American Journal of Rhinology and Allergy · 2015 · 13 citations · 23 references
Life SciencesBiochemistryMolecular BiologyCell SignalingGene ExpressionSignal TransductionCyclic Nucleotide SignalingIon Channel ExpressionIon ChannelsNasal PhysiologyAquaporin RegulationAquaporin-mediated Water TransportAquaporinsCyclic Adenosine Monophosphate PathwayCyclic Adenosine Monophosphate SignalingHistamine-mediated SecretionNasal Secretion Physiology
BACKGROUND: Aquaporin 5 (AQP5) is a water-specific channel protein. It is thought to be a key participant in fluid secretion and a rate-limiting barrier to the secretion seen during allergic inflammation. We sought to determine the effect of histamine on AQP5 expression in human nasal epithelial cells (HNEpC). METHODS: HNEpC cells were cultured with four concentrations of histamine in vitro. The phosphorylation of cyclic adenosine monophosphate-responsive element binding protein (CREB) at serine 133 and the AQP5 protein were measured by using immunocytochemistry and Western blotting. Real-time polymerase chain reaction was used to detect AQP5 messenger ribonucleic acid (mRNA). RESULTS: Concentration-dependent histamine induced-inhibition of CREB phosphorylation at serine 133 in HNEpC cells was observed, and AQP5 mRNA and protein were also downregulated in a concentration-dependent fashion. CONCLUSION: Histamine downregulates AQP5 production in HNEpC cells by inhibiting CREB phosphorylation at serine 133.
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Fluorescence ratio imaging of cyclic AMP in single cells
Stephen Adams, A. Harootunian, Ying J. Buechler et al. · Nature · 1991 · 698 citations
Carissa M. Krane, James E. Melvin, Ha‐Van Nguyen et al. · Journal of Biological Chemistry · 2001 · 314 citations · Full text