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

The action of brevin, an F-actin severing protein, on the mechanical properties and ATPase activity of skinned smooth muscle

Brevin is a protein which regulates the actin gel-sol transformation: it severs F-actin filaments into shorter ones. This action is Ca-dependent and is prevented by tropomyosin. We tested the effect of brevin on isometric contractions of skinned smooth muscle (taenia coli) and noted a dramatic loss of tension that possibly reflects some F-actin fragmentation. This effect is tentatively attributed to a partial loss of tropomyosin in the skinning procedure. We also studied the effect of brevin on unloaded shortenings of skinned preparations: thin bundles and enzymatically dissociated cells. We observed a marked increase of the velocity of shortening in the presence of brevin. This effect cannot be attributed to an increased ATPase activity as the latter is slightly reduced in the presence of brevin. We interpret this result as reflecting a decrease in internal resistance to movement, possibly by solation of an actin-filamin domain