Open AccessActivation of mitogen-activated protein kinases by vascular endothelial growth factor and basic fibroblast growth factor in capillary endothelial cells is inhibited by the antiangiogenic factor 16-kDa N-terminal fragment of prolactin.
Author(s) -
Gisela D’Angelo,
Ingrid Struman,
Joseph Martial,
Richard I. Weiner
Publication year - 1995
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.92.14.6374
Subject(s) - mapk/erk pathway , vascular endothelial growth factor , basic fibroblast growth factor , vascular endothelial growth factor b , vascular endothelial growth factor c , autophosphorylation , microbiology and biotechnology , angiogenesis , vascular endothelial growth factor a , mitogen activated protein kinase , fibroblast growth factor , protein kinase a , growth factor , vascular endothelial growth inhibitor , biology , fibroblast growth factor receptor , chemistry , kinase , cancer research , biochemistry , receptor , vegf receptors
A number of factors both stimulating and inhibiting angiogenesis have been described. In the current work, we demonstrate that the angiogenic factor vascular endothelial growth factor (VEGF) activates mitogen-activated protein kinase (MAPK) as has been previously shown for basic fibroblast growth factor. The antiagiogenic factor 16-kDa N-terminal fragment of human prolactin inhibits activation of MAPK distal to autophosphorylation of the putative VEGF receptor, Flk-1, and phospholipase C-gamma. These data show that activation and inhibition of MAPK may play a central role in the control of angiogenesis.