ArticleFEBS open bio2014
Analysis of aquaporin 9 expression in human epidermis and cultured keratinocytes.
Article in FEBS open bio, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Review
- Aquaporins in Allergic Response: A New Player.Clinical reviews in allergy & immunology · 2025Review
- Exploring the Shared Diagnostic Genes in IBD and Psoriasis through Bioinformatics and Experimental Assays.International journal of medical sciences · 2025Article
- Role of aquaporins in brain water transport and edema.Frontiers in neuroscience · 2025Review
- Review
- Integration of machine learning to identify diagnostic genes in leukocytes for acute myocardial infarction patients.Journal of translational medicine · 2023Article
- Aquaporins in Skin.Advances in experimental medicine and biology · 2023Article
- The Multifaceted Role of Aquaporin-9 in Health and Its Potential as a Clinical Biomarker.Biomolecules · 2022Review
- Aquaporins Are One of the Critical Factors in the Disruption of the Skin Barrier in Inflammatory Skin Diseases.International journal of molecular sciences · 2022Review
- Article
- N-Acetylglutaminoyl-S-farnesyl-L-cysteine (SIG-1191): an anti-inflammatory molecule that increases the expression of the aquaglyceroporin, aquaporin-3, in human keratinocytes.Archives of dermatological research · 2017Article
- A Systematic Characterization of Aquaporin-9 Expression in Human Normal and Pathological Tissues.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aquaporin 9 (AQP9) is a member of the aquaglyceroporin family that transports glycerol, urea and other small solutes as well as water. Compared to the expression and function in epidermal keratinocytes of AQP3, another aquaglyceroporin, our knowledge of epidermal AQP9 remains elusive. In this study, we investigated the expression of AQP9 in the human epidermis and cultured keratinocytes. Immunofluorescence studies revealed that AQP9 expression is highly restricted to the stratum granulosum of the human epidermis, where occludin is also expressed at the tight junctions. Interestingly, the AQP3 staining decreased sharply below the cell layers in which AQP9 is expressed. In cultured normal human epidermal keratinocytes (NHEK), knock-down of AQP9 expression in the differentiated cells induced by RNA interference reduced glycerol uptake, which was not as pronounced as was the case with AQP3 knock-down cells. In contrast, similar reduction of urea uptake was detected in AQP9 and AQP3 knock-down cells. These findings suggested that AQP9 expression in NHEK facilitates at least the transport of glycerol and urea. Finally, we analyzed the effect of retinoic acid (RA), a potent stimulator of keratinocyte proliferation, on AQP3 and AQP9 mRNA expression in differentiated NHEK. Stimulation with RA at 1 μM for 24 h augmented AQP3 expression and down-regulated AQP9 expression. Collectively, these results indicate that AQP9 expression in epidermal keratinocytes is regulated in a different manner from that of AQP3.
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Registered trials
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