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Jørgen Frøkiær

Functional requirement of aquaporin-5 in plasma membranes of sweat glands

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Standard

Functional requirement of aquaporin-5 in plasma membranes of sweat glands. / Nejsum, Lene Niemann; Kwon, Tae-Hwan; Jensen, Uffe B; Fumagalli, Ornella; Frøkiaer, Jørgen; Krane, Carissa M; Menon, Anil G; King, Landon S; Agre, Peter C; Nielsen, Søren.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 99, No. 1, 08.01.2002, p. 511-6.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Nejsum, LN, Kwon, T-H, Jensen, UB, Fumagalli, O, Frøkiaer, J, Krane, CM, Menon, AG, King, LS, Agre, PC & Nielsen, S 2002, 'Functional requirement of aquaporin-5 in plasma membranes of sweat glands', Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 1, pp. 511-6. https://doi.org/10.1073/pnas.012588099

APA

Nejsum, L. N., Kwon, T-H., Jensen, U. B., Fumagalli, O., Frøkiaer, J., Krane, C. M., Menon, A. G., King, L. S., Agre, P. C., & Nielsen, S. (2002). Functional requirement of aquaporin-5 in plasma membranes of sweat glands. Proceedings of the National Academy of Sciences of the United States of America, 99(1), 511-6. https://doi.org/10.1073/pnas.012588099

CBE

Nejsum LN, Kwon T-H, Jensen UB, Fumagalli O, Frøkiaer J, Krane CM, Menon AG, King LS, Agre PC, Nielsen S. 2002. Functional requirement of aquaporin-5 in plasma membranes of sweat glands. Proceedings of the National Academy of Sciences of the United States of America. 99(1):511-6. https://doi.org/10.1073/pnas.012588099

MLA

Nejsum, Lene Niemann et al. "Functional requirement of aquaporin-5 in plasma membranes of sweat glands". Proceedings of the National Academy of Sciences of the United States of America. 2002, 99(1). 511-6. https://doi.org/10.1073/pnas.012588099

Vancouver

Nejsum LN, Kwon T-H, Jensen UB, Fumagalli O, Frøkiaer J, Krane CM et al. Functional requirement of aquaporin-5 in plasma membranes of sweat glands. Proceedings of the National Academy of Sciences of the United States of America. 2002 Jan 8;99(1):511-6. https://doi.org/10.1073/pnas.012588099

Author

Nejsum, Lene Niemann ; Kwon, Tae-Hwan ; Jensen, Uffe B ; Fumagalli, Ornella ; Frøkiaer, Jørgen ; Krane, Carissa M ; Menon, Anil G ; King, Landon S ; Agre, Peter C ; Nielsen, Søren. / Functional requirement of aquaporin-5 in plasma membranes of sweat glands. In: Proceedings of the National Academy of Sciences of the United States of America. 2002 ; Vol. 99, No. 1. pp. 511-6.

Bibtex

@article{b3976f0df77643858cf9dec2dfef8181,
title = "Functional requirement of aquaporin-5 in plasma membranes of sweat glands",
abstract = "The distribution and function of aquaporins (AQPs) have not previously been defined in sweat glands. In this study, AQP1, AQP3, and AQP5 mRNA were demonstrated in rat paw by reverse transcription (RT)-PCR, but AQP2 and AQP4 were not. AQP1, AQP3, and AQP5 protein were confirmed in these tissues by immunoblotting. AQP1 was identified in capillary endothelial cells by immunohistochemical labeling, but not in sweat glands or epidermis. Abundant AQP3 expression was seen in basal levels of epidermis, but not in sweat glands. AQP2 and AQP4 were not observed in either skin or sweat glands. Immunohistochemical labeling revealed abundant AQP5 in secretory parts of rat and mouse sweat glands, where immunoelectron microscopy demonstrated abundant AQP5 labeling in the apical plasma membrane. AQP5 immunolabeling of human sweat glands yielded a similar pattern. To establish the role of AQP5 in sweat secretion, we tested the response of adult mice to s.c. injection of pilocarpine, as visualized by reaction of secreted amylase with iodine/starch. The number of active sweat glands was dramatically reduced in AQP5-null (-/-) mice compared with heterozygous (+/-) and wild-type (+/+) mice. We conclude that the presence of AQP5 in plasma membranes of sweat glands is essential for secretion, providing potential insight into mechanisms underlying mammalian thermoregulation, tactile sensitivity, and the pathophysiology of hyperhidrosis.",
keywords = "Animals, Aquaporin 2, Aquaporin 3, Aquaporin 4, Aquaporin 5, Aquaporin 6, Aquaporins, Cell Membrane, Heterozygote, Immunoblotting, Immunohistochemistry, Kidney, Lung, Membrane Proteins, Mice, Mice, Transgenic, Microscopy, Immunoelectron, Muscarinic Agonists, Pilocarpine, RNA, Messenger, Rats, Rats, Wistar, Reverse Transcriptase Polymerase Chain Reaction, Skin, Subcellular Fractions, Sweat Glands, Water",
author = "Nejsum, {Lene Niemann} and Tae-Hwan Kwon and Jensen, {Uffe B} and Ornella Fumagalli and J{\o}rgen Fr{\o}kiaer and Krane, {Carissa M} and Menon, {Anil G} and King, {Landon S} and Agre, {Peter C} and S{\o}ren Nielsen",
year = "2002",
month = jan,
day = "8",
doi = "10.1073/pnas.012588099",
language = "English",
volume = "99",
pages = "511--6",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "1",

}

RIS

TY - JOUR

T1 - Functional requirement of aquaporin-5 in plasma membranes of sweat glands

AU - Nejsum, Lene Niemann

AU - Kwon, Tae-Hwan

AU - Jensen, Uffe B

AU - Fumagalli, Ornella

AU - Frøkiaer, Jørgen

AU - Krane, Carissa M

AU - Menon, Anil G

AU - King, Landon S

AU - Agre, Peter C

AU - Nielsen, Søren

PY - 2002/1/8

Y1 - 2002/1/8

N2 - The distribution and function of aquaporins (AQPs) have not previously been defined in sweat glands. In this study, AQP1, AQP3, and AQP5 mRNA were demonstrated in rat paw by reverse transcription (RT)-PCR, but AQP2 and AQP4 were not. AQP1, AQP3, and AQP5 protein were confirmed in these tissues by immunoblotting. AQP1 was identified in capillary endothelial cells by immunohistochemical labeling, but not in sweat glands or epidermis. Abundant AQP3 expression was seen in basal levels of epidermis, but not in sweat glands. AQP2 and AQP4 were not observed in either skin or sweat glands. Immunohistochemical labeling revealed abundant AQP5 in secretory parts of rat and mouse sweat glands, where immunoelectron microscopy demonstrated abundant AQP5 labeling in the apical plasma membrane. AQP5 immunolabeling of human sweat glands yielded a similar pattern. To establish the role of AQP5 in sweat secretion, we tested the response of adult mice to s.c. injection of pilocarpine, as visualized by reaction of secreted amylase with iodine/starch. The number of active sweat glands was dramatically reduced in AQP5-null (-/-) mice compared with heterozygous (+/-) and wild-type (+/+) mice. We conclude that the presence of AQP5 in plasma membranes of sweat glands is essential for secretion, providing potential insight into mechanisms underlying mammalian thermoregulation, tactile sensitivity, and the pathophysiology of hyperhidrosis.

AB - The distribution and function of aquaporins (AQPs) have not previously been defined in sweat glands. In this study, AQP1, AQP3, and AQP5 mRNA were demonstrated in rat paw by reverse transcription (RT)-PCR, but AQP2 and AQP4 were not. AQP1, AQP3, and AQP5 protein were confirmed in these tissues by immunoblotting. AQP1 was identified in capillary endothelial cells by immunohistochemical labeling, but not in sweat glands or epidermis. Abundant AQP3 expression was seen in basal levels of epidermis, but not in sweat glands. AQP2 and AQP4 were not observed in either skin or sweat glands. Immunohistochemical labeling revealed abundant AQP5 in secretory parts of rat and mouse sweat glands, where immunoelectron microscopy demonstrated abundant AQP5 labeling in the apical plasma membrane. AQP5 immunolabeling of human sweat glands yielded a similar pattern. To establish the role of AQP5 in sweat secretion, we tested the response of adult mice to s.c. injection of pilocarpine, as visualized by reaction of secreted amylase with iodine/starch. The number of active sweat glands was dramatically reduced in AQP5-null (-/-) mice compared with heterozygous (+/-) and wild-type (+/+) mice. We conclude that the presence of AQP5 in plasma membranes of sweat glands is essential for secretion, providing potential insight into mechanisms underlying mammalian thermoregulation, tactile sensitivity, and the pathophysiology of hyperhidrosis.

KW - Animals

KW - Aquaporin 2

KW - Aquaporin 3

KW - Aquaporin 4

KW - Aquaporin 5

KW - Aquaporin 6

KW - Aquaporins

KW - Cell Membrane

KW - Heterozygote

KW - Immunoblotting

KW - Immunohistochemistry

KW - Kidney

KW - Lung

KW - Membrane Proteins

KW - Mice

KW - Mice, Transgenic

KW - Microscopy, Immunoelectron

KW - Muscarinic Agonists

KW - Pilocarpine

KW - RNA, Messenger

KW - Rats

KW - Rats, Wistar

KW - Reverse Transcriptase Polymerase Chain Reaction

KW - Skin

KW - Subcellular Fractions

KW - Sweat Glands

KW - Water

U2 - 10.1073/pnas.012588099

DO - 10.1073/pnas.012588099

M3 - Journal article

C2 - 11773623

VL - 99

SP - 511

EP - 516

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 1

ER -