Ca2+ transient, cell volume, and microviscosity of the plasma membrane in smooth muscle

Despite pronounced differences by which membrane-depolarizing or phospholipase C-activating stimuli initiate contractile responses, a rise in [Ca2+](i) is considered the primary mechanism for induction of smooth muscle contractions. Subsequent to the formation of the well-characterized Ca-4(2+) calmodulin complex, interaction with the catalytic subunit of myosin tight chain kinase triggers phosphorylation of 20 kDa myosin light chain and activates actin dependent Mg2+-ATPase activity, which ultimately leads to the development of tension. The present article reviews the fundamental mechanisms leading to an increase in [Ca2+](i) and discusses the biochemical processes involved in the transient and sustained phases of contraction. Moreover, the commentary summarizes current knowledge on the modulatory effect of changes in the microviscosity of the plasma membrane on the Ca2+ transient as well as the contractile response of smooth muscle. Evidence has accumulated that these changes in microviscosity alter the activity of membrane bound enzymes and affect the generation of endogenous mediators responsible for the regulation of cytosolic Ca2+ concentrations and for the [Ca2+](i) sensitivity of myosin light chain, phosphorylation. (C) 1991 Elsevier Science Inc.