The Na-K-ATPase α₁β₁ heterodimer as a cell adhesion molecule in epithelia
The ion gradients generated by the Na-K-ATPase play a critical role in epithelia by driving transepithelial transport of various solutes. The efficiency of this Na-K-ATPase-driven vectorial transport depends on the integrity of epithelial junctions that maintain polar distribution of membrane transp...
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| Veröffentlicht in: | American Journal of Physiology: Cell Physiology 2012-05, Vol.302 (9), p.C1271-C1281 |
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| container_end_page | C1281 |
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| container_issue | 9 |
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| container_title | American Journal of Physiology: Cell Physiology |
| container_volume | 302 |
| creator | Vagin, Olga Dada, Laura A Tokhtaeva, Elmira Sachs, George |
| description | The ion gradients generated by the Na-K-ATPase play a critical role in epithelia by driving transepithelial transport of various solutes. The efficiency of this Na-K-ATPase-driven vectorial transport depends on the integrity of epithelial junctions that maintain polar distribution of membrane transporters, including the basolateral sodium pump, and restrict paracellular diffusion of solutes. The review summarizes the data showing that, in addition to pumping ions, the Na-K-ATPase located at the sites of cell-cell junction acts as a cell adhesion molecule by interacting with the Na-K-ATPase of the adjacent cell in the intercellular space accompanied by anchoring to the cytoskeleton in the cytoplasm. The review also discusses the experimental evidence on the importance of a specific amino acid region in the extracellular domain of the Na-K-ATPase β(1) subunit for the Na-K-ATPase trans-dimerization and intercellular adhesion. Furthermore, a possible role of N-glycans linked to the Na-K-ATPase β(1) subunit in regulation of epithelial junctions by modulating β(1)-β(1) interactions is discussed. |
| doi_str_mv | 10.1152/ajpcell.00456.2011 |
| format | Article |
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The efficiency of this Na-K-ATPase-driven vectorial transport depends on the integrity of epithelial junctions that maintain polar distribution of membrane transporters, including the basolateral sodium pump, and restrict paracellular diffusion of solutes. The review summarizes the data showing that, in addition to pumping ions, the Na-K-ATPase located at the sites of cell-cell junction acts as a cell adhesion molecule by interacting with the Na-K-ATPase of the adjacent cell in the intercellular space accompanied by anchoring to the cytoskeleton in the cytoplasm. The review also discusses the experimental evidence on the importance of a specific amino acid region in the extracellular domain of the Na-K-ATPase β(1) subunit for the Na-K-ATPase trans-dimerization and intercellular adhesion. Furthermore, a possible role of N-glycans linked to the Na-K-ATPase β(1) subunit in regulation of epithelial junctions by modulating β(1)-β(1) interactions is discussed.</description><subject>Animals</subject><subject>Cell Adhesion Molecules - chemistry</subject><subject>Cell Adhesion Molecules - metabolism</subject><subject>Epithelial Cells - chemistry</subject><subject>Epithelial Cells - metabolism</subject><subject>Humans</subject><subject>Intercellular Junctions - chemistry</subject><subject>Intercellular Junctions - metabolism</subject><subject>Protein Multimerization</subject><subject>Protein Structure, Quaternary</subject><subject>Review</subject><subject>Sodium-Potassium-Exchanging ATPase - chemistry</subject><subject>Sodium-Potassium-Exchanging ATPase - metabolism</subject><issn>1522-1563</issn><issn>0363-6143</issn><issn>1522-1563</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUMtOwzAQtBCIlsIPcEA-ckmJ7STGF6Sq4iUqyqGco42zJq7yIk6QOMIfwYf0I_gSUlFQueyuNKOZ2SHkmPljxkJ-BstaY56PfT8IozH3Gdshwx7gHgsjsbt1D8iBc0u_J_JI7ZMB51xKGYZDMl9kSO_Bu_MmiwdwSFcfX-9vq89-0AxbbKrUFthQcBTo2o1CmqGzVUmLKkfd5UhtSbG2bYa5hUOyZyB3eLTZI_J4dbmY3niz-fXtdDLzllwx5iVamZSBEkaLPqBWLBQm4kIqppEbE2kN5zIMUkQjOASJUCwJJARgUEshxIhc_OjWXVJgqrFsG8jjurEFNK9xBTb-j5Q2i5-ql1iIiKkg6gVONwJN9dyha-PCuvWDUGLVuZj1dTIpeOj31JNtrz-T3xbFNxL0eVI</recordid><startdate>20120501</startdate><enddate>20120501</enddate><creator>Vagin, Olga</creator><creator>Dada, Laura A</creator><creator>Tokhtaeva, Elmira</creator><creator>Sachs, George</creator><general>American Physiological Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20120501</creationdate><title>The Na-K-ATPase α₁β₁ heterodimer as a cell adhesion molecule in epithelia</title><author>Vagin, Olga ; Dada, Laura A ; Tokhtaeva, Elmira ; Sachs, George</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-j2911-bc9fd1a93fc3156c9153f623791ce2ff6cca8754deef32a4b391b47a4afec7333</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Animals</topic><topic>Cell Adhesion Molecules - chemistry</topic><topic>Cell Adhesion Molecules - metabolism</topic><topic>Epithelial Cells - chemistry</topic><topic>Epithelial Cells - metabolism</topic><topic>Humans</topic><topic>Intercellular Junctions - chemistry</topic><topic>Intercellular Junctions - metabolism</topic><topic>Protein Multimerization</topic><topic>Protein Structure, Quaternary</topic><topic>Review</topic><topic>Sodium-Potassium-Exchanging ATPase - chemistry</topic><topic>Sodium-Potassium-Exchanging ATPase - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vagin, Olga</creatorcontrib><creatorcontrib>Dada, Laura A</creatorcontrib><creatorcontrib>Tokhtaeva, Elmira</creatorcontrib><creatorcontrib>Sachs, George</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>American Journal of Physiology: Cell Physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vagin, Olga</au><au>Dada, Laura A</au><au>Tokhtaeva, Elmira</au><au>Sachs, George</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Na-K-ATPase α₁β₁ heterodimer as a cell adhesion molecule in epithelia</atitle><jtitle>American Journal of Physiology: Cell Physiology</jtitle><addtitle>Am J Physiol Cell Physiol</addtitle><date>2012-05-01</date><risdate>2012</risdate><volume>302</volume><issue>9</issue><spage>C1271</spage><epage>C1281</epage><pages>C1271-C1281</pages><issn>1522-1563</issn><issn>0363-6143</issn><eissn>1522-1563</eissn><abstract>The ion gradients generated by the Na-K-ATPase play a critical role in epithelia by driving transepithelial transport of various solutes. The efficiency of this Na-K-ATPase-driven vectorial transport depends on the integrity of epithelial junctions that maintain polar distribution of membrane transporters, including the basolateral sodium pump, and restrict paracellular diffusion of solutes. The review summarizes the data showing that, in addition to pumping ions, the Na-K-ATPase located at the sites of cell-cell junction acts as a cell adhesion molecule by interacting with the Na-K-ATPase of the adjacent cell in the intercellular space accompanied by anchoring to the cytoskeleton in the cytoplasm. The review also discusses the experimental evidence on the importance of a specific amino acid region in the extracellular domain of the Na-K-ATPase β(1) subunit for the Na-K-ATPase trans-dimerization and intercellular adhesion. 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| ispartof | American Journal of Physiology: Cell Physiology, 2012-05, Vol.302 (9), p.C1271-C1281 |
| issn | 1522-1563 0363-6143 1522-1563 |
| language | eng |
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| source | MEDLINE; American Physiological Society; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Cell Adhesion Molecules - chemistry Cell Adhesion Molecules - metabolism Epithelial Cells - chemistry Epithelial Cells - metabolism Humans Intercellular Junctions - chemistry Intercellular Junctions - metabolism Protein Multimerization Protein Structure, Quaternary Review Sodium-Potassium-Exchanging ATPase - chemistry Sodium-Potassium-Exchanging ATPase - metabolism |
| title | The Na-K-ATPase α₁β₁ heterodimer as a cell adhesion molecule in epithelia |
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