Myosin light chain kinase is expressed in neurons and glia: immunoblotting and immunocytochemical studies.

The contractile protein myosin is thought to subserve motility-related functions in a wide range of eukaryotic non-muscle cells including both neurons and glia. To determine if the Ca2+/calmodulin-dependent enzyme, myosin light chain kinase (MLCK) is involved in the regulation of neural myosin we investigated the presence and localization of MLCK in a variety of neural tissues by immunoblotting and immunocytochemistry. A specific immunoreactive protein (M(r) = 146,000) was detected in blotted homogenates from many regions of rat brain and from primary cultures of either astrocytes or cerebellar granule cells grown in the absence of other cell types. At the light microscopic level, MLCK-immunoreactivity was evident in many regions of rat brain, as well as in the cultured astrocytes and cerebellar granule cells. MLCK-immunoreactivity was observed to be largely cytosolic in astrocytes but with a proportion associated with the cytoskeleton. In the cerebellar granule cells immunoreactivity was present in neuronal processes as well as somata. The detection of MLCK in neural cells suggests that MLCK-catalyzed myosin phosphorylation may couple changes in intracellular calcium concentrations to motility-related functions of neurons and glia.