Quantitative Proteomic Analysis of the Adipocyte Plasma Membrane
The adipocyte is a key regulator of mammalian metabolism. To advance our understanding of this important cell, we have used quantitative proteomics to define the protein composition of the adipocyte plasma membrane (PM) in the presence and absence of insulin. Using this approach, we have identified...
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| Veröffentlicht in: | Journal of proteome research 2011-11, Vol.10 (11), p.4970-4982 |
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| container_title | Journal of proteome research |
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| creator | Prior, Matthew J Larance, Mark Lawrence, Robert T Soul, Jamie Humphrey, Sean Burchfield, James Kistler, Carol Davey, Jonathon R La-Borde, Penelope J Buckley, Michael Kanazawa, Hiroshi Parton, Robert G Guilhaus, Michael James, David E |
| description | The adipocyte is a key regulator of mammalian metabolism. To advance our understanding of this important cell, we have used quantitative proteomics to define the protein composition of the adipocyte plasma membrane (PM) in the presence and absence of insulin. Using this approach, we have identified a high confidence list of 486 PM proteins, 52 of which potentially represent novel cell surface proteins, including a member of the adiponectin receptor family and an unusually high number of hydrolases with no known function. Several novel insulin-responsive proteins including the sodium/hydrogen exchanger, NHE6 and the collagens III and VI were also identified, and we provide evidence of PM-ER association suggestive of a unique functional association between these two organelles in the adipocyte. Together these studies provide a wealth of potential therapeutic targets for the manipulation of adipocyte function and a valuable resource for metabolic research and PM biology. |
| doi_str_mv | 10.1021/pr200446r |
| format | Article |
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To advance our understanding of this important cell, we have used quantitative proteomics to define the protein composition of the adipocyte plasma membrane (PM) in the presence and absence of insulin. Using this approach, we have identified a high confidence list of 486 PM proteins, 52 of which potentially represent novel cell surface proteins, including a member of the adiponectin receptor family and an unusually high number of hydrolases with no known function. Several novel insulin-responsive proteins including the sodium/hydrogen exchanger, NHE6 and the collagens III and VI were also identified, and we provide evidence of PM-ER association suggestive of a unique functional association between these two organelles in the adipocyte. Together these studies provide a wealth of potential therapeutic targets for the manipulation of adipocyte function and a valuable resource for metabolic research and PM biology.</description><identifier>ISSN: 1535-3893</identifier><identifier>EISSN: 1535-3907</identifier><identifier>DOI: 10.1021/pr200446r</identifier><identifier>PMID: 21928809</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>3T3-L1 Cells ; Adipocytes - metabolism ; Animals ; Calnexin - isolation & purification ; Calnexin - metabolism ; Caveolin 1 - isolation & purification ; Caveolin 1 - metabolism ; Cell Fractionation ; Cell Membrane - metabolism ; Cell Membrane - ultrastructure ; Endoplasmic Reticulum - metabolism ; Endoplasmic Reticulum - ultrastructure ; Membrane Proteins - isolation & purification ; Membrane Proteins - metabolism ; Mice ; Proteomics ; Qa-SNARE Proteins - isolation & purification ; Qa-SNARE Proteins - metabolism ; Sodium-Hydrogen Exchangers - metabolism ; Syntaxin 16 - isolation & purification ; Syntaxin 16 - metabolism ; Tandem Mass Spectrometry</subject><ispartof>Journal of proteome research, 2011-11, Vol.10 (11), p.4970-4982</ispartof><rights>Copyright © 2011 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a314t-cfe5f9e353bc29453caa0818100aef25576f123e338e592ff930d2275221ca5e3</citedby><cites>FETCH-LOGICAL-a314t-cfe5f9e353bc29453caa0818100aef25576f123e338e592ff930d2275221ca5e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/pr200446r$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/pr200446r$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21928809$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Prior, Matthew J</creatorcontrib><creatorcontrib>Larance, Mark</creatorcontrib><creatorcontrib>Lawrence, Robert T</creatorcontrib><creatorcontrib>Soul, Jamie</creatorcontrib><creatorcontrib>Humphrey, Sean</creatorcontrib><creatorcontrib>Burchfield, James</creatorcontrib><creatorcontrib>Kistler, Carol</creatorcontrib><creatorcontrib>Davey, Jonathon R</creatorcontrib><creatorcontrib>La-Borde, Penelope J</creatorcontrib><creatorcontrib>Buckley, Michael</creatorcontrib><creatorcontrib>Kanazawa, Hiroshi</creatorcontrib><creatorcontrib>Parton, Robert G</creatorcontrib><creatorcontrib>Guilhaus, Michael</creatorcontrib><creatorcontrib>James, David E</creatorcontrib><title>Quantitative Proteomic Analysis of the Adipocyte Plasma Membrane</title><title>Journal of proteome research</title><addtitle>J. Proteome Res</addtitle><description>The adipocyte is a key regulator of mammalian metabolism. To advance our understanding of this important cell, we have used quantitative proteomics to define the protein composition of the adipocyte plasma membrane (PM) in the presence and absence of insulin. Using this approach, we have identified a high confidence list of 486 PM proteins, 52 of which potentially represent novel cell surface proteins, including a member of the adiponectin receptor family and an unusually high number of hydrolases with no known function. Several novel insulin-responsive proteins including the sodium/hydrogen exchanger, NHE6 and the collagens III and VI were also identified, and we provide evidence of PM-ER association suggestive of a unique functional association between these two organelles in the adipocyte. Together these studies provide a wealth of potential therapeutic targets for the manipulation of adipocyte function and a valuable resource for metabolic research and PM biology.</description><subject>3T3-L1 Cells</subject><subject>Adipocytes - metabolism</subject><subject>Animals</subject><subject>Calnexin - isolation & purification</subject><subject>Calnexin - metabolism</subject><subject>Caveolin 1 - isolation & purification</subject><subject>Caveolin 1 - metabolism</subject><subject>Cell Fractionation</subject><subject>Cell Membrane - metabolism</subject><subject>Cell Membrane - ultrastructure</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Endoplasmic Reticulum - ultrastructure</subject><subject>Membrane Proteins - isolation & purification</subject><subject>Membrane Proteins - metabolism</subject><subject>Mice</subject><subject>Proteomics</subject><subject>Qa-SNARE Proteins - isolation & purification</subject><subject>Qa-SNARE Proteins - metabolism</subject><subject>Sodium-Hydrogen Exchangers - metabolism</subject><subject>Syntaxin 16 - isolation & purification</subject><subject>Syntaxin 16 - metabolism</subject><subject>Tandem Mass Spectrometry</subject><issn>1535-3893</issn><issn>1535-3907</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0EtLAzEUhuEgiq3VhX9AZiPiYvQkmXQmO0vxBhUVdB3S9ARTZpoxyQj99470snKVLB4-Di8h5xRuKDB62wYGUBTjcECGVHCRcwnl4e5fST4gJzEuAagogR-TAaOSVRXIIbl77_QquaST-8HsLfiEvnEmm6x0vY4uZt5m6QuzycK13qxTb2odG529YDMPeoWn5MjqOuLZ9h2Rz4f7j-lTPnt9fJ5OZrnmtEi5sSisRC743DBZCG60hopWFECjZUKUY0sZR84rFJJZKzksGCsFY9RogXxErja7bfDfHcakGhcN1nV_g--iksA4k32FXl5vpAk-xoBWtcE1OqwVBfXXS-179fZiu9rNG1zs5S5QDy43QJuolr4LfZf4z9Avq-dwkg</recordid><startdate>20111104</startdate><enddate>20111104</enddate><creator>Prior, Matthew J</creator><creator>Larance, Mark</creator><creator>Lawrence, Robert T</creator><creator>Soul, Jamie</creator><creator>Humphrey, Sean</creator><creator>Burchfield, James</creator><creator>Kistler, Carol</creator><creator>Davey, Jonathon R</creator><creator>La-Borde, Penelope J</creator><creator>Buckley, Michael</creator><creator>Kanazawa, Hiroshi</creator><creator>Parton, Robert G</creator><creator>Guilhaus, Michael</creator><creator>James, David E</creator><general>American Chemical 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>20111104</creationdate><title>Quantitative Proteomic Analysis of the Adipocyte Plasma Membrane</title><author>Prior, Matthew J ; Larance, Mark ; Lawrence, Robert T ; Soul, Jamie ; Humphrey, Sean ; Burchfield, James ; Kistler, Carol ; Davey, Jonathon R ; La-Borde, Penelope J ; Buckley, Michael ; Kanazawa, Hiroshi ; Parton, Robert G ; Guilhaus, Michael ; James, David E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a314t-cfe5f9e353bc29453caa0818100aef25576f123e338e592ff930d2275221ca5e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>3T3-L1 Cells</topic><topic>Adipocytes - metabolism</topic><topic>Animals</topic><topic>Calnexin - isolation & purification</topic><topic>Calnexin - metabolism</topic><topic>Caveolin 1 - isolation & purification</topic><topic>Caveolin 1 - metabolism</topic><topic>Cell Fractionation</topic><topic>Cell Membrane - metabolism</topic><topic>Cell Membrane - ultrastructure</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Endoplasmic Reticulum - ultrastructure</topic><topic>Membrane Proteins - isolation & purification</topic><topic>Membrane Proteins - metabolism</topic><topic>Mice</topic><topic>Proteomics</topic><topic>Qa-SNARE Proteins - isolation & purification</topic><topic>Qa-SNARE Proteins - metabolism</topic><topic>Sodium-Hydrogen Exchangers - metabolism</topic><topic>Syntaxin 16 - isolation & purification</topic><topic>Syntaxin 16 - metabolism</topic><topic>Tandem Mass Spectrometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Prior, Matthew J</creatorcontrib><creatorcontrib>Larance, Mark</creatorcontrib><creatorcontrib>Lawrence, Robert T</creatorcontrib><creatorcontrib>Soul, Jamie</creatorcontrib><creatorcontrib>Humphrey, Sean</creatorcontrib><creatorcontrib>Burchfield, James</creatorcontrib><creatorcontrib>Kistler, Carol</creatorcontrib><creatorcontrib>Davey, Jonathon R</creatorcontrib><creatorcontrib>La-Borde, Penelope J</creatorcontrib><creatorcontrib>Buckley, Michael</creatorcontrib><creatorcontrib>Kanazawa, Hiroshi</creatorcontrib><creatorcontrib>Parton, Robert G</creatorcontrib><creatorcontrib>Guilhaus, Michael</creatorcontrib><creatorcontrib>James, David E</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>Journal of proteome research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Prior, Matthew J</au><au>Larance, Mark</au><au>Lawrence, Robert T</au><au>Soul, Jamie</au><au>Humphrey, Sean</au><au>Burchfield, James</au><au>Kistler, Carol</au><au>Davey, Jonathon R</au><au>La-Borde, Penelope J</au><au>Buckley, Michael</au><au>Kanazawa, Hiroshi</au><au>Parton, Robert G</au><au>Guilhaus, Michael</au><au>James, David E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Quantitative Proteomic Analysis of the Adipocyte Plasma Membrane</atitle><jtitle>Journal of proteome research</jtitle><addtitle>J. Proteome Res</addtitle><date>2011-11-04</date><risdate>2011</risdate><volume>10</volume><issue>11</issue><spage>4970</spage><epage>4982</epage><pages>4970-4982</pages><issn>1535-3893</issn><eissn>1535-3907</eissn><abstract>The adipocyte is a key regulator of mammalian metabolism. To advance our understanding of this important cell, we have used quantitative proteomics to define the protein composition of the adipocyte plasma membrane (PM) in the presence and absence of insulin. Using this approach, we have identified a high confidence list of 486 PM proteins, 52 of which potentially represent novel cell surface proteins, including a member of the adiponectin receptor family and an unusually high number of hydrolases with no known function. 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| source | MEDLINE; American Chemical Society Journals |
| subjects | 3T3-L1 Cells Adipocytes - metabolism Animals Calnexin - isolation & purification Calnexin - metabolism Caveolin 1 - isolation & purification Caveolin 1 - metabolism Cell Fractionation Cell Membrane - metabolism Cell Membrane - ultrastructure Endoplasmic Reticulum - metabolism Endoplasmic Reticulum - ultrastructure Membrane Proteins - isolation & purification Membrane Proteins - metabolism Mice Proteomics Qa-SNARE Proteins - isolation & purification Qa-SNARE Proteins - metabolism Sodium-Hydrogen Exchangers - metabolism Syntaxin 16 - isolation & purification Syntaxin 16 - metabolism Tandem Mass Spectrometry |
| title | Quantitative Proteomic Analysis of the Adipocyte Plasma Membrane |
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