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1 Division of Molecular and Cellular Physiology, Department of Physiological Sciences, Lund University, Lund, Sweden
* To whom correspondence should be addressed. E-mail: Per.Hellstrand{at}mphy.lu.se.
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 following [35S-]methionine incorporation revealed stretch-dependent synthesis of several proteins, of which SM22 and actin were particularly prominent. Inhibition of RhoA activity by cell-permeable C3 toxin increased tissue mechanical compliance and reduced stretch-dependent ERK1/2 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 ERK 1/2 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 (10-6 M) concentration. The results show that stretch stabilizes the contractile smooth muscle phenotype. Stretch-dependent differentiation marker expression requires an intact cytoskeleton either for stretch sensing, for control of protein expression via the level of unpolymerized G-actin, or both.
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