Development of epidermis creates stratified epithelium with different sets of ion-transporting enzymes in its layers. We have characterized expression of Na,K- and H,K-ATPase α and β subunits and FXYD isoforms in rat skin. Maturation of rat skin from newborn to adult is associated with an increase in FXYD4 and a decrease of Na,K-ATPase α1-isoform, ATP1B4 and FXYD6 transcripts. Na,K-ATPase of rat epidermis is represented predominantly by α1 and β3 isoforms. Keratinization is associated with the loss of the Na,K-ATPase α-subunit and an enrichment of αng. Na,K-ATPase α1 is abundant in the innermost layer, stratum basale, where it is lacking in basal membranes, thus indicating lateroapical polarization of Na,K-ATPase. Immunocytochemical detection of Na,K-ATPase in Xenopus laevis skin shows that cellular and subcellular localization of the enzyme has a pattern highly similar to that of mammals: basolateral in glandular epithelium and lateroapical in epidermis.
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