In the late 1960s, Howard Holtzer's group at the University of Pennsylvania made the unexpected observation that virtually all eukaryotic cells assemble a variety of actin-based structures (Ishikawa et al., 1969). At that time, scientists thought that actin and myosin were restricted to muscle cells and ascribed contractile activity in other cells to a variety of molecules and structures. Holtzer's fluorescent antibodies to sarcomeric myosin decorated muscle but not any other cell type. “That's why,” he says, “we were so surprised to find actin filaments in nonmuscle cells.”
Holtzer and colleagues observed HMM-decorated filaments in every cell type examined, from skeletal and cardiac muscle cells to fibroblasts, chondroblasts, keratocytes, glia, and blood cells. Most decorated filaments in these different cell types localized to stress fibers. HMM-decorated filaments were also seen at the cleavage furrow of metaphase cells and at the core of the microvilli of intestinal and tracheal cells. In an early review of this work, Holtzer et al. (1972) suggested that there might be more than one type of actin and that each might be associated with a variety of actin-binding proteins in different cell types.
By the mid- to late-1970s, numerous studies using fluorescent antibodies to nonsarcomeric actin (Lazarides and Weber, 1974) and nonsarcomeric myosin (Adelstein et al., 1971), as well as fluorescent phalloidin for visualizing filamentous actin, confirmed the presence of both actin and myosin in most cells. Different cell types were later shown to contain distinct isoforms of both contractile proteins. In plant cells, actin filaments capable of binding HMM were shown to be involved in cytoplasmic streaming and moving organelles (Palevitz et al., 1974); Allen (1974) made similar observations for animal cells.