Adaptable interaction between aquaporin-1 and band 3 reveals a potential role of water channel in blood CO2 transport

Kate Hsu, Ting Ying Lee, Ammasi Periasamy, Fu Jen Kao, Li Tzu Li, Chuang Yu Lin, Hui Ju Lin, Marie Lin

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

Human CO2 respiration requires rapid conversion between CO2 and HCO32. Carbonic anhydrase II facilitates this reversible reaction inside red blood cells, and band 3 [anion exchanger 1 (AE1)] provides a passage for HCO32 flux across the cell membrane. These 2 proteins are core components of the CO2 transport metabolon. Intracellular H2O is necessary for CO2/HCO32 conversion. However, abundantly expressed aquaporin 1 (AQP1) in erythrocytes is thought not to be part of band 3 complexes or the CO2 transport metabolon. To solve this conundrum, we used Förster resonance energy transfer (FRET) measured by fluorescence lifetime imaging (FLIM-FRET) and identified interaction between aquaporin-1 and band 3 at a distance of 8 nm, within the range of dipole–dipole interaction. Notably, their interaction was adaptable to membrane tonicity changes. This suggests that the function of AQP1 in tonicity response could be coupled or correlated to its function in band 3-mediated CO2/HCO32 exchange. By demonstrating AQP1 as a mobile component of the CO2 transport metabolon, our results uncover a potential role of water channel in blood CO2 transport and respiration.

Original languageEnglish
Pages (from-to)4256-4264
Number of pages9
JournalFASEB Journal
Volume31
Issue number10
DOIs
StatePublished - Oct 2017

Keywords

  • Anion exchanger-1
  • Erythrocyte
  • FLIM-FRET
  • Miltenberger subtype III

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