Adaptable interaction between aquaporin-1 and band 3 reveals a potential role of water channel in blood CO2 transport. 2017

Kate Hsu, and Ting-Ying Lee, and Ammasi Periasamy, and Fu-Jen Kao, and Li-Tzu Li, and Chuang-Yu Lin, and Hui-Ju Lin, and Marie Lin
Transfusion Medicine Laboratory, Mackay Memorial Hospital, Tamsui, Taiwan; khsu1@mmh.org.tw.

Human CO2 respiration requires rapid conversion between CO2 and HCO3- Carbonic anhydrase II facilitates this reversible reaction inside red blood cells, and band 3 [anion exchanger 1 (AE1)] provides a passage for HCO3- flux across the cell membrane. These 2 proteins are core components of the CO2 transport metabolon. Intracellular H2O is necessary for CO2/HCO3- 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/HCO3- 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.-Hsu, K., Lee, T.-Y., Periasamy, A., Kao, F.-J., Li, L.-T., Lin, C.-Y., Lin, H.-J., Lin, M. Adaptable interaction between aquaporin-1 and band 3 reveals a potential role of water channel in blood CO2 transport.

UI MeSH Term Description Entries
D002245 Carbon Dioxide A colorless, odorless gas that can be formed by the body and is necessary for the respiration cycle of plants and animals. Carbonic Anhydride,Anhydride, Carbonic,Dioxide, Carbon
D002463 Cell Membrane Permeability A quality of cell membranes which permits the passage of solvents and solutes into and out of cells. Permeability, Cell Membrane
D004910 Erythrocyte Membrane The semi-permeable outer structure of a red blood cell. It is known as a red cell 'ghost' after HEMOLYSIS. Erythrocyte Ghost,Red Cell Cytoskeleton,Red Cell Ghost,Erythrocyte Cytoskeleton,Cytoskeleton, Erythrocyte,Cytoskeleton, Red Cell,Erythrocyte Cytoskeletons,Erythrocyte Ghosts,Erythrocyte Membranes,Ghost, Erythrocyte,Ghost, Red Cell,Membrane, Erythrocyte,Red Cell Cytoskeletons,Red Cell Ghosts
D004912 Erythrocytes Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN. Blood Cells, Red,Blood Corpuscles, Red,Red Blood Cells,Red Blood Corpuscles,Blood Cell, Red,Blood Corpuscle, Red,Erythrocyte,Red Blood Cell,Red Blood Corpuscle
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D006863 Hydrogen-Ion Concentration The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations
D001457 Anion Exchange Protein 1, Erythrocyte A major integral transmembrane protein of the ERYTHROCYTE MEMBRANE. It is the anion exchanger responsible for electroneutral transporting in CHLORIDE IONS in exchange of BICARBONATE IONS allowing CO2 uptake and transport from tissues to lungs by the red blood cells. Genetic mutations that result in a loss of the protein function have been associated with type 4 HEREDITARY SPHEROCYTOSIS. Anion Transport Protein, Erythrocyte,Band 3 Protein,Erythrocyte Anion Transport Protein,Erythrocyte Membrane Band 3 Protein,AE1 Anion Exchanger,AE1 Chloride-Bicarbonate Exchanger,AE1 Cl- HCO3- Exchanger,AE1 Gene Product,Anion Exchanger 1,Antigens, CD233,Band 3 Anion Transport Protein,Band III Protein,CD233 Antigen,CD233 Antigens,Capnophorin,EPB3 Protein,Erythrocyte Anion Exchanger,Erythrocyte Membrane Anion Transport Protein,Erythrocyte Membrane Protein Band 3, Diego Blood Group,Protein Band 3,SLC4A1 Protein,Solute Carrier Family 4 Member 1,Solute Carrier Family 4, Anion Exchanger, Member 1,AE1 Chloride Bicarbonate Exchanger,AE1 Cl HCO3 Exchanger,Anion Exchanger, Erythrocyte,Antigen, CD233,Chloride-Bicarbonate Exchanger, AE1,Exchanger 1, Anion,Protein, EPB3
D001692 Biological Transport The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments. Transport, Biological,Biologic Transport,Transport, Biologic
D051398 Aquaporin 1 Aquaporin 1 forms a water-specific channel that is constitutively expressed at the PLASMA MEMBRANE of ERYTHROCYTES and KIDNEY TUBULES, PROXIMAL. It provides these cells with a high permeability to WATER. In humans polymorphisms of this protein result in the Colton blood group antigen. AQP-CHIP Protein,AQP1 Protein,Aquaporin 1 Protein,Aquaporin-CHIP,CHIP28 Protein,Channel-Forming Integral Membrane Protein Of 28 kDa,AQP CHIP Protein,Aquaporin CHIP,Channel Forming Integral Membrane Protein Of 28 kDa

Related Publications

Kate Hsu, and Ting-Ying Lee, and Ammasi Periasamy, and Fu-Jen Kao, and Li-Tzu Li, and Chuang-Yu Lin, and Hui-Ju Lin, and Marie Lin
January 2018, Frontiers in physiology,
Kate Hsu, and Ting-Ying Lee, and Ammasi Periasamy, and Fu-Jen Kao, and Li-Tzu Li, and Chuang-Yu Lin, and Hui-Ju Lin, and Marie Lin
December 1998, The Journal of biological chemistry,
Kate Hsu, and Ting-Ying Lee, and Ammasi Periasamy, and Fu-Jen Kao, and Li-Tzu Li, and Chuang-Yu Lin, and Hui-Ju Lin, and Marie Lin
March 2004, The Journal of biological chemistry,
Kate Hsu, and Ting-Ying Lee, and Ammasi Periasamy, and Fu-Jen Kao, and Li-Tzu Li, and Chuang-Yu Lin, and Hui-Ju Lin, and Marie Lin
April 1998, Biochemical and biophysical research communications,
Kate Hsu, and Ting-Ying Lee, and Ammasi Periasamy, and Fu-Jen Kao, and Li-Tzu Li, and Chuang-Yu Lin, and Hui-Ju Lin, and Marie Lin
January 2014, Sub-cellular biochemistry,
Kate Hsu, and Ting-Ying Lee, and Ammasi Periasamy, and Fu-Jen Kao, and Li-Tzu Li, and Chuang-Yu Lin, and Hui-Ju Lin, and Marie Lin
December 1984, Biochimica et biophysica acta,
Kate Hsu, and Ting-Ying Lee, and Ammasi Periasamy, and Fu-Jen Kao, and Li-Tzu Li, and Chuang-Yu Lin, and Hui-Ju Lin, and Marie Lin
August 2006, Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association,
Kate Hsu, and Ting-Ying Lee, and Ammasi Periasamy, and Fu-Jen Kao, and Li-Tzu Li, and Chuang-Yu Lin, and Hui-Ju Lin, and Marie Lin
May 2012, Nihon yakurigaku zasshi. Folia pharmacologica Japonica,
Kate Hsu, and Ting-Ying Lee, and Ammasi Periasamy, and Fu-Jen Kao, and Li-Tzu Li, and Chuang-Yu Lin, and Hui-Ju Lin, and Marie Lin
February 1998, The American journal of physiology,
Kate Hsu, and Ting-Ying Lee, and Ammasi Periasamy, and Fu-Jen Kao, and Li-Tzu Li, and Chuang-Yu Lin, and Hui-Ju Lin, and Marie Lin
January 1997, Journal of the American Society of Nephrology : JASN,
Copied contents to your clipboard!