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Aquaporin-8-facilitated mitochondrial ammonia transport
- Source :
- Biochemical and biophysical research communications, 393 (2010): 217–221. doi:10.1016/j.bbrc.2010.01.104, info:cnr-pdr/source/autori:Soria LR, Fanelli E, Altamura N, Svelto M, Marinelli RA, Calamita G. Altamura N, Svelto M, Marinelli RA, Calamita G./titolo:Aquaporin-8-facilitated mitochondrial ammonia transport./doi:10.1016%2Fj.bbrc.2010.01.104/rivista:Biochemical and biophysical research communications (Print)/anno:2010/pagina_da:217/pagina_a:221/intervallo_pagine:217–221/volume:393
- Publication Year :
- 2010
-
Abstract
- Aquaporin-8 (AQP8) is a membrane channel permeable to water and ammonia. As AQP8 is expressed in the inner mitochondrial membrane of several mammalian tissues, we studied the effect of the AQP8 expression on the mitochondrial transport of ammonia. Recombinant rat AQP8 was expressed in the yeast Saccharomyces cerevisiae. The presence of AQP8 in the inner membrane of yeast mitochondria was demonstrated by subcellular fractionation and immunoblotting analysis. The ammonia transport was determined in isolated mitochondria by stopped flow light scattering using formamide as ammonia analog. We found that the presence of AQP8 increased by threefold mitochondrial formamide transport. AQP8-facilitated mitochondrial formamide transport in rat native tissue was confirmed in liver (a mitochondrial AQP8-expressing tissue) vs. brain (a mitochondrial AQP8 non-expressing tissue). Comparative studies indicated that the AQP8-mediated mitochondrial movement of formamide was markedly higher than that of water. Together, our data suggest that ammonia diffusional transport is a major function for mitochondrial AQP8.
- Subjects :
- Biophysics
Aquaporin
Mitochondria, Liver
Saccharomyces cerevisiae
Mitochondrion
Aquaporins
Biochemistry
Mitochondrial membrane transport protein
Ammonia
Yeast expression system
Inner mitochondrial membrane
Inner membrane
Animals
Molecular Biology
Mitochondrial transport
biology
Formamides
Brain
Water
Aqua-ammoniaporin
Biological Transport
Cell Biology
Mitochondrial carrier
Recombinant Proteins
Mitochondria
Rats
Liver
biology.protein
ATP–ADP translocase
Ammonia transport
Subjects
Details
- ISSN :
- 10902104
- Volume :
- 393
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Biochemical and biophysical research communications
- Accession number :
- edsair.doi.dedup.....6a67f9e3fcf7e3620c70a8bee4ca6ed8
- Full Text :
- https://doi.org/10.1016/j.bbrc.2010.01.104