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Titolo:
DIFFERENTIAL ACTIVATION OF MITOGEN-ACTIVATED PROTEIN-KINASE IN RESPONSE TO BASIC FIBROBLAST GROWTH-FACTOR IN SKELETAL-MUSCLE CELLS
Autore:
CAMPBELL JS; WENDEROTH MP; HAUSCHKA SD; KREBS EG;
Indirizzi:
UNIV WASHINGTON,DEPT PHARMACOL SEATTLE WA 98195 UNIV WASHINGTON,DEPT PHARMACOL SEATTLE WA 98195 UNIV WASHINGTON,DEPT BIOCHEM SEATTLE WA 98195 UNIV WASHINGTON,HOWARD HUGHES MED INST SEATTLE WA 98195
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 3, volume: 92, anno: 1995,
pagine: 870 - 874
SICI:
0027-8424(1995)92:3<870:DAOMPI>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
IMMEDIATE-EARLY GENE; SIGNAL-TRANSDUCTION; TERMINAL DIFFERENTIATION; ENCODED PROTEIN; S6 KINASE; CASCADE; PHOSPHORYLATES; PURIFICATION; PHOSPHATASE; RSK;
Keywords:
MITOGEN-ACTIVATED PROTEIN KINASE KINASE; MITOGEN-ACTIVATED PROTEIN KINASE PHOSPHATASE ACTIVITY; MUSCLE DIFFERENTIATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
J.S. Campbell et al., "DIFFERENTIAL ACTIVATION OF MITOGEN-ACTIVATED PROTEIN-KINASE IN RESPONSE TO BASIC FIBROBLAST GROWTH-FACTOR IN SKELETAL-MUSCLE CELLS", Proceedings of the National Academy of Sciences of the United Statesof America, 92(3), 1995, pp. 870-874

Abstract

In the MM114 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 theMAPK cascade in myoblasts, MM14 cells mere 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 In contrast, when serum and bFGF were withdrawn for 10 hr, the activities of MAPKK, MAPK, and S6 peptide kinase were all stimulated by bFGF treatment.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.

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Documento generato il 29/09/20 alle ore 20:38:40