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Caveolin Moves from Caveolae to the Golgi Apparatus in Response to Cholesterol Oxidation
Caveolae are a membrane specialization used to internalize molecules by potocytosis. Caveolin, an integral membrane protein, is associated with the striated coat present on the cytoplasmic surface of the caveolae membrane. We now report that oxidation of caveolar cholesterol with cholesterol oxidase...
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Published in: | The Journal of cell biology 1994-12, Vol.127 (5), p.1185-1197 |
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creator | Smart, Eric J. Ying, Yun-Shu Conrad, Patricia A. Richard G. W. Anderson |
description | Caveolae are a membrane specialization used to internalize molecules by potocytosis. Caveolin, an integral membrane protein, is associated with the striated coat present on the cytoplasmic surface of the caveolae membrane. We now report that oxidation of caveolar cholesterol with cholesterol oxidase rapidly displaces the caveolin from the plasma membrane to intracellular vesicles that colocalize with Golgi apparatus markers. After the enzyme is removed from the medium, caveolin returns to caveolae. When untreated cells are gently homogenized, caveolin on the plasma membrane is accessible to both anti-caveolin IgG and trypsin. After cholesterol oxidase treatment, however, Golgi-associated caveolin is inaccessible to both of these molecules. Brefeldin A, which inhibits ER to Golgi trafficking, blocks the appearance of caveolin in the Golgi apparatus but does not prevent caveolin from leaving the plasma membrane. Indirect immunogold localization experiments show that in the presence of cholesterol oxidase caveolin leaves the plasma membrane and becomes associated with endoplasmic reticulum and Golgi compartments. Surprisingly, the loss of caveolin from the plasma membrane does not affect the number or morphology of the caveolae. |
doi_str_mv | 10.1083/jcb.127.5.1185 |
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W. Anderson</creator><creatorcontrib>Smart, Eric J. ; Ying, Yun-Shu ; Conrad, Patricia A. ; Richard G. W. Anderson</creatorcontrib><description>Caveolae are a membrane specialization used to internalize molecules by potocytosis. Caveolin, an integral membrane protein, is associated with the striated coat present on the cytoplasmic surface of the caveolae membrane. We now report that oxidation of caveolar cholesterol with cholesterol oxidase rapidly displaces the caveolin from the plasma membrane to intracellular vesicles that colocalize with Golgi apparatus markers. After the enzyme is removed from the medium, caveolin returns to caveolae. When untreated cells are gently homogenized, caveolin on the plasma membrane is accessible to both anti-caveolin IgG and trypsin. After cholesterol oxidase treatment, however, Golgi-associated caveolin is inaccessible to both of these molecules. Brefeldin A, which inhibits ER to Golgi trafficking, blocks the appearance of caveolin in the Golgi apparatus but does not prevent caveolin from leaving the plasma membrane. Indirect immunogold localization experiments show that in the presence of cholesterol oxidase caveolin leaves the plasma membrane and becomes associated with endoplasmic reticulum and Golgi compartments. Surprisingly, the loss of caveolin from the plasma membrane does not affect the number or morphology of the caveolae.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.127.5.1185</identifier><identifier>PMID: 7962084</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Biological Transport ; Brefeldin A ; Caveolae ; Caveolin 1 ; Caveolins ; Cell Membrane - metabolism ; Cell Membrane - ultrastructure ; Cell membranes ; Cells ; Cells, Cultured ; Cholestenones ; Cholesterol - metabolism ; Cholesterol Oxidase - metabolism ; Cholesterols ; Cyclopentanes - pharmacology ; Endoplasmic Reticulum - metabolism ; Epithelial cells ; Fibroblasts ; Fluorescent Antibody Technique ; Golgi apparatus ; Golgi Apparatus - metabolism ; Humans ; Immunohistochemistry ; Membrane Proteins - analysis ; Membrane Proteins - metabolism ; Oxidases ; Oxidation-Reduction ; Temperature</subject><ispartof>The Journal of cell biology, 1994-12, Vol.127 (5), p.1185-1197</ispartof><rights>Copyright 1994 The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c472t-d1253b93f2fdd0db61fb29a03cfc098c299e32fdd2d736e51d220aba3c0e7b023</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7962084$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Smart, Eric J.</creatorcontrib><creatorcontrib>Ying, Yun-Shu</creatorcontrib><creatorcontrib>Conrad, Patricia A.</creatorcontrib><creatorcontrib>Richard G. W. Anderson</creatorcontrib><title>Caveolin Moves from Caveolae to the Golgi Apparatus in Response to Cholesterol Oxidation</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>Caveolae are a membrane specialization used to internalize molecules by potocytosis. Caveolin, an integral membrane protein, is associated with the striated coat present on the cytoplasmic surface of the caveolae membrane. We now report that oxidation of caveolar cholesterol with cholesterol oxidase rapidly displaces the caveolin from the plasma membrane to intracellular vesicles that colocalize with Golgi apparatus markers. After the enzyme is removed from the medium, caveolin returns to caveolae. When untreated cells are gently homogenized, caveolin on the plasma membrane is accessible to both anti-caveolin IgG and trypsin. After cholesterol oxidase treatment, however, Golgi-associated caveolin is inaccessible to both of these molecules. Brefeldin A, which inhibits ER to Golgi trafficking, blocks the appearance of caveolin in the Golgi apparatus but does not prevent caveolin from leaving the plasma membrane. Indirect immunogold localization experiments show that in the presence of cholesterol oxidase caveolin leaves the plasma membrane and becomes associated with endoplasmic reticulum and Golgi compartments. Surprisingly, the loss of caveolin from the plasma membrane does not affect the number or morphology of the caveolae.</description><subject>Biological Transport</subject><subject>Brefeldin A</subject><subject>Caveolae</subject><subject>Caveolin 1</subject><subject>Caveolins</subject><subject>Cell Membrane - metabolism</subject><subject>Cell Membrane - ultrastructure</subject><subject>Cell membranes</subject><subject>Cells</subject><subject>Cells, Cultured</subject><subject>Cholestenones</subject><subject>Cholesterol - metabolism</subject><subject>Cholesterol Oxidase - metabolism</subject><subject>Cholesterols</subject><subject>Cyclopentanes - pharmacology</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Epithelial cells</subject><subject>Fibroblasts</subject><subject>Fluorescent Antibody Technique</subject><subject>Golgi apparatus</subject><subject>Golgi Apparatus - metabolism</subject><subject>Humans</subject><subject>Immunohistochemistry</subject><subject>Membrane Proteins - analysis</subject><subject>Membrane Proteins - metabolism</subject><subject>Oxidases</subject><subject>Oxidation-Reduction</subject><subject>Temperature</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><recordid>eNpVkc1LwzAchoMoc06vnhRy8tb6S9LPizCKTmEyEAVvIU3TraNratIO_e_N7JiaSyDvkzcfD0KXBHwCCbtdy9wnNPZDn5AkPEJjEgbgJSSAYzQGoMRLQxqeojNr1wAQxAEboVGcRhSSYIzeM7FVuq4a_Ky3yuLS6A0e1oTCncbdSuGZrpcVnratMKLrLXb0i7KtbuwPkq10rWynjK7x4rMqRFfp5hydlKK26mI_T9Dbw_1r9ujNF7OnbDr3ZBDTzisIDVmespKWRQFFHpEyp6kAJksJaSJpmiq2y2gRs0iFpKAURC6YBBXnQNkE3Q29bZ9vVCFV0xlR89ZUG2G-uBYV_5801Yov9ZZTQoFGgSu42RcY_dG7d_BNZaWqa9Eo3VseRwmJ3XCgP4DSaGuNKg-HEOA7F9y54M4FD_nOhdtw_fdqB3z_-S6_GvK17bT5bYtI5Byyb-5MkLo</recordid><startdate>19941201</startdate><enddate>19941201</enddate><creator>Smart, Eric J.</creator><creator>Ying, Yun-Shu</creator><creator>Conrad, Patricia A.</creator><creator>Richard G. W. Anderson</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</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><scope>5PM</scope></search><sort><creationdate>19941201</creationdate><title>Caveolin Moves from Caveolae to the Golgi Apparatus in Response to Cholesterol Oxidation</title><author>Smart, Eric J. ; Ying, Yun-Shu ; Conrad, Patricia A. ; Richard G. W. Anderson</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c472t-d1253b93f2fdd0db61fb29a03cfc098c299e32fdd2d736e51d220aba3c0e7b023</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Biological Transport</topic><topic>Brefeldin A</topic><topic>Caveolae</topic><topic>Caveolin 1</topic><topic>Caveolins</topic><topic>Cell Membrane - metabolism</topic><topic>Cell Membrane - ultrastructure</topic><topic>Cell membranes</topic><topic>Cells</topic><topic>Cells, Cultured</topic><topic>Cholestenones</topic><topic>Cholesterol - metabolism</topic><topic>Cholesterol Oxidase - metabolism</topic><topic>Cholesterols</topic><topic>Cyclopentanes - pharmacology</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Epithelial cells</topic><topic>Fibroblasts</topic><topic>Fluorescent Antibody Technique</topic><topic>Golgi apparatus</topic><topic>Golgi Apparatus - metabolism</topic><topic>Humans</topic><topic>Immunohistochemistry</topic><topic>Membrane Proteins - analysis</topic><topic>Membrane Proteins - metabolism</topic><topic>Oxidases</topic><topic>Oxidation-Reduction</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Smart, Eric J.</creatorcontrib><creatorcontrib>Ying, Yun-Shu</creatorcontrib><creatorcontrib>Conrad, Patricia A.</creatorcontrib><creatorcontrib>Richard G. W. Anderson</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Smart, Eric J.</au><au>Ying, Yun-Shu</au><au>Conrad, Patricia A.</au><au>Richard G. W. Anderson</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Caveolin Moves from Caveolae to the Golgi Apparatus in Response to Cholesterol Oxidation</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>1994-12-01</date><risdate>1994</risdate><volume>127</volume><issue>5</issue><spage>1185</spage><epage>1197</epage><pages>1185-1197</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><abstract>Caveolae are a membrane specialization used to internalize molecules by potocytosis. Caveolin, an integral membrane protein, is associated with the striated coat present on the cytoplasmic surface of the caveolae membrane. We now report that oxidation of caveolar cholesterol with cholesterol oxidase rapidly displaces the caveolin from the plasma membrane to intracellular vesicles that colocalize with Golgi apparatus markers. After the enzyme is removed from the medium, caveolin returns to caveolae. When untreated cells are gently homogenized, caveolin on the plasma membrane is accessible to both anti-caveolin IgG and trypsin. After cholesterol oxidase treatment, however, Golgi-associated caveolin is inaccessible to both of these molecules. Brefeldin A, which inhibits ER to Golgi trafficking, blocks the appearance of caveolin in the Golgi apparatus but does not prevent caveolin from leaving the plasma membrane. Indirect immunogold localization experiments show that in the presence of cholesterol oxidase caveolin leaves the plasma membrane and becomes associated with endoplasmic reticulum and Golgi compartments. Surprisingly, the loss of caveolin from the plasma membrane does not affect the number or morphology of the caveolae.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>7962084</pmid><doi>10.1083/jcb.127.5.1185</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Biological Transport Brefeldin A Caveolae Caveolin 1 Caveolins Cell Membrane - metabolism Cell Membrane - ultrastructure Cell membranes Cells Cells, Cultured Cholestenones Cholesterol - metabolism Cholesterol Oxidase - metabolism Cholesterols Cyclopentanes - pharmacology Endoplasmic Reticulum - metabolism Epithelial cells Fibroblasts Fluorescent Antibody Technique Golgi apparatus Golgi Apparatus - metabolism Humans Immunohistochemistry Membrane Proteins - analysis Membrane Proteins - metabolism Oxidases Oxidation-Reduction Temperature |
title | Caveolin Moves from Caveolae to the Golgi Apparatus in Response to Cholesterol Oxidation |
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