Abstract
Aquaporin-11 (AQP11) is an intracellular aquaporin expressed in various tissues, including brain tissues in mammals. While AQP11-deficient mice have developed fatal polycystic kidneys at one month old, the role of AQP11 in the brain was not well appreciated. In this study, we examined the AQP11 expression in the mouse brain and the brain phenotype of AQP11-deficient mice. AQP11 messenger ribonucleic acid (mRNA) and protein were expressed in the brain, but much less than in the thymus and kidney. Immunostaining showed that AQP11 was localized at the epithelium of the choroid plexus and at the endothelium of the brain capillary, suggesting that AQP11 may be involved in water transport at the choroid plexus and blood-brain barrier (BBB) in the brain. The expression of AQP4, another brain AQP expressed at the BBB, was decreased by half in AQP11-deficient mice, thereby suggesting the presence of the interaction between AQP11 and AQP4. The brain of AQP11-deficient mice, however, did not show any morphological abnormalities and the function of the BBB was intact. Our findings provide a novel insight into a water transport mechanism mediated by AQPs in the brain, which may lead to a new therapy for brain edema.
Highlights
Aquaporins (AQPs) are a family of transmembrane proteins transporting water and small solutes
The third subfamily is a superaquaporin (SAQP) whose NPA boxes are distantly related to other AQPs
AQP4 is expressed at astrocyte endfeet to regulate water transport to the brain parenchyma, as its absence has ameliorated brain edema induced by brain infarction [11] and exacerbated the recovery of brain edema caused by vascular inflammation [12]
Summary
Aquaporins (AQPs) are a family of transmembrane proteins transporting water and small solutes (reviewed in [1,2,3,4]). There are 13 members of AQPs in mammals (AQP0-12), which have specific tissue expression patterns to regulate water and/or solute transports in various organs. Their physiological and pathological importance has not yet been fully clarified even after the analysis of AQP deficient mice and humans [6]. The second subfamily, an aquaglyceroporin (AQGP), transports glycerol as well as water, such as AQP3. Includes AQP11 and AQP12, which are localized inside the cell, thereby making their functional. HoweTvheer,pfuurrpthoesresotuf dthieiss shtauvdeynwotaysettobleoecnaldizoenAe QsinPc1e1 tihnetnh.e mouse brain to correlate with a neural phenTohtyeppeuorfpAosQePo1f1t-hdiesfsictuiednyt mwiacse,towlhoiccahliwzeilAl gQivPe11aninintshieghmtoinutsoe tbhreairnolteoocfoArrQelPa1te winitthheabnreauinr.al phenotype of AQP11-deficient mice, which will give an insight into the role of AQP11 in the brain
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