scholarly journals p38 Mitogen-Activated Protein Kinase Activity Commits Embryonic Stem Cells to Either Neurogenesis or Cardiomyogenesis

Stem Cells ◽  
2006 ◽  
Vol 24 (5) ◽  
pp. 1399-1406 ◽  
Author(s):  
Myriam Aouadi ◽  
Frédéric Bost ◽  
Leslie Caron ◽  
Kathiane Laurent ◽  
Yannick Le Marchand Brustel ◽  
...  
Keyword(s):  
Stem Cells ◽  
Embryonic Stem Cells ◽  
Protein Kinase ◽  
Kinase Activity ◽  
Embryonic Stem ◽  
Mitogen Activated Protein Kinase ◽  
Protein Kinase Activity ◽  
Mitogen Activated Protein

scholarly journals p38 Mitogen Activated Protein Kinase Controls Two Successive-Steps During the Early Mesodermal Commitment of Embryonic Stem Cells

2011 ◽  
Vol 20 (7) ◽  
pp. 1233-1246 ◽  
Author(s):  
Emilie Barruet ◽  
Ola Hadadeh ◽  
Franck Peiretti ◽  
Valérie M. Renault ◽  
Yasmine Hadjal ◽  
...  
Keyword(s):  
Stem Cells ◽  
Embryonic Stem Cells ◽  
Protein Kinase ◽  
Embryonic Stem ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein

scholarly journals IGF-I and insulin activate mitogen-activated protein kinase via the type 1 IGF receptor in mouse embryonic stem cells

Reproduction ◽  
2007 ◽  
Vol 134 (1) ◽  
pp. 41-49 ◽  
Author(s):  
Thanh T Nguyen ◽  
Allan M Sheppard ◽  
Peter L Kaye ◽  
Peter G Noakes
Keyword(s):  
Stem Cells ◽  
Protein Synthesis ◽  
Embryonic Stem Cells ◽  
Protein Kinase ◽  
Embryonic Stem ◽  
Mitogen Activated Protein Kinase ◽  
Igf I ◽  
Mitogen Activated Protein ◽  
Igf Receptor

Although IGF-I and insulin are important modulators of preimplantation embryonic physiology, the signalling pathways activated during development remain to be elucidated. As a model of preimplantation embryos, pluripotent mouse embryonic stem cells were used to investigate which receptor mediated actions of physiological concentrations of IGF-I and insulin on growth measured by protein synthesis. Exposure of mouse embryonic stem (ES) cells to 1.7 pM IGF-I or 1.7 nM insulin for 4 h caused ~25% increase in protein synthesis when compared with cells cultured in basal medium containing BSA. Dose–response studies showed 100-fold higher potency of IGF-I that pointed to the type 1 IGF receptor as the mediating receptor for both ligands. This was confirmed using an anti-type 1 IGF receptor-blocking antibody (αIR3). Both 1.7 pM IGF-I and 1.7 nM insulin increased phosphorylation of the type 1 IGF receptor and this increase was blocked by αIR3, but the insulin receptor was not phosphorylated. Finally, binding of either agonist led to downstream phosphorylation of ERK1/2 mitogen-activated protein kinase (MAPK) also via IGF-1R as this was blocked by αIR3. Together, these results suggest that IGF-I and insulin modulate ES cell physiology through binding to the type 1 IGF receptor and subsequent activation of MAPK pathway.

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