Aquaporin-11: A channel protein lacking apparent transport function expressed in brain
Author Information
Author(s): Gorelick Daniel A, Praetorius Jeppe, Tsunenari Takashi, Nielsen Søren, Agre Peter
Primary Institution: Johns Hopkins University School of Medicine
Hypothesis
What is the tissue distribution of rat AQP11 and what solutes does it transport?
Conclusion
AQP11 is functionally distinct from other proteins of the aquaporin superfamily and could represent a new aquaporin subfamily.
Supporting Evidence
- AQP11 RNA and protein are found in multiple rat tissues, including kidney, liver, testes, and brain.
- AQP11 has a unique distribution in the brain, appearing in Purkinje cell dendrites and hippocampal neurons.
- Xenopus oocytes expressing AQP11 failed to transport water, glycerol, urea, or ions.
Takeaway
AQP11 is a protein found in the brain and other tissues, but it doesn't seem to help transport water or other substances like other aquaporins do.
Methodology
The study involved cloning, sequence analysis, Northern blotting, RT-PCR, and functional expression in Xenopus oocytes.
Limitations
The study did not quantitatively measure AQP11 mRNA levels, making it difficult to infer relative abundance.
Digital Object Identifier (DOI)
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