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Aquaporins

BL

This post started as a continuation on a previous post on clearing aluminum using silica. The question was asked as how silica is transported in our bodies. The answer is by aquaporins. Silicates can induce the exression these aquaporins. If alumina can traverse these channels, is this a way for alumina to get out of intracellular places? The other question that needs to be answered is if alumina is associated with oxygen, bound to thiols, or what? Some of these references hint that any alumina silicates that are formed might interact with these multipurpose channels. Reference [1] is one of many warnings that silicates are irritants even if they might bump up the expression of aquaporins.

An excellent Aquaporin review [2]

Aquaporins are found in all major domains of life on this planet from bacteria to plants, and animals. [2] They are multi purpose transporters for urea, glycerol, H2O2, and metaloid oxides. [2] The corresponding author of this review was emailed and asked if aquaporins can transport alumina.

Can auaporins transport alumina? Dr Barry Rosen was contacted. Dr Rosen thought it might be possible with teh caviate that his professional expertise and chemistry knowledge was with As(OH)3, areseic.
Good luck, Barry Rosen”

Periodic table of metalloidsThe hydroxyacids of lower oxidation state metalloid species (B(III), Si(IV), Ge(IV), As(III) and Sb(III)) are substrates of aquaglyceroporin (AQP) channels in bacteria, protozoans, fungi, plants and animals. Like glycerol, they are uncharged polar molecules with volumes small enough to fit through the approximately 5 Å diameter opening of the channel. Shown is a composite bacterial-yeast-mammalian cell with As(OH)3 entering via the E. coli GlpF AQP (the structure is PDB 1LDA). Inside the cell, the metalloid reacts with three GSH molecules to form the major cytosolic species, As(GS)3. This molecule is detoxified by removal from the cytosol. In fungi and plants, As(GS)3 (or other thiol derivatives such as phytochelatin conjugates) are pumped into the vacuole by ABC transporters such as the yeast Ycf1, or, in animals, into bile or blood by related MRP pumps. As(GS)3 can also be detoxified by methylation catalyzed by As(III) S-adenosylmethionine methyltransferases (AS3MT in animals, ArsM in microbes). The product of the first round of methylation, CH3As(GS)2 is a substrate of MRPs, and, after hydrolysis to CH3As(OH)2, is a substrate of AQPs.

References

  1. Hao X, Wang H, Liu W, Liu S, Peng Z, Sun Y, Zhao J, Jiang Q, Liu H. Enhanced expression levels of aquaporin-1 and aquaporin-4 in A549 cells exposed to silicon dioxide. Mol Med Rep. 2016 Sep;14(3):2101-6. PMC free article
  2. Mukhopadhyay R, Bhattacharjee H, Rosen BP. Aquaglyceroporins: generalized metalloid channels. Biochim Biophys Acta. 2014 May;1840(5):1583-91. PMC free article

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