Na-K-ATPase regulates tight junction permeability through occludin phosphorylation in pancreatic epithelial cells
Tight junctions are crucial for maintaining the polarity and vectorial transport functions of epithelial cells. We and others have shown that Na-K-ATPase plays a key role in the organization and permeability of tight junctions in mammalian cells and analogous septate junctions in Drosophila. However...
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| Veröffentlicht in: | American journal of physiology: Gastrointestinal and liver physiology 2007-01, Vol.292 (1), p.G124-G133 |
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| container_title | American journal of physiology: Gastrointestinal and liver physiology |
| container_volume | 292 |
| creator | Rajasekaran, Sigrid A Barwe, Sonali P Gopal, Jegan Ryazantsev, Sergey Schneeberger, Eveline E Rajasekaran, Ayyappan K |
| description | Tight junctions are crucial for maintaining the polarity and vectorial transport functions of epithelial cells. We and others have shown that Na-K-ATPase plays a key role in the organization and permeability of tight junctions in mammalian cells and analogous septate junctions in Drosophila. However, the mechanism by which Na-K-ATPase modulates tight junctions is not known. In this study, using a well-differentiated human pancreatic epithelial cell line HPAF-II, we demonstrate that Na-K-ATPase is present at the apical junctions and forms a complex with protein phosphatase-2A, a protein known to be present at tight junctions. Inhibition of Na-K-ATPase ion transport function reduced protein phosphatase-2A activity, hyperphosphorylated occludin, induced rearrangement of tight junction strands, and increased permeability of tight junctions to ionic and nonionic solutes. These data suggest that Na-K-ATPase is required for controlling the tight junction gate function. |
| doi_str_mv | 10.1152/ajpgi.00297.2006 |
| format | Article |
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We and others have shown that Na-K-ATPase plays a key role in the organization and permeability of tight junctions in mammalian cells and analogous septate junctions in Drosophila. However, the mechanism by which Na-K-ATPase modulates tight junctions is not known. In this study, using a well-differentiated human pancreatic epithelial cell line HPAF-II, we demonstrate that Na-K-ATPase is present at the apical junctions and forms a complex with protein phosphatase-2A, a protein known to be present at tight junctions. Inhibition of Na-K-ATPase ion transport function reduced protein phosphatase-2A activity, hyperphosphorylated occludin, induced rearrangement of tight junction strands, and increased permeability of tight junctions to ionic and nonionic solutes. These data suggest that Na-K-ATPase is required for controlling the tight junction gate function.</description><identifier>ISSN: 0193-1857</identifier><identifier>EISSN: 1522-1547</identifier><identifier>DOI: 10.1152/ajpgi.00297.2006</identifier><identifier>PMID: 16959951</identifier><identifier>CODEN: APGPDF</identifier><language>eng</language><publisher>United States: American Physiological Society</publisher><subject>Cadherins - metabolism ; Cell Line ; Enzyme Inhibitors - pharmacology ; Epithelial Cells - physiology ; Freeze Fracturing ; Humans ; Membrane Proteins - metabolism ; Microscopy, Confocal ; Microscopy, Immunoelectron ; Occludin ; Pancreas ; Pancreas - cytology ; Pancreas - physiology ; Pancreas - ultrastructure ; Permeability ; Phosphoproteins - metabolism ; Phosphorylation ; Proteins ; Sodium ; Sodium-Potassium-Exchanging ATPase - drug effects ; Sodium-Potassium-Exchanging ATPase - metabolism ; Tight Junctions - drug effects ; Tight Junctions - physiology ; Tight Junctions - ultrastructure ; Zonula Occludens-1 Protein</subject><ispartof>American journal of physiology: Gastrointestinal and liver physiology, 2007-01, Vol.292 (1), p.G124-G133</ispartof><rights>Copyright American Physiological Society Jan 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c390t-c443b685f4b81a846911a359c30966443640266b12f3b2211e087aae261b04ad3</citedby><cites>FETCH-LOGICAL-c390t-c443b685f4b81a846911a359c30966443640266b12f3b2211e087aae261b04ad3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,3038,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16959951$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rajasekaran, Sigrid A</creatorcontrib><creatorcontrib>Barwe, Sonali P</creatorcontrib><creatorcontrib>Gopal, Jegan</creatorcontrib><creatorcontrib>Ryazantsev, Sergey</creatorcontrib><creatorcontrib>Schneeberger, Eveline E</creatorcontrib><creatorcontrib>Rajasekaran, Ayyappan K</creatorcontrib><title>Na-K-ATPase regulates tight junction permeability through occludin phosphorylation in pancreatic epithelial cells</title><title>American journal of physiology: Gastrointestinal and liver physiology</title><addtitle>Am J Physiol Gastrointest Liver Physiol</addtitle><description>Tight junctions are crucial for maintaining the polarity and vectorial transport functions of epithelial cells. We and others have shown that Na-K-ATPase plays a key role in the organization and permeability of tight junctions in mammalian cells and analogous septate junctions in Drosophila. However, the mechanism by which Na-K-ATPase modulates tight junctions is not known. In this study, using a well-differentiated human pancreatic epithelial cell line HPAF-II, we demonstrate that Na-K-ATPase is present at the apical junctions and forms a complex with protein phosphatase-2A, a protein known to be present at tight junctions. Inhibition of Na-K-ATPase ion transport function reduced protein phosphatase-2A activity, hyperphosphorylated occludin, induced rearrangement of tight junction strands, and increased permeability of tight junctions to ionic and nonionic solutes. These data suggest that Na-K-ATPase is required for controlling the tight junction gate function.</description><subject>Cadherins - metabolism</subject><subject>Cell Line</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Epithelial Cells - physiology</subject><subject>Freeze Fracturing</subject><subject>Humans</subject><subject>Membrane Proteins - metabolism</subject><subject>Microscopy, Confocal</subject><subject>Microscopy, Immunoelectron</subject><subject>Occludin</subject><subject>Pancreas</subject><subject>Pancreas - cytology</subject><subject>Pancreas - physiology</subject><subject>Pancreas - ultrastructure</subject><subject>Permeability</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>Proteins</subject><subject>Sodium</subject><subject>Sodium-Potassium-Exchanging ATPase - drug effects</subject><subject>Sodium-Potassium-Exchanging ATPase - metabolism</subject><subject>Tight Junctions - drug effects</subject><subject>Tight Junctions - physiology</subject><subject>Tight Junctions - ultrastructure</subject><subject>Zonula Occludens-1 Protein</subject><issn>0193-1857</issn><issn>1522-1547</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkb1v2zAQxYmgReIm2TsVQoducu74JXE0gvQDNdoMyUxQNG3RkCWZpAb_96FiAwU6EATvfu_hjo-QzwhLREEfzH7c-SUAVdWSAsgrsshlWqLg1QeyAFSsxFpUN-RTjHsAEBTxmtygVEIpgQty_GPK3-Xq5dlEVwS3mzqTXCyS37Wp2E-9TX7oi9GFgzON73w6FakNw7Rri8Habtr43G2HmE84Ze1MzyXT2-Dy0xZu9Kl1nTddYV3XxTvycWu66O4v9y15_f708vizXP_98etxtS4tU5BKyzlrZC22vKnR1FwqRMOEsgyUlLkpOVApG6Rb1tC8loO6MsZRiQ1ws2G35NvZdwzDcXIx6YOP8wSmd8MUtaw5Zj-Wwa__gfthCn2eTVNGRS0r4BmCM2TDEGNwWz0GfzDhpBH0nIV-z0K_Z6HnLLLky8V3ag5u809w-Xz2BikJhio</recordid><startdate>200701</startdate><enddate>200701</enddate><creator>Rajasekaran, Sigrid A</creator><creator>Barwe, Sonali P</creator><creator>Gopal, Jegan</creator><creator>Ryazantsev, Sergey</creator><creator>Schneeberger, Eveline E</creator><creator>Rajasekaran, Ayyappan K</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>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>200701</creationdate><title>Na-K-ATPase regulates tight junction permeability through occludin phosphorylation in pancreatic epithelial cells</title><author>Rajasekaran, Sigrid A ; Barwe, Sonali P ; Gopal, Jegan ; Ryazantsev, Sergey ; Schneeberger, Eveline E ; Rajasekaran, Ayyappan K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c390t-c443b685f4b81a846911a359c30966443640266b12f3b2211e087aae261b04ad3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Cadherins - metabolism</topic><topic>Cell Line</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Epithelial Cells - physiology</topic><topic>Freeze Fracturing</topic><topic>Humans</topic><topic>Membrane Proteins - metabolism</topic><topic>Microscopy, Confocal</topic><topic>Microscopy, Immunoelectron</topic><topic>Occludin</topic><topic>Pancreas</topic><topic>Pancreas - cytology</topic><topic>Pancreas - physiology</topic><topic>Pancreas - ultrastructure</topic><topic>Permeability</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorylation</topic><topic>Proteins</topic><topic>Sodium</topic><topic>Sodium-Potassium-Exchanging ATPase - drug effects</topic><topic>Sodium-Potassium-Exchanging ATPase - metabolism</topic><topic>Tight Junctions - drug effects</topic><topic>Tight Junctions - physiology</topic><topic>Tight Junctions - ultrastructure</topic><topic>Zonula Occludens-1 Protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rajasekaran, Sigrid A</creatorcontrib><creatorcontrib>Barwe, Sonali P</creatorcontrib><creatorcontrib>Gopal, Jegan</creatorcontrib><creatorcontrib>Ryazantsev, Sergey</creatorcontrib><creatorcontrib>Schneeberger, Eveline E</creatorcontrib><creatorcontrib>Rajasekaran, Ayyappan K</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>American journal of physiology: Gastrointestinal and liver physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rajasekaran, Sigrid A</au><au>Barwe, Sonali P</au><au>Gopal, Jegan</au><au>Ryazantsev, Sergey</au><au>Schneeberger, Eveline E</au><au>Rajasekaran, Ayyappan K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Na-K-ATPase regulates tight junction permeability through occludin phosphorylation in pancreatic epithelial cells</atitle><jtitle>American journal of physiology: Gastrointestinal and liver physiology</jtitle><addtitle>Am J Physiol Gastrointest Liver Physiol</addtitle><date>2007-01</date><risdate>2007</risdate><volume>292</volume><issue>1</issue><spage>G124</spage><epage>G133</epage><pages>G124-G133</pages><issn>0193-1857</issn><eissn>1522-1547</eissn><coden>APGPDF</coden><abstract>Tight junctions are crucial for maintaining the polarity and vectorial transport functions of epithelial cells. We and others have shown that Na-K-ATPase plays a key role in the organization and permeability of tight junctions in mammalian cells and analogous septate junctions in Drosophila. However, the mechanism by which Na-K-ATPase modulates tight junctions is not known. In this study, using a well-differentiated human pancreatic epithelial cell line HPAF-II, we demonstrate that Na-K-ATPase is present at the apical junctions and forms a complex with protein phosphatase-2A, a protein known to be present at tight junctions. Inhibition of Na-K-ATPase ion transport function reduced protein phosphatase-2A activity, hyperphosphorylated occludin, induced rearrangement of tight junction strands, and increased permeability of tight junctions to ionic and nonionic solutes. These data suggest that Na-K-ATPase is required for controlling the tight junction gate function.</abstract><cop>United States</cop><pub>American Physiological Society</pub><pmid>16959951</pmid><doi>10.1152/ajpgi.00297.2006</doi></addata></record> |
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| source | MEDLINE; American Physiological Society; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Cadherins - metabolism Cell Line Enzyme Inhibitors - pharmacology Epithelial Cells - physiology Freeze Fracturing Humans Membrane Proteins - metabolism Microscopy, Confocal Microscopy, Immunoelectron Occludin Pancreas Pancreas - cytology Pancreas - physiology Pancreas - ultrastructure Permeability Phosphoproteins - metabolism Phosphorylation Proteins Sodium Sodium-Potassium-Exchanging ATPase - drug effects Sodium-Potassium-Exchanging ATPase - metabolism Tight Junctions - drug effects Tight Junctions - physiology Tight Junctions - ultrastructure Zonula Occludens-1 Protein |
| title | Na-K-ATPase regulates tight junction permeability through occludin phosphorylation in pancreatic epithelial cells |
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