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Vol. 12, Issue 9, 2730-2741, September 2001
*Department of Pathology, CMU, University of Geneva, 1211 Geneva 4, Switzerland; and To evaluate whether Department of Cell Biology, University
of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104
-smooth muscle actin (-SMA) plays a role
in fibroblast contractility, we first compared the contractile activity
of rat subcutaneous fibroblasts (SCFs), expressing low levels of
-SMA, with that of lung fibroblasts (LFs), expressing high levels of
-SMA, with the use of silicone substrates of different stiffness
degrees. On medium stiffness substrates the percentage of cells
producing wrinkles was similar to that of -SMA-positive cells in
each fibroblast population. On high stiffness substrates, wrinkle
production was limited to a subpopulation of LFs very positive for
-SMA. In a second approach, we measured the isotonic contraction of
SCF- and LF-populated attached collagen lattices. SCFs exhibited 41%
diameter reduction compared with 63% by LFs. TGF
1 increased -SMA
expression and lattice contraction by SCFs to the levels of LFs;
TGF-antagonizing agents reduced -SMA expression and lattice
contraction by LFs to the level of SCFs. Finally, 3T3 fibroblasts
transiently or permanently transfected with -SMA cDNA exhibited a
significantly higher lattice contraction compared with wild-type 3T3
fibroblasts or to fibroblasts transfected with -cardiac and - or
-cytoplasmic actin. This took place in the absence of any change in
smooth muscle or nonmuscle myosin heavy-chain expression. Our results
indicate that an increased -SMA expression is sufficient to enhance
fibroblast contractile activity.
Corresponding author. E-mail address:
Giulio.Gabbiani{at}medecine.unige.ch.
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