Functional expression of AQP3 in human skin epidermis and reconstructed epidermis

Rachid Sougrat, Maryse Morand, Catherine Gondran, Patrick Barré, R. Gobin, Frediric Bonté, Mara Dumas, Jean Marc Verbavatz

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    144 Scopus citations

    Abstract

    The purpose of this study was to examine the presence of aquaporin water channels in human skin and to assess their functional role. On western blots of human epidermis obtained from plastic surgery, a strong signal was obtained with polyclonal anti-aquaporin-3 antibodies. By indirect immunofluorescence on 5 μm cryosections, anti-aquaporin-3 antibodies strongly stained keratinocyte plasma membranes in human epidermis, whereas no staining was observed in the dermis or the stratum corneum or when anti-aquaporin-3 antibodies were preabsorbed with the peptide used for immunization. Similarly, a strong signal with anti-aquaporin-3 antibodies was observed in keratinocyte plasma membranes of reconstructed human epidermis in culture at the air-liquid interface for up to 3 wk. The keratinocyte plasma membrane localization of aquaporin-3 was confirmed at the electron microscope level in prickle cells. In addition an intracellular localization of aquaporin-3 was also detected in epidermis basal cells. Osmotically induced transepidermal water permeability was measured on stripped human skin and on reconstructed epidermis. Water transport across both stripped human skin and 2-3 wk reconstructed epidermis was comparable, inhibited by > 50% by 1 mM HgCl2 and fully inhibited by acid pH. By stopped-flow light scattering, keratinocyte plasma membranes, where aquaporin-3 is localized, exhibited a high, pH-sensitive, water permeability. Although human skin is highly impermeable to water, this is primarily accounted for by the stratum corneum, where a steep water content gradient was demonstrated. In contrast, the water content of viable strata of the epidermis is remarkably constant. Our results suggest that the human epidermis, below the stratum corneum, exhibits a high, aquaporin-3-mediated, water permeability. We propose that the role of aquaporin-3 is to water-clamp viable layers of the epidermis in order to improve the hydration of the epidermis below the stratum corneum.

    Original languageEnglish (US)
    Pages (from-to)678-685
    Number of pages8
    JournalJournal of Investigative Dermatology
    Volume118
    Issue number4
    DOIs
    StatePublished - Jan 1 2002

    Keywords

    • Aquaporin water channels
    • Human keratinocytes
    • Water permeability

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Dermatology
    • Cell Biology

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