
-
Lymphokines / genetics
-
Lymphokines / metabolism
-
Lymphokines / pharmacology*
-
Mice
-
Mice, Inbred BALB C
-
Moths
-
Phosphorylation
-
Protein-Tyrosine Kinases / antagonists & inhibitors
-
Tyrosine / metabolism*
-
Vascular Endothelial Growth Factor A
-
Vascular Endothelial Growth Factors
Substances
-
Actins
-
Endothelial Growth Factors
-
Isoflavones
-
Lymphokines
-
Vascular Endothelial Growth Factor A
-
Vascular Endothelial Growth Factors
-
Tyrosine
-
Genistein
-
Protein-Tyrosine Kinases