Changes in shape and motility of cells transfected with parvalbumin cDNA.

Parvalbumin is thought to act as a Ca2+ buffer in skeletal muscle fibers, but its physiological role in brain, kidney, and testis remains unclear. We have transfected parvalbumin cDNA into a human ovarian adenocarcinoma cell line, which normally does not express this protein. The induced expression of parvalbumin under the control of three different promoters causes: (1) changes in the morphology of the cells from epitheloid to fusiform, (2) an increase in motility of whole cell clusters, and (3) a decrease in the mitotic rate. Transfection with a mutated cDNA of rat parvalbumin incapable of binding Ca2+ had no effect on these three parameters. Our results indicate that ectopic expression of parvalbumin influences not only cell division [Rasmussen and Means (1989) Mol. Endocrinol. 3, 588-596], but also cell shape and motility by modulating intracellular Ca2+ handling. This may be a basic function of parvalbumin when it is intrinsically expressed in differentiated nonmuscle cells.