In vivo studies of aquaporins 3 and 10 in human stratum corneum
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In vivo studies of aquaporins 3 and 10 in human stratum corneum. / Jungersted, Jakob; Bomholt, Julie; Bajraktari, Niada; Hansen, Jesper Søndergaard; Klærke, Dan Arne; Pedersen, Per Amstrup; Hedfalk, Kristina; Nielsen, Kent Høier; Agner, Tove; Hélix-Nielsen, Claus.
In: Archives of Dermatological Research, Vol. 305, No. 8, 2013, p. 699-704.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - In vivo studies of aquaporins 3 and 10 in human stratum corneum
AU - Jungersted, Jakob
AU - Bomholt, Julie
AU - Bajraktari, Niada
AU - Hansen, Jesper Søndergaard
AU - Klærke, Dan Arne
AU - Pedersen, Per Amstrup
AU - Hedfalk, Kristina
AU - Nielsen, Kent Høier
AU - Agner, Tove
AU - Hélix-Nielsen, Claus
PY - 2013
Y1 - 2013
N2 - Aquaporins (AQPs) constitute one family of transmembrane proteins facilitating transport of water across cell membranes. Due to their specificity, AQPs have a broad spectrum of physiological functions, and for keratinocytes there are indications that these channel proteins are involved in cell migration and proliferation with consequences for the antimicrobial defense of the skin. AQP3 and AQP10 are aqua-glyceroporins, known to transport glycerol as well as water. AQP3 is the predominant AQP in human skin and has previously been demonstrated in the basal layer of epidermis in normal human skin, but not in stratum corneum (SC). AQP10 has not previously been identified in human skin. Previous studies have demonstrated the presence of AQP3 and AQP10 mRNA in keratinocytes. In this study, our aim was to investigate if these aquaporin proteins were actually present in human SC cells. This can be seen as a first step toward elucidating the possible functional role of AQP3 and AQP10 in SC hydration. Specifically we investigate the presence of AQP3 and AQP10 in vivo in human SC using "minimal-invasive" technique for obtaining SC samples. SC samples were obtained from six healthy volunteers. Western blotting and immunohistochemistry were used to demonstrate the presence of AQP3 as well as AQP10. The presence of AQP3 and AQP10 was verified by Western blotting, allowing for detection of proteins by specific antibodies. Applying immunohistochemistry, cell-like structures in the shape of corneocytes were identified in all samples by AQP3 and AQP10 antibodies. In conclusion, identification of AQP3 and AQP10 protein in SC in an in vivo model is new. Together with the new "minimal-invasive" method for SC collection presented, this opens for new possibilities to study the role of AQPs in relation to function of the skin barrier.
AB - Aquaporins (AQPs) constitute one family of transmembrane proteins facilitating transport of water across cell membranes. Due to their specificity, AQPs have a broad spectrum of physiological functions, and for keratinocytes there are indications that these channel proteins are involved in cell migration and proliferation with consequences for the antimicrobial defense of the skin. AQP3 and AQP10 are aqua-glyceroporins, known to transport glycerol as well as water. AQP3 is the predominant AQP in human skin and has previously been demonstrated in the basal layer of epidermis in normal human skin, but not in stratum corneum (SC). AQP10 has not previously been identified in human skin. Previous studies have demonstrated the presence of AQP3 and AQP10 mRNA in keratinocytes. In this study, our aim was to investigate if these aquaporin proteins were actually present in human SC cells. This can be seen as a first step toward elucidating the possible functional role of AQP3 and AQP10 in SC hydration. Specifically we investigate the presence of AQP3 and AQP10 in vivo in human SC using "minimal-invasive" technique for obtaining SC samples. SC samples were obtained from six healthy volunteers. Western blotting and immunohistochemistry were used to demonstrate the presence of AQP3 as well as AQP10. The presence of AQP3 and AQP10 was verified by Western blotting, allowing for detection of proteins by specific antibodies. Applying immunohistochemistry, cell-like structures in the shape of corneocytes were identified in all samples by AQP3 and AQP10 antibodies. In conclusion, identification of AQP3 and AQP10 protein in SC in an in vivo model is new. Together with the new "minimal-invasive" method for SC collection presented, this opens for new possibilities to study the role of AQPs in relation to function of the skin barrier.
U2 - 10.1007/s00403-013-1365-2
DO - 10.1007/s00403-013-1365-2
M3 - Journal article
C2 - 23677388
VL - 305
SP - 699
EP - 704
JO - Archiv für Dermatologische Forschung
JF - Archiv für Dermatologische Forschung
SN - 0340-3696
IS - 8
ER -
ID: 45809497