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(Received for publication, March 12, 1996)
From the The kinases and regulatory proteins that convey
signals initiated by transforming growth factor-
Volume 271, Number 28,
Issue of July 12, 1996
pp. 16567-16572
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
1 on Gene Expression
,
Division of Nephrology, Department of
Pediatrics, The Hospital for Sick Children, University of Toronto,
Toronto M5G 1X8, Canada and the § Division of Nephrology,
Technion and Rambam Medical Center, Haifa 31096, Israel
(TGF-) to the
nucleus are poorly characterized. To study the role of the
extracellular signal-regulated kinase (ERK) pathway in this process, we
transiently transfected NIH 3T3 fibroblasts with TGF--responsive
luciferase reporter genes and expression vectors designed to interrupt
this kinase cascade. Mitogen-activated protein (MAP) kinase
phosphatase-1 and a dominant negative MAP/ERK kinase 1 mutant reduced
stimulation of plasminogen activator inhibitor-1 (PAI-1) promoter
activity by TGF-1 from 11.5- to 4-fold and 4.9-fold, respectively.
Similar results were observed with the type I collagen promoters.
TGF-1 increased ERK1 activity 4.5-fold at 5 min and 3.1-fold at
3 h, while Jun kinase and p38 activity were not affected.
Cotransfection of a dominant negative mutant of the small G protein,
Rac, but not dominant negative Ras, Cdc42, or Rho mutants, reduced the
effects of TGF-1 on the PAI-1 promoter by approximately half. In
support of a role for Rac in signaling by TGF-, GTP binding to Rac
was increased 3.7-fold following exposure of NIH 3T3 cells to TGF-1
for 3 min. These findings indicate that TGF-1 modulates gene
expression partly through ERK and Rac in NIH 3T3 cells.
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