Complex stiffness of smooth muscle cytoplasm in the presence of Ca-activated brevin.

Brevin, an F-actin severing protein, regulates actin gel-sol transformation in a Ca(2+)-dependent way. Here, we tested its effect on the stiffness of the cytoplasm of skinned smooth muscle, in the absence of actin-myosin interaction (inhibited myosin ATPase). Complex stiffness was measured by imposing sinusoidal stretches and releases at different frequencies (1-50 Hz). In the presence of Ca-activated brevin, the stiffness decreased by about 30%, at all frequencies, from its initial values in Ca-free, relaxing solution. This decrease reflected a fall in both elasticity and viscosity of the cytoplasm. We propose that brevin specifically operates on an actin network in parallel with the contractile apparatus, e.g. on the actin-filamin gel.