Cationic currents in mature MDCK cells are almost exclusively due to K+ channels. Harvesting with trypsin-EDTA destroys 80-90% of these channels. Upon replating, K+ currents recover in 12-20 h, by means a process that requires synthesis of proteins and of RNA. In the present work we demonstrate that this restoration depends on a Ca2+ activated-cell contact. Thus, cells in confluent monolayers bathed with 1.8 mM Ca2+ have a K+ current of 343 +/- 82 pA; confluent without Ca2+ have only 90 +/- 12 pA (27% of control; and without cell-cell contacts incubated with 1.8 mM Ca2+ (subconfl+Ca2+) have 104 +/- 21 pA (31% of control). This demonstration that the expression of K+ channels depends on Ca-activated cell-attaching molecules suggests that a molecule of the type of uvomorulin is involved.