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Aquaporin-11: a channel protein lacking apparent transport function expressed in brain.

Authors: Gorelick, DA  Praetorius, J  Tsunenari, T  Nielsen, S  Agre, P 
Citation: Gorelick DA, etal., BMC Biochem. 2006 May 1;7:14.
Pubmed: (View Article at PubMed) PMID:16650285
DOI: Full-text: DOI:10.1186/1471-2091-7-14

BACKGROUND: The aquaporins are a family of integral membrane proteins composed of two subfamilies: the orthodox aquaporins, which transport only water, and the aquaglyceroporins, which transport glycerol, urea, or other small solutes. Two recently described aquaporins, numbers 11 and 12, appear to be more distantly related to the other mammalian aquaporins and aquaglyceroporins. RESULTS: We report on the characterization of Aquaporin-11 (AQP11). AQP11 RNA and protein is found in multiple rat tissues, including kidney, liver, testes and brain. AQP11 has a unique distribution in brain, appearing in Purkinje cell dendrites, hippocampal neurons of CA1 and CA2, and cerebral cortical neurons. Immunofluorescent staining of Purkinje cells indicates that AQP11 is intracellular. Unlike other aquaporins, Xenopus oocytes expressing AQP11 in the plasma membrane failed to transport water, glycerol, urea, or ions. CONCLUSION: AQP11 is functionally distinct from other proteins of the aquaporin superfamily and could represent a new aquaporin subfamily. Further studies are necessary to elucidate the role of AQP11 in the brain.

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RGD Object Information
RGD ID: 2292708
Created: 2008-05-05
Species: All species
Last Modified: 2008-05-05
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.