In vivo studies of aquaporins 3 and 10 in human stratum corneum

Jakob Jungersted; Julie Bomholt; Niada Bajraktari; Jesper Søndergaard Hansen; Dan Arne Klærke; Per Amstrup Pedersen; Kristina Hedfalk; Kent Høier Nielsen; Tove Agner; Claus Hélix-Nielsen

doi:10.1007/s00403-013-1365-2

In vivo studies of aquaporins 3 and 10 in human stratum corneum

Jakob Jungersted, Julie Bomholt, Niada Bajraktari, Jesper Søndergaard Hansen, Dan Arne Klærke, Per Amstrup Pedersen, Kristina Hedfalk, Kent Høier Nielsen, Tove Agner, Claus Hélix-Nielsen

Molecular Integrative Physiology

18 Citations (Scopus)

Abstract

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.

Original language	English
Journal	Archives of Dermatological Research
Volume	305
Issue number	8
Pages (from-to)	699-704
Number of pages	6
ISSN	0340-3696
DOIs	https://doi.org/10.1007/s00403-013-1365-2
Publication status	Published - Oct 2013

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10.1007/s00403-013-1365-2

http://dx.doi.org/10.1007/s00403-013-1365-2

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@article{a2ff57c9e61b4b09ac14a0d333d64cfd,

title = "In vivo studies of aquaporins 3 and 10 in human stratum corneum",

abstract = "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.",

author = "Jakob Jungersted and Julie Bomholt and Niada Bajraktari and Hansen, {Jesper S{\o}ndergaard} and Kl{\ae}rke, {Dan Arne} and Pedersen, {Per Amstrup} and Kristina Hedfalk and Nielsen, {Kent H{\o}ier} and Tove Agner and Claus H{\'e}lix-Nielsen",

year = "2013",

month = oct,

doi = "10.1007/s00403-013-1365-2",

language = "English",

volume = "305",

pages = "699--704",

journal = "Archiv f{\"u}r Dermatologische Forschung",

issn = "0340-3696",

publisher = "Springer",

number = "8",

}

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 - 2013/10

Y1 - 2013/10

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

SN - 0340-3696

VL - 305

SP - 699

EP - 704

JO - Archiv für Dermatologische Forschung

JF - Archiv für Dermatologische Forschung

IS - 8

ER -