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Copper inhibits the water and glycerol permeability of aquaporin-3
Department of Woman and Child Health, Karolinska Institutet.ORCID iD: 0000-0003-3402-9672
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2004 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 279, no 50, 51939-51943 p.Article in journal (Refereed) Published
Abstract [en]

Aquaporin-3 (AQP3) is an aquaglyceroporin expressed in erythrocytes and several other tissues. Erythrocytes are, together with kidney and liver, the main targets for copper toxicity. Here we report that both water and glycerol permeability of human AQP3 is inhibited by copper. Inhibition is fast, dose-dependent, and reversible. If copper is dissolved in carbonic acid-bicarbonate buffer, the natural buffer system in our body, doses in the range of those observed in Wilson disease and in copper poisoning caused significant inhibition. AQP7, another aquaglyceroporin, was insensitive to copper. Three extracellular amino acid residues, Trp128, Ser152, and His241, were identified as responsible for the effect of copper on AQP3. We have previously shown that Ser152 is involved in regulation of AQP3 by pH. The fact that Ser152 mediates regulation of AQP3 by copper may explain the phenomenon of exquisite sensitivity of human erythrocytes to copper at acidic pH. When AQP3 was co-expressed with another AQP, only glycerol but not water permeability was inhibited by copper. Our results provide a better understanding of processes that occur in severe copper metabolism defects such as Wilson disease and in copper poisoning.

Place, publisher, year, edition, pages
2004. Vol. 279, no 50, 51939-51943 p.
National Category
Cell Biology
URN: urn:nbn:se:kth:diva-80468DOI: 10.1074/jbc.M407645200ISI: 000225493400028PubMedID: 15456785OAI: diva2:496367
QC 20120302Available from: 2012-02-09 Created: 2012-02-09 Last updated: 2012-03-02Bibliographically approved

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Zelenina, Marina
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