Parvalbumin is thought to act as a Ca2+ buffer in skeletal muscle fibe
rs, but its physiological role in brain, kidney, and testis remains un
clear. We have transfected parvalbumin cDNA into a human ovarian adeno
carcinoma cell Line, which normally does not express this protein. The
induced expression of parvalbumin under the control of three differen
t promoters causes: (1) changes in the morphology of the cells from ep
itheloid to fusiform, (2) an increase in motility of whole cell cluste
rs, and (3) a decrease in the mitotic rate. Transfection with a mutate
d cDNA of rat parvalbumin incapable of binding Ca2+ had no effect on t
hese three parameters. Our results indicate that ectopic expression of
parvalbumin influences not only cell division [Rasmussen and Means (1
989) 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 no
nmuscle cells. (C) 1995 Academic Press, Inc.