Abstract
FGF2 has been shown to enhance proliferation and maintain differentiation potential in hMSCs during in vitro propagation. In this study, we investigated the role of mitogen-activated protein kinase in the functions of FGF2 in hMSCs. We demonstrated that FGF2 induces the transient activation of c-Jun N-terminal kinase (JNK), but not extracellular signal-regulated protein kinase or p38 protein kinase. SP600125 and a dominant negative JNK1 significantly reduced the FGF2-enhanced proliferation of hMSCs. Treatment with SP600125 also diminished the activity of FGF2 in the maintenance of adipogenic and osteogenic differentiation potential. These results suggest that JNK signaling is involved in the FGF2-induced stimulation of the proliferation and the maintenance of differentiation potential in hMSCs.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Anthracenes / metabolism
-
Bone Marrow Cells / cytology
-
Bone Marrow Cells / physiology
-
Cell Differentiation / physiology
-
Cell Proliferation*
-
Cells, Cultured
-
Enzyme Activation
-
Extracellular Signal-Regulated MAP Kinases / metabolism
-
Fibroblast Growth Factor 2 / metabolism*
-
Humans
-
JNK Mitogen-Activated Protein Kinases / antagonists & inhibitors
-
JNK Mitogen-Activated Protein Kinases / genetics
-
JNK Mitogen-Activated Protein Kinases / metabolism*
-
Mesenchymal Stem Cells / cytology
-
Mesenchymal Stem Cells / physiology*
-
Recombinant Fusion Proteins / genetics
-
Recombinant Fusion Proteins / metabolism
-
Signal Transduction / physiology*
-
p38 Mitogen-Activated Protein Kinases / metabolism
Substances
-
Anthracenes
-
Recombinant Fusion Proteins
-
Fibroblast Growth Factor 2
-
pyrazolanthrone
-
Extracellular Signal-Regulated MAP Kinases
-
JNK Mitogen-Activated Protein Kinases
-
p38 Mitogen-Activated Protein Kinases