Adaptable interaction between aquaporin‐1 and band 3 reveals a potential role of water channel in blood CO2 transport
ABSTRACT 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...
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| creator | Hsu, Kate Lee, Ting‐Ying Periasamy, Ammasi Kao, Fu‐Jen Li, Li‐Tzu Lin, Chuang‐Yu Lin, Hui‐Ju Lin, Marie |
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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. FASEB J. 31, 4256–4264 (2017). www.fasebj.org |
| doi_str_mv | 10.1096/fj.201601282R |
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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. FASEB J. 31, 4256–4264 (2017). www.fasebj.org</description><identifier>ISSN: 0892-6638</identifier><identifier>EISSN: 1530-6860</identifier><identifier>DOI: 10.1096/fj.201601282R</identifier><identifier>PMID: 28596233</identifier><language>eng</language><publisher>Bethesda: Federation of American Societies for Experimental Biology</publisher><subject>anion exchanger‐1 ; Anion exchanging ; Aquaporin 1 ; Aquaporins ; Carbon dioxide ; Carbonic anhydrase ; Carbonic anhydrase II ; Conversion ; Dipoles ; Energy measurement ; Energy transfer ; erythrocyte ; Erythrocytes ; FLIM‐FRET ; Fluorescence ; Fluorescence resonance energy transfer ; Miltenberger subtype III ; Proteins ; Respiration ; Transport</subject><ispartof>The FASEB journal, 2017-10, Vol.31 (10), p.4256-4264</ispartof><rights>FASEB</rights><rights>Copyright Federation of American Societies for Experimental Biology (FASEB) Oct 2017</rights><rights>FASEB 2017 FASEB</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1096%2Ffj.201601282R$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1096%2Ffj.201601282R$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,314,780,784,885,1417,27924,27925,45574,45575</link.rule.ids></links><search><creatorcontrib>Hsu, Kate</creatorcontrib><creatorcontrib>Lee, Ting‐Ying</creatorcontrib><creatorcontrib>Periasamy, Ammasi</creatorcontrib><creatorcontrib>Kao, Fu‐Jen</creatorcontrib><creatorcontrib>Li, Li‐Tzu</creatorcontrib><creatorcontrib>Lin, Chuang‐Yu</creatorcontrib><creatorcontrib>Lin, Hui‐Ju</creatorcontrib><creatorcontrib>Lin, Marie</creatorcontrib><title>Adaptable interaction between aquaporin‐1 and band 3 reveals a potential role of water channel in blood CO2 transport</title><title>The FASEB journal</title><description>ABSTRACT
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. FASEB J. 31, 4256–4264 (2017). www.fasebj.org</description><subject>anion exchanger‐1</subject><subject>Anion exchanging</subject><subject>Aquaporin 1</subject><subject>Aquaporins</subject><subject>Carbon dioxide</subject><subject>Carbonic anhydrase</subject><subject>Carbonic anhydrase II</subject><subject>Conversion</subject><subject>Dipoles</subject><subject>Energy measurement</subject><subject>Energy transfer</subject><subject>erythrocyte</subject><subject>Erythrocytes</subject><subject>FLIM‐FRET</subject><subject>Fluorescence</subject><subject>Fluorescence resonance energy transfer</subject><subject>Miltenberger subtype III</subject><subject>Proteins</subject><subject>Respiration</subject><subject>Transport</subject><issn>0892-6638</issn><issn>1530-6860</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><recordid>eNpdkUFrFTEQgIMo9lk9eg948bJ1kuxmswhCffi0UihUPYfZ7KzNY1-yze720Zs_wd_oLzGlpaW9zMDMNx8zDGNvBRwJaPSHfnskQWgQ0sjzZ2wlKgWFNhqesxWYRhZaK3PAXk3TFgBERl-yA2mqRkulVmx_3OE4YzsQ92GmhG72MfCW5j1R4Hi54BiTD__-_BUcQ8fbm6B4oivCYeLIxzhTmD0OPMVsiT3fYxZxd4Eh0JC1vB1i7Pj6TPI5YZiycH7NXvR5nt7c5UP2a_Pl5_pbcXr29WR9fFqMSqrzogEHrVM9lL2EptSylrrpTG9cBZUQuiqJyg4bKSW40miJzjnMPeqobk2nDtmnW--4tDvqXF414WDH5HeYrm1Ebx93gr-wv-OV1RJqYSAL3t8JUrxcaJrtzk-OhgEDxWWyogFTKqh1ndF3T9BtXFLI52UqQ0aJqsrUx1tq7we6vt9EgL35p-239uGfdvPjs9x8fyio_1dTlxg</recordid><startdate>201710</startdate><enddate>201710</enddate><creator>Hsu, Kate</creator><creator>Lee, Ting‐Ying</creator><creator>Periasamy, Ammasi</creator><creator>Kao, Fu‐Jen</creator><creator>Li, Li‐Tzu</creator><creator>Lin, Chuang‐Yu</creator><creator>Lin, Hui‐Ju</creator><creator>Lin, Marie</creator><general>Federation of American Societies for Experimental Biology</general><general>Federation of American Societies for Experimental Biology (FASEB)</general><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U7</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>201710</creationdate><title>Adaptable interaction between aquaporin‐1 and band 3 reveals a potential role of water channel in blood CO2 transport</title><author>Hsu, Kate ; Lee, Ting‐Ying ; Periasamy, Ammasi ; Kao, Fu‐Jen ; Li, Li‐Tzu ; Lin, Chuang‐Yu ; Lin, Hui‐Ju ; Lin, Marie</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p323R-90c0bc3f04f2094627269d8f8c50511654ee4da92220c4862accca505ede7b8d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>anion exchanger‐1</topic><topic>Anion exchanging</topic><topic>Aquaporin 1</topic><topic>Aquaporins</topic><topic>Carbon dioxide</topic><topic>Carbonic anhydrase</topic><topic>Carbonic anhydrase II</topic><topic>Conversion</topic><topic>Dipoles</topic><topic>Energy measurement</topic><topic>Energy transfer</topic><topic>erythrocyte</topic><topic>Erythrocytes</topic><topic>FLIM‐FRET</topic><topic>Fluorescence</topic><topic>Fluorescence resonance energy transfer</topic><topic>Miltenberger subtype III</topic><topic>Proteins</topic><topic>Respiration</topic><topic>Transport</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hsu, Kate</creatorcontrib><creatorcontrib>Lee, Ting‐Ying</creatorcontrib><creatorcontrib>Periasamy, Ammasi</creatorcontrib><creatorcontrib>Kao, Fu‐Jen</creatorcontrib><creatorcontrib>Li, Li‐Tzu</creatorcontrib><creatorcontrib>Lin, Chuang‐Yu</creatorcontrib><creatorcontrib>Lin, Hui‐Ju</creatorcontrib><creatorcontrib>Lin, Marie</creatorcontrib><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The FASEB journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hsu, Kate</au><au>Lee, Ting‐Ying</au><au>Periasamy, Ammasi</au><au>Kao, Fu‐Jen</au><au>Li, Li‐Tzu</au><au>Lin, Chuang‐Yu</au><au>Lin, Hui‐Ju</au><au>Lin, Marie</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Adaptable interaction between aquaporin‐1 and band 3 reveals a potential role of water channel in blood CO2 transport</atitle><jtitle>The FASEB journal</jtitle><date>2017-10</date><risdate>2017</risdate><volume>31</volume><issue>10</issue><spage>4256</spage><epage>4264</epage><pages>4256-4264</pages><issn>0892-6638</issn><eissn>1530-6860</eissn><abstract>ABSTRACT
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. FASEB J. 31, 4256–4264 (2017). www.fasebj.org</abstract><cop>Bethesda</cop><pub>Federation of American Societies for Experimental Biology</pub><pmid>28596233</pmid><doi>10.1096/fj.201601282R</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | anion exchanger‐1 Anion exchanging Aquaporin 1 Aquaporins Carbon dioxide Carbonic anhydrase Carbonic anhydrase II Conversion Dipoles Energy measurement Energy transfer erythrocyte Erythrocytes FLIM‐FRET Fluorescence Fluorescence resonance energy transfer Miltenberger subtype III Proteins Respiration Transport |
| title | Adaptable interaction between aquaporin‐1 and band 3 reveals a potential role of water channel in blood CO2 transport |
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