NDLI: Differential activation of mitogen-activated protein kinase in response to basic fibroblast growth factor in skeletal muscle cells.

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Differential activation of mitogen-activated protein kinase in response to basic fibroblast growth factor in skeletal muscle cells.

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Differential activation of mitogen-activated protein kinase in response to basic fibroblast growth factor in skeletal muscle cells.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Campbell, J. S. Krebs, E. G. Wenderoth, M. P. Hauschka, S. D.
Description	Author Affiliation: Campbell JS ( Department of Pharmacology, University of Washington, Seattle 98195.);
Abstract	In the MM14 mouse myoblast cell line, fibroblast growth factor (FGF) stimulates proliferation and represses differentiation. However, the intracellular signaling pathways used by FGF to affect these cellular processes are unknown. The predominant FGF receptor present on MM14 cells, FGFR1, is a receptor tyrosine kinase capable of activating the mitogen-activated protein kinase (MAPK) cascade in fibroblast and neuronal cell lines. To determine whether the FGF signal is mediated via the MAPK cascade in myoblasts, MM14 cells were stimulated with basic FGF (bFGF) and activities of the various kinases were measured. After withdrawal from serum and bFGF for 3 hr, bFGF stimulated MAPK kinase (MAPKK) activity, but MAPK and S6 peptide kinase activities were not detected. In contrast, when serum and bFGF were withdrawn for 10 hr, the activities of MAPKK, MAPK, and S6 peptide kinase were all stimulated by bFGF treatment. The inability of bFGF to stimulate MAPK after 3 hr of withdrawal may be due, in part, to the presence of a MAPK phosphatase activity that was detected in MM14 cell extracts. This dephosphorylating activity diminishes during commitment to terminal differentiation and is inhibited by sodium orthovanadate. Thus, the ability of bFGF to stimulate MAPK in MM14 cells is correlated with the loss of a MAPK phosphatase activity. These results show that although bFGF activates MAPKK in proliferating myoblasts, the mitogenic signal does not progress to the downstream kinases, providing a physiological example of an uncoupling of the MAPK cascade.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	3
Volume Number	92
Language	English
Publisher	National Academy of Sciences
Publisher Date	1995-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Calcium-Calmodulin-Dependent Protein Kinases Metabolism Fibroblast Growth Factor 2 Pharmacology Muscle, Skeletal Enzymology Animals Cell Differentiation Drug Effects Cell Division Cell Fractionation Cell Line Enzyme Activation Mice Microcystins Mitogen-Activated Protein Kinase 1 Mitogen-Activated Protein Kinase Kinases Cytology Peptides, Cyclic Phosphoprotein Phosphatases Antagonists & Inhibitors Protein Kinases Protein-Serine-Threonine Kinases Recombinant Proteins Ribosomal Protein S6 Kinases Signal Transduction Vanadates Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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