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Postnatal regulation of X,K‐ ATP ases in rat skin and conserved lateroapical polarization of Na,K‐ ATP ase in vertebrate epidermis
Author(s) -
Pestov Nikolay B.,
Korneenko Tatyana V.,
Shakhparonov Mikhail I.,
Modyanov Nikolai N.
Publication year - 2013
Publication title -
experimental dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.108
H-Index - 96
eISSN - 1600-0625
pISSN - 0906-6705
DOI - 10.1111/exd.12149
Subject(s) - xenopus , epidermis (zoology) , gene isoform , biology , microbiology and biotechnology , biochemistry , anatomy , gene
Development of epidermis creates stratified epithelium with different sets of ion‐transporting enzymes in its layers. We have characterized expression of N a,K‐ and H ,K‐ ATP ase α and β subunits and FXYD isoforms in rat skin. Maturation of rat skin from newborn to adult is associated with an increase in FXYD 4 and a decrease of Na,K‐ ATP ase α1‐isoform, ATP 1B4 and FXYD 6 transcripts. Na,K‐ ATP ase of rat epidermis is represented predominantly by α1 and β3 isoforms. Keratinization is associated with the loss of the Na,K‐ ATP ase α‐subunit and an enrichment of αng. Na,K‐ ATP ase α1 is abundant in the innermost layer, stratum basale , where it is lacking in basal membranes, thus indicating lateroapical polarization of Na,K‐ ATP ase. Immunocytochemical detection of Na,K‐ ATP ase 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.