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Division of Molecular and Cellular Physiology, Department of Physiological Sciences, Biomedical Center, Lund University, SE-221 84 Lund, Sweden
Signaling mechanisms for
stretch-dependent growth and differentiation of vascular smooth muscle
were investigated in mechanically loaded rat portal veins in organ
culture. Stretch-dependent protein synthesis was found to depend on
endogenous release of angiotensin II. Autoradiography after
[35S]methionine incorporation revealed stretch-dependent
synthesis of several proteins, of which SM22 and actin were
particularly prominent. Inhibition of RhoA activity by cell-permeant C3
toxin increased tissue mechanical compliance and reduced
stretch-dependent extracellular signal-regulated kinase (ERK)1/2
activation, growth, and synthesis of actin and SM22, suggesting a role
of the actin cytoskeleton. In contrast, inhibition of Rho-associated
kinase by Y-27632 did not reduce ERK1/2 phosphorylation or actin and SM22 synthesis and did not affect tissue mechanical compliance but
still inhibited overall growth. The actin polymerization inhibitors latrunculin B and cytochalasin D both inhibited growth and caused increased tissue compliance. Whereas latrunculin B
concentration-dependently reduced actin and SM22 synthesis,
cytochalasin D did so at low (10
8 M) but not at high
(106 M) concentration. The results show that stretch
stabilizes the contractile smooth muscle phenotype. Stretch-dependent
differentiation marker expression requires an intact cytoskeleton for
stretch sensing, control of protein expression via the level of
unpolymerized G-actin, or both.
SM22; cytoskeleton; rat portal vein; RhoA; hypertension
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