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J Biol Chem, Vol. 275, Issue 3, 1739-1748, January 21, 2000
From the Center for Cardiovascular Research, University of
Rochester, Rochester, New York 14642 and the § Department
of Internal Medicine (First Division), Kobe University School of
Medicine, Kobe 650-0017, Japan
Reactive oxygen species and growth factors
stimulate similar intracellular signal transduction events including
activation of Src kinase family members and extracellular
signal-regulated kinases (ERK1/2). A potentially important downstream
effector of Src and ERK1/2 is p90 ribosomal S6 kinase (p90RSK), which
plays an important role in cell growth by activating several
transcription factors as well as the
Na+/H+ exchanger. In the present study,
we determined whether H2O2 activates p90RSK to
gain insight into signal transduction mechanisms activated by reactive
oxygen species. H2O2 (200 µM)
stimulated ERK1/2 and p90RSK activity in lymphocytes, endothelial
cells, and fibroblasts. The MEK-1 inhibitor, PD98059 (30 µM), inhibited H2O2-mediated activation of ERK1/2 but not of p90RSK. An essential role for Fyn and
Ras in p90RSK activation was suggested by five findings. 1) The
tyrosine kinase inhibitor, herbimycin A, and the specific Src kinase
family inhibitor, PP1, blocked p90RSK activation by H2O2 in a concentration-dependent
manner. 2) p90RSK activation by H2O2 was
significantly reduced in fibroblasts derived from transgenic mice
deficient in Fyn, but not c-Src. 3) H2O2
rapidly activated Ras (peak at 2-5 min), which preceded p90RSK
activation (peak at 20 min). 4) Dominant negative Ras completely
blocked H2O2-induced activation of p90RSK. 5)
In Fyn
Reactive Oxygen Species Activate p90 Ribosomal S6 Kinase via
Fyn and Ras*
,§,
/ fibroblasts, activation of Ras by
H2O2 was significantly attenuated. These
results show essential roles for Fyn and Ras in
H2O2-mediated activation of p90RSK and
establish redox-sensitive regulation of Ras and p90RSK as a new
function for Fyn.
*
This study was supported by a grant from the Japanese Heart
Foundation, Bayer Yakuhin Research Grant Abroad (to J.-i. A.), and
National Institutes of Health Grants HL44721 and HL49192 (to B. C. B.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
These authors contributed equally to this work.
¶
To whom correspondence should be addressed: Cardiology Unit,
Box 679, 601 Elmwood Ave., University of Rochester School of Medicine
and Dentistry, Rochester, NY 14642. Tel.: 716-273-1947; Fax:
716-273-1497; E-mail: bradford_berk@urmc.rochester.edu.
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