Insulin-stimulated trafficking of ENaC in renal cells requires PI 3-kinase activity
1 Department of Biology, Indiana University-Purdue University at Indianapolis, Indianapolis 46202; and 2 Therapeutic Area Discovery Research and Chemistry Information Technology and 3 Cardiovascular Research, Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, Indiana 46285 ENaC-EGF...
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| Veröffentlicht in: | American Journal of Physiology: Cell Physiology 2003-06, Vol.284 (6), p.C1645-C1653 |
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| container_issue | 6 |
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| container_title | American Journal of Physiology: Cell Physiology |
| container_volume | 284 |
| creator | Blazer-Yost, Bonnie L Esterman, Michail A Vlahos, Chris J |
| description | 1 Department of Biology, Indiana University-Purdue
University at Indianapolis, Indianapolis 46202; and
2 Therapeutic Area Discovery Research and Chemistry
Information Technology and 3 Cardiovascular Research,
Lilly Research Laboratories, Eli Lilly and Company, Indianapolis,
Indiana 46285
ENaC-EGFP (enhanced green fluorescent
protein-tagged -subunit of the epithelial Na + channel)
stably transfected clonal lines derived from the A6 parental cell line
were used to study the physical mechanisms of insulin-stimulated
Na + transport. Within 1 min of insulin stimulation, ENaC
migrates from a diffuse cytoplasmic localization to the apical and
lateral membranes. Concurrently, after insulin stimulation,
phosphatidylinositol 3-kinase (PI 3-kinase) is colocalized with ENaC on
the lateral but not apical membrane. An inhibitor of PI 3-kinase,
LY-294002, does not inhibit ENaC/PI 3-kinase colocalization but does
alter the intracellular site of the colocalization, preventing the
translocation of ENaC to the lateral and apical membranes. These data
show that insulin stimulation causes the migration of ENaC to the
lateral and apical cell membranes and that this trafficking is
dependent on PI 3-kinase activity.
epithelial sodium channels; phosphatidylinositol
3,4,5-bisphosphate; phosphatidylinositol 3-kinase; phosphoinositide
pathway; transepithelial signal transduction; sodium transport |
| doi_str_mv | 10.1152/ajpcell.00372.2002 |
| format | Article |
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University at Indianapolis, Indianapolis 46202; and
2 Therapeutic Area Discovery Research and Chemistry
Information Technology and 3 Cardiovascular Research,
Lilly Research Laboratories, Eli Lilly and Company, Indianapolis,
Indiana 46285
ENaC-EGFP (enhanced green fluorescent
protein-tagged -subunit of the epithelial Na + channel)
stably transfected clonal lines derived from the A6 parental cell line
were used to study the physical mechanisms of insulin-stimulated
Na + transport. Within 1 min of insulin stimulation, ENaC
migrates from a diffuse cytoplasmic localization to the apical and
lateral membranes. Concurrently, after insulin stimulation,
phosphatidylinositol 3-kinase (PI 3-kinase) is colocalized with ENaC on
the lateral but not apical membrane. An inhibitor of PI 3-kinase,
LY-294002, does not inhibit ENaC/PI 3-kinase colocalization but does
alter the intracellular site of the colocalization, preventing the
translocation of ENaC to the lateral and apical membranes. These data
show that insulin stimulation causes the migration of ENaC to the
lateral and apical cell membranes and that this trafficking is
dependent on PI 3-kinase activity.
epithelial sodium channels; phosphatidylinositol
3,4,5-bisphosphate; phosphatidylinositol 3-kinase; phosphoinositide
pathway; transepithelial signal transduction; sodium transport</description><identifier>ISSN: 0363-6143</identifier><identifier>EISSN: 1522-1563</identifier><identifier>DOI: 10.1152/ajpcell.00372.2002</identifier><identifier>PMID: 12606308</identifier><language>eng</language><publisher>United States</publisher><subject>Animals ; Biological Transport - physiology ; Cell Line ; Cell Membrane - metabolism ; Cell Polarity ; Chromones - metabolism ; Electrophysiology ; Enzyme Inhibitors - metabolism ; Epithelial Sodium Channels ; Insulin - metabolism ; Kidney - cytology ; Kidney - metabolism ; Microscopy, Fluorescence ; Morpholines - metabolism ; Phosphatidylinositol 3-Kinases - antagonists & inhibitors ; Phosphatidylinositol 3-Kinases - metabolism ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Sodium - metabolism ; Sodium Channels - genetics ; Sodium Channels - metabolism ; Xenopus laevis</subject><ispartof>American Journal of Physiology: Cell Physiology, 2003-06, Vol.284 (6), p.C1645-C1653</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c455t-47fb13b1a8e7a8dd3ba48979c8a65b3c83957d8b8de8b923f36b2116b071bda93</citedby><cites>FETCH-LOGICAL-c455t-47fb13b1a8e7a8dd3ba48979c8a65b3c83957d8b8de8b923f36b2116b071bda93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,3026,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12606308$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Blazer-Yost, Bonnie L</creatorcontrib><creatorcontrib>Esterman, Michail A</creatorcontrib><creatorcontrib>Vlahos, Chris J</creatorcontrib><title>Insulin-stimulated trafficking of ENaC in renal cells requires PI 3-kinase activity</title><title>American Journal of Physiology: Cell Physiology</title><addtitle>Am J Physiol Cell Physiol</addtitle><description>1 Department of Biology, Indiana University-Purdue
University at Indianapolis, Indianapolis 46202; and
2 Therapeutic Area Discovery Research and Chemistry
Information Technology and 3 Cardiovascular Research,
Lilly Research Laboratories, Eli Lilly and Company, Indianapolis,
Indiana 46285
ENaC-EGFP (enhanced green fluorescent
protein-tagged -subunit of the epithelial Na + channel)
stably transfected clonal lines derived from the A6 parental cell line
were used to study the physical mechanisms of insulin-stimulated
Na + transport. Within 1 min of insulin stimulation, ENaC
migrates from a diffuse cytoplasmic localization to the apical and
lateral membranes. Concurrently, after insulin stimulation,
phosphatidylinositol 3-kinase (PI 3-kinase) is colocalized with ENaC on
the lateral but not apical membrane. An inhibitor of PI 3-kinase,
LY-294002, does not inhibit ENaC/PI 3-kinase colocalization but does
alter the intracellular site of the colocalization, preventing the
translocation of ENaC to the lateral and apical membranes. These data
show that insulin stimulation causes the migration of ENaC to the
lateral and apical cell membranes and that this trafficking is
dependent on PI 3-kinase activity.
epithelial sodium channels; phosphatidylinositol
3,4,5-bisphosphate; phosphatidylinositol 3-kinase; phosphoinositide
pathway; transepithelial signal transduction; sodium transport</description><subject>Animals</subject><subject>Biological Transport - physiology</subject><subject>Cell Line</subject><subject>Cell Membrane - metabolism</subject><subject>Cell Polarity</subject><subject>Chromones - metabolism</subject><subject>Electrophysiology</subject><subject>Enzyme Inhibitors - metabolism</subject><subject>Epithelial Sodium Channels</subject><subject>Insulin - metabolism</subject><subject>Kidney - cytology</subject><subject>Kidney - metabolism</subject><subject>Microscopy, Fluorescence</subject><subject>Morpholines - metabolism</subject><subject>Phosphatidylinositol 3-Kinases - antagonists & inhibitors</subject><subject>Phosphatidylinositol 3-Kinases - metabolism</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Sodium - metabolism</subject><subject>Sodium Channels - genetics</subject><subject>Sodium Channels - metabolism</subject><subject>Xenopus laevis</subject><issn>0363-6143</issn><issn>1522-1563</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kMtOwzAQRS0EoqXwAyyQV-wS_Egchx2qWqhUARJlbdmJ07q4SYgTIH-PS8tjw8oj-Z47owPAOUYhxjG5kus609aGCNGEhAQhcgCG_oMEOGb0EAwRZTRgOKIDcOLcGiEUEZYegwEmDDGK-BA8zUrXWVMGrjWbzspW57BtZFGY7MWUS1gVcHIvx9CUsNGltHC70fn5tTONdvBxBmngk9JpKLPWvJm2PwVHhbROn-3fEXieThbju2D-cDsb38yDLIrjNoiSQmGqsOQ6kTzPqZIRT5M045LFimacpnGSc8VzzVVKaEGZIhgzhRKscpnSEbjc9dZN9dpp14qNcdv7ZKmrzomEEo5xlPgg2QWzpnKu0YWoG7ORTS8wEluVYq9SfKkUW5Ueuti3d2qj819k784Hwl1gZZard29D1KvemcpWy_6nkPBIMDHGLIo9cP0_MO2sXeiP9pv8A4o6L-gnpsyWcA</recordid><startdate>20030601</startdate><enddate>20030601</enddate><creator>Blazer-Yost, Bonnie L</creator><creator>Esterman, Michail A</creator><creator>Vlahos, Chris J</creator><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>20030601</creationdate><title>Insulin-stimulated trafficking of ENaC in renal cells requires PI 3-kinase activity</title><author>Blazer-Yost, Bonnie L ; Esterman, Michail A ; Vlahos, Chris J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c455t-47fb13b1a8e7a8dd3ba48979c8a65b3c83957d8b8de8b923f36b2116b071bda93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Animals</topic><topic>Biological Transport - physiology</topic><topic>Cell Line</topic><topic>Cell Membrane - metabolism</topic><topic>Cell Polarity</topic><topic>Chromones - metabolism</topic><topic>Electrophysiology</topic><topic>Enzyme Inhibitors - metabolism</topic><topic>Epithelial Sodium Channels</topic><topic>Insulin - metabolism</topic><topic>Kidney - cytology</topic><topic>Kidney - metabolism</topic><topic>Microscopy, Fluorescence</topic><topic>Morpholines - metabolism</topic><topic>Phosphatidylinositol 3-Kinases - antagonists & inhibitors</topic><topic>Phosphatidylinositol 3-Kinases - metabolism</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Sodium - metabolism</topic><topic>Sodium Channels - genetics</topic><topic>Sodium Channels - metabolism</topic><topic>Xenopus laevis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Blazer-Yost, Bonnie L</creatorcontrib><creatorcontrib>Esterman, Michail A</creatorcontrib><creatorcontrib>Vlahos, Chris J</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: Cell Physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Blazer-Yost, Bonnie L</au><au>Esterman, Michail A</au><au>Vlahos, Chris J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Insulin-stimulated trafficking of ENaC in renal cells requires PI 3-kinase activity</atitle><jtitle>American Journal of Physiology: Cell Physiology</jtitle><addtitle>Am J Physiol Cell Physiol</addtitle><date>2003-06-01</date><risdate>2003</risdate><volume>284</volume><issue>6</issue><spage>C1645</spage><epage>C1653</epage><pages>C1645-C1653</pages><issn>0363-6143</issn><eissn>1522-1563</eissn><abstract>1 Department of Biology, Indiana University-Purdue
University at Indianapolis, Indianapolis 46202; and
2 Therapeutic Area Discovery Research and Chemistry
Information Technology and 3 Cardiovascular Research,
Lilly Research Laboratories, Eli Lilly and Company, Indianapolis,
Indiana 46285
ENaC-EGFP (enhanced green fluorescent
protein-tagged -subunit of the epithelial Na + channel)
stably transfected clonal lines derived from the A6 parental cell line
were used to study the physical mechanisms of insulin-stimulated
Na + transport. Within 1 min of insulin stimulation, ENaC
migrates from a diffuse cytoplasmic localization to the apical and
lateral membranes. Concurrently, after insulin stimulation,
phosphatidylinositol 3-kinase (PI 3-kinase) is colocalized with ENaC on
the lateral but not apical membrane. An inhibitor of PI 3-kinase,
LY-294002, does not inhibit ENaC/PI 3-kinase colocalization but does
alter the intracellular site of the colocalization, preventing the
translocation of ENaC to the lateral and apical membranes. These data
show that insulin stimulation causes the migration of ENaC to the
lateral and apical cell membranes and that this trafficking is
dependent on PI 3-kinase activity.
epithelial sodium channels; phosphatidylinositol
3,4,5-bisphosphate; phosphatidylinositol 3-kinase; phosphoinositide
pathway; transepithelial signal transduction; sodium transport</abstract><cop>United States</cop><pmid>12606308</pmid><doi>10.1152/ajpcell.00372.2002</doi></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0363-6143 |
| ispartof | American Journal of Physiology: Cell Physiology, 2003-06, Vol.284 (6), p.C1645-C1653 |
| issn | 0363-6143 1522-1563 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73281147 |
| source | MEDLINE; American Physiological Society; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Animals Biological Transport - physiology Cell Line Cell Membrane - metabolism Cell Polarity Chromones - metabolism Electrophysiology Enzyme Inhibitors - metabolism Epithelial Sodium Channels Insulin - metabolism Kidney - cytology Kidney - metabolism Microscopy, Fluorescence Morpholines - metabolism Phosphatidylinositol 3-Kinases - antagonists & inhibitors Phosphatidylinositol 3-Kinases - metabolism Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Sodium - metabolism Sodium Channels - genetics Sodium Channels - metabolism Xenopus laevis |
| title | Insulin-stimulated trafficking of ENaC in renal cells requires PI 3-kinase activity |
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