Ligands that activate protein kinase-C differ in their ability to regulate basic fibroblast growth factor and insulin-like growth factor-I messenger ribonucleic acid levels.

Endocrinology ◽  
1993 ◽  
Vol 132 (4) ◽  
pp. 1593-1602 ◽  
Author(s):  
W L Lowe ◽  
M A Yorek ◽  
R M Teasdale
Keyword(s):  
Protein Kinase C ◽  
Growth Factor ◽  
Protein Kinase ◽  
Fibroblast Growth Factor ◽  
Ribonucleic Acid ◽  
Fibroblast Growth ◽  
Messenger Ribonucleic Acid ◽  
Factor I ◽  
Kinase C ◽  
Activate Protein Kinase

Requirement for Protein Kinase C Activation in Basic Fibroblast Growth Factor–Induced Human Endothelial Cell Proliferation

1995 ◽  
Vol 77 (2) ◽  
pp. 231-238 ◽  
Author(s):  
K. Craig Kent ◽  
Shinsuke Mii ◽  
Elizabeth O. Harrington ◽  
James D. Chang ◽  
Sheila Mallette ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Protein Kinase C ◽  
Endothelial Cell ◽  
Growth Factor ◽  
Protein Kinase ◽  
Fibroblast Growth Factor ◽  
Endothelial Cell Proliferation ◽  
Fibroblast Growth ◽  
Kinase C ◽  
Protein Kinase C Activation

scholarly journals Basic fibroblast growth factor requires a long-lasting activation of protein kinase C to induce cell proliferation in transformed fetal bovine aortic endothelial cells.

1991 ◽  
Vol 2 (9) ◽  
pp. 719-726 ◽  
Author(s):  
M Presta ◽  
L Tiberio ◽  
M Rusnati ◽  
P Dell'Era ◽  
G Ragnotti
Keyword(s):  
Cell Proliferation ◽  
Protein Kinase C ◽  
Growth Factor ◽  
Protein Kinase ◽  
Fibroblast Growth Factor ◽  
Fibroblast Growth ◽  
Mitogenic Response ◽  
Kinase C ◽  
Fetal Bovine ◽  
Induce Cell Proliferation

Basic fibroblast growth factor (bFGF) induces a protein kinase C (PKC)-dependent mitogenic response in transformed fetal bovine aortic endothelial GM 7373 cells. A long-lasting interaction of bFGF with the cell is required to induce cell proliferation. bFGF-treated cells are in fact committed to proliferate only after they have entered the phase S of the cell cycle, 12-14 h after the beginning of bFGF treatment. Before that time, the mitogenic response to bFGF is abolished by 1) removal of extracellular bFGF by suramin, 2) addition of neutralizing anti-bFGF antibodies to the culture medium, 3) inhibition of PKC activity by the protein kinase inhibitor H-7, and 4) down-regulation of PKC by cotreatment with phorbol ester. Thus the requirement for a prolonged interaction of bFGF with the cell reflects the requirement for a prolonged activation of PKC. Similar conclusions can be drawn for the PKC activators 12-O-tetradecanoyl phorbol 13-acetate and 1,2-dioctanoyl-sn-glycerol. The two molecules require 16 and 6 h, respectively, of activation of PKC to induce 50% of maximal cell proliferation. The requirement for a long-lasting activation of PKC appears to be a mechanism for the control of cell proliferation capable of discriminating among transient nonmitogenic stimuli and long-lasting mitogenic stimuli.

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