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Published on: June 21, 2013
Histamine downregulates aquaporin 5 in human nasal epithelial cells
Weiwei Wang1, Xiaolian Wang, Lan Ma
1Department of Anatomy, Schools of Medicine and Nursing Sciences, Huzhou University, China.
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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