GLUT4 Overexpression or Deficiency in Adipocytes of Transgenic Mice Alters the Composition of GLUT4 Vesicles and the Subcellular Localization of GLUT4 and Insulin-responsive Aminopeptidase
The majority of GLUT4 is sequestered in unique intracellular vesicles in the absence of insulin. Upon insulin stimulation GLUT4 vesicles translocate to, and fuse with, the plasma membrane. To determine the effect of GLUT4 content on the distribution and subcellular trafficking of GLUT4 and other ves...
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| Veröffentlicht in: | The Journal of biological chemistry 2004-05, Vol.279 (20), p.21598-21605 |
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| container_title | The Journal of biological chemistry |
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| creator | Carvalho, Eugenia Schellhorn, Sarah E Zabolotny, Janice M Martin, Sally Tozzo, Effie Peroni, Odile D Houseknecht, Karen L Mundt, Adrian James, David E Kahn, Barbara B |
| description | The majority of GLUT4 is sequestered in unique intracellular vesicles in the absence of insulin. Upon insulin stimulation
GLUT4 vesicles translocate to, and fuse with, the plasma membrane. To determine the effect of GLUT4 content on the distribution
and subcellular trafficking of GLUT4 and other vesicle proteins, adipocytes of adipose-specific, GLUT4-deficient (aP2-GLUT4-/-)
mice and adipose-specific, GLUT4-overexpressing (aP2-GLUT4-Tg) mice were studied. GLUT4 amount was reduced by 80-95% in aP2-GLUT4-/-
adipocytes and increased â¼10-fold in aP2-GLUT4-Tg adipocytes compared with controls. Insulin-responsive aminopeptidase (IRAP)
protein amount was decreased 35% in aP2-GLUT4-/- adipocytes and increased 45% in aP2-GLUT4-Tg adipocytes. VAMP2 protein was
also decreased by 60% in aP2-GLUT4-/- adipocytes and increased 2-fold in aP2-GLUT4-Tg adipocytes. IRAP and VAMP2 mRNA levels
were unaffected in aP2-GLUT4-Tg, suggesting that overexpression of GLUT4 affects IRAP and VAMP2 protein stability. The amount
and subcellular distribution of syntaxin4, SNAP23, Munc-18c, and GLUT1 were unchanged in either aP2-GLUT4-/- or aP2-GLUT4-Tg
adipocytes, but transferrin receptor was partially redistributed to the plasma membrane in aP2-GLUT4-Tg adipocytes. Immunogold
electron microscopy revealed that overexpression of GLUT4 in adipocytes increased the number of GLUT4 molecules per vesicle
nearly 2-fold and the number of GLUT4 and IRAP-containing vesicles per cell 3-fold. In addition, the proportion of cellular
GLUT4 and IRAP at the plasma membrane in unstimulated aP2-GLUT4-Tg adipocytes was increased 4- and 2-fold, respectively, suggesting
that sequestration of GLUT4 and IRAP is saturable. Our results show that GLUT4 overexpression or deficiency affects the amount
of other GLUT4-vesicle proteins including IRAP and VAMP2 and that GLUT4 sequestration is saturable. |
| doi_str_mv | 10.1074/jbc.M312269200 |
| format | Article |
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GLUT4 vesicles translocate to, and fuse with, the plasma membrane. To determine the effect of GLUT4 content on the distribution
and subcellular trafficking of GLUT4 and other vesicle proteins, adipocytes of adipose-specific, GLUT4-deficient (aP2-GLUT4-/-)
mice and adipose-specific, GLUT4-overexpressing (aP2-GLUT4-Tg) mice were studied. GLUT4 amount was reduced by 80-95% in aP2-GLUT4-/-
adipocytes and increased â¼10-fold in aP2-GLUT4-Tg adipocytes compared with controls. Insulin-responsive aminopeptidase (IRAP)
protein amount was decreased 35% in aP2-GLUT4-/- adipocytes and increased 45% in aP2-GLUT4-Tg adipocytes. VAMP2 protein was
also decreased by 60% in aP2-GLUT4-/- adipocytes and increased 2-fold in aP2-GLUT4-Tg adipocytes. IRAP and VAMP2 mRNA levels
were unaffected in aP2-GLUT4-Tg, suggesting that overexpression of GLUT4 affects IRAP and VAMP2 protein stability. The amount
and subcellular distribution of syntaxin4, SNAP23, Munc-18c, and GLUT1 were unchanged in either aP2-GLUT4-/- or aP2-GLUT4-Tg
adipocytes, but transferrin receptor was partially redistributed to the plasma membrane in aP2-GLUT4-Tg adipocytes. Immunogold
electron microscopy revealed that overexpression of GLUT4 in adipocytes increased the number of GLUT4 molecules per vesicle
nearly 2-fold and the number of GLUT4 and IRAP-containing vesicles per cell 3-fold. In addition, the proportion of cellular
GLUT4 and IRAP at the plasma membrane in unstimulated aP2-GLUT4-Tg adipocytes was increased 4- and 2-fold, respectively, suggesting
that sequestration of GLUT4 and IRAP is saturable. Our results show that GLUT4 overexpression or deficiency affects the amount
of other GLUT4-vesicle proteins including IRAP and VAMP2 and that GLUT4 sequestration is saturable.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M312269200</identifier><identifier>PMID: 14985357</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Adipocytes - drug effects ; Adipocytes - physiology ; Aminopeptidases - metabolism ; Animals ; Biological Transport ; Cystinyl Aminopeptidase ; Glucose - metabolism ; Glucose Transporter Type 4 ; Insulin - pharmacology ; Kinetics ; Membrane Proteins - metabolism ; Mice ; Mice, Knockout ; Mice, Transgenic ; Monosaccharide Transport Proteins - deficiency ; Monosaccharide Transport Proteins - genetics ; Monosaccharide Transport Proteins - metabolism ; Muscle Proteins ; R-SNARE Proteins ; Subcellular Fractions - metabolism</subject><ispartof>The Journal of biological chemistry, 2004-05, Vol.279 (20), p.21598-21605</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c391t-188ced171db2ecc9d764d365b78e6ae1fd5d067df86ee7c2d9dec893a781b06a3</citedby><cites>FETCH-LOGICAL-c391t-188ced171db2ecc9d764d365b78e6ae1fd5d067df86ee7c2d9dec893a781b06a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14985357$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Carvalho, Eugenia</creatorcontrib><creatorcontrib>Schellhorn, Sarah E</creatorcontrib><creatorcontrib>Zabolotny, Janice M</creatorcontrib><creatorcontrib>Martin, Sally</creatorcontrib><creatorcontrib>Tozzo, Effie</creatorcontrib><creatorcontrib>Peroni, Odile D</creatorcontrib><creatorcontrib>Houseknecht, Karen L</creatorcontrib><creatorcontrib>Mundt, Adrian</creatorcontrib><creatorcontrib>James, David E</creatorcontrib><creatorcontrib>Kahn, Barbara B</creatorcontrib><title>GLUT4 Overexpression or Deficiency in Adipocytes of Transgenic Mice Alters the Composition of GLUT4 Vesicles and the Subcellular Localization of GLUT4 and Insulin-responsive Aminopeptidase</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The majority of GLUT4 is sequestered in unique intracellular vesicles in the absence of insulin. Upon insulin stimulation
GLUT4 vesicles translocate to, and fuse with, the plasma membrane. To determine the effect of GLUT4 content on the distribution
and subcellular trafficking of GLUT4 and other vesicle proteins, adipocytes of adipose-specific, GLUT4-deficient (aP2-GLUT4-/-)
mice and adipose-specific, GLUT4-overexpressing (aP2-GLUT4-Tg) mice were studied. GLUT4 amount was reduced by 80-95% in aP2-GLUT4-/-
adipocytes and increased â¼10-fold in aP2-GLUT4-Tg adipocytes compared with controls. Insulin-responsive aminopeptidase (IRAP)
protein amount was decreased 35% in aP2-GLUT4-/- adipocytes and increased 45% in aP2-GLUT4-Tg adipocytes. VAMP2 protein was
also decreased by 60% in aP2-GLUT4-/- adipocytes and increased 2-fold in aP2-GLUT4-Tg adipocytes. IRAP and VAMP2 mRNA levels
were unaffected in aP2-GLUT4-Tg, suggesting that overexpression of GLUT4 affects IRAP and VAMP2 protein stability. The amount
and subcellular distribution of syntaxin4, SNAP23, Munc-18c, and GLUT1 were unchanged in either aP2-GLUT4-/- or aP2-GLUT4-Tg
adipocytes, but transferrin receptor was partially redistributed to the plasma membrane in aP2-GLUT4-Tg adipocytes. Immunogold
electron microscopy revealed that overexpression of GLUT4 in adipocytes increased the number of GLUT4 molecules per vesicle
nearly 2-fold and the number of GLUT4 and IRAP-containing vesicles per cell 3-fold. In addition, the proportion of cellular
GLUT4 and IRAP at the plasma membrane in unstimulated aP2-GLUT4-Tg adipocytes was increased 4- and 2-fold, respectively, suggesting
that sequestration of GLUT4 and IRAP is saturable. Our results show that GLUT4 overexpression or deficiency affects the amount
of other GLUT4-vesicle proteins including IRAP and VAMP2 and that GLUT4 sequestration is saturable.</description><subject>Adipocytes - drug effects</subject><subject>Adipocytes - physiology</subject><subject>Aminopeptidases - metabolism</subject><subject>Animals</subject><subject>Biological Transport</subject><subject>Cystinyl Aminopeptidase</subject><subject>Glucose - metabolism</subject><subject>Glucose Transporter Type 4</subject><subject>Insulin - pharmacology</subject><subject>Kinetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Mice, Transgenic</subject><subject>Monosaccharide Transport Proteins - deficiency</subject><subject>Monosaccharide Transport Proteins - genetics</subject><subject>Monosaccharide Transport Proteins - metabolism</subject><subject>Muscle Proteins</subject><subject>R-SNARE Proteins</subject><subject>Subcellular Fractions - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1DAURi0EokNhyxJ5gdhl8E8S28vRFEqlqbpgithZjn3TcZXYwU4Kw7PxcGQ6I1Ws8OZuzneurz6E3lKypESUH-8bu7zmlLFaMUKeoQUlkhe8ot-fowUhjBaKVfIMvcr5nsyvVPQlOqOlkhWvxAL9udzcbkt88wAJfg0JcvYx4JjwBbTeegh2j33AK-eHaPcjZBxbvE0m5DsI3uJrbwGvuhFSxuMO8Dr2Q8x-fLS0-Gj_Btnbbs6a4B6pr1NjoeumziS8idZ0_rf5N3Igr0KeOh-K-VdDDNk_zJt6H-IAw-idyfAavWhNl-HNaZ6j28-ftusvxebm8mq92hSWKzoWVEoLjgrqGgbWKifq0vG6aoSE2gBtXeVILVwrawBhmVMOrFTcCEkbUht-jj4cvUOKPybIo-59PhxgAsQpa0EVVaqU_wWpUEIoyWZweQRtijknaPWQfG_SXlOiD8XquVj9VOwceHcyT00P7gk_NTkD74_Azt_tfvoEuvHR7qDXTCjNiGa0UpL_Bcw7rmU</recordid><startdate>20040514</startdate><enddate>20040514</enddate><creator>Carvalho, Eugenia</creator><creator>Schellhorn, Sarah E</creator><creator>Zabolotny, Janice M</creator><creator>Martin, Sally</creator><creator>Tozzo, Effie</creator><creator>Peroni, Odile D</creator><creator>Houseknecht, Karen L</creator><creator>Mundt, Adrian</creator><creator>James, David E</creator><creator>Kahn, Barbara B</creator><general>American Society for Biochemistry and Molecular Biology</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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20040514</creationdate><title>GLUT4 Overexpression or Deficiency in Adipocytes of Transgenic Mice Alters the Composition of GLUT4 Vesicles and the Subcellular Localization of GLUT4 and Insulin-responsive Aminopeptidase</title><author>Carvalho, Eugenia ; Schellhorn, Sarah E ; Zabolotny, Janice M ; Martin, Sally ; Tozzo, Effie ; Peroni, Odile D ; Houseknecht, Karen L ; Mundt, Adrian ; James, David E ; Kahn, Barbara B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c391t-188ced171db2ecc9d764d365b78e6ae1fd5d067df86ee7c2d9dec893a781b06a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Adipocytes - drug effects</topic><topic>Adipocytes - physiology</topic><topic>Aminopeptidases - metabolism</topic><topic>Animals</topic><topic>Biological Transport</topic><topic>Cystinyl Aminopeptidase</topic><topic>Glucose - metabolism</topic><topic>Glucose Transporter Type 4</topic><topic>Insulin - pharmacology</topic><topic>Kinetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>Mice, Transgenic</topic><topic>Monosaccharide Transport Proteins - deficiency</topic><topic>Monosaccharide Transport Proteins - genetics</topic><topic>Monosaccharide Transport Proteins - metabolism</topic><topic>Muscle Proteins</topic><topic>R-SNARE Proteins</topic><topic>Subcellular Fractions - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Carvalho, Eugenia</creatorcontrib><creatorcontrib>Schellhorn, Sarah E</creatorcontrib><creatorcontrib>Zabolotny, Janice M</creatorcontrib><creatorcontrib>Martin, Sally</creatorcontrib><creatorcontrib>Tozzo, Effie</creatorcontrib><creatorcontrib>Peroni, Odile D</creatorcontrib><creatorcontrib>Houseknecht, Karen L</creatorcontrib><creatorcontrib>Mundt, Adrian</creatorcontrib><creatorcontrib>James, David E</creatorcontrib><creatorcontrib>Kahn, Barbara B</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Carvalho, Eugenia</au><au>Schellhorn, Sarah E</au><au>Zabolotny, Janice M</au><au>Martin, Sally</au><au>Tozzo, Effie</au><au>Peroni, Odile D</au><au>Houseknecht, Karen L</au><au>Mundt, Adrian</au><au>James, David E</au><au>Kahn, Barbara B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>GLUT4 Overexpression or Deficiency in Adipocytes of Transgenic Mice Alters the Composition of GLUT4 Vesicles and the Subcellular Localization of GLUT4 and Insulin-responsive Aminopeptidase</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2004-05-14</date><risdate>2004</risdate><volume>279</volume><issue>20</issue><spage>21598</spage><epage>21605</epage><pages>21598-21605</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The majority of GLUT4 is sequestered in unique intracellular vesicles in the absence of insulin. Upon insulin stimulation
GLUT4 vesicles translocate to, and fuse with, the plasma membrane. To determine the effect of GLUT4 content on the distribution
and subcellular trafficking of GLUT4 and other vesicle proteins, adipocytes of adipose-specific, GLUT4-deficient (aP2-GLUT4-/-)
mice and adipose-specific, GLUT4-overexpressing (aP2-GLUT4-Tg) mice were studied. GLUT4 amount was reduced by 80-95% in aP2-GLUT4-/-
adipocytes and increased â¼10-fold in aP2-GLUT4-Tg adipocytes compared with controls. Insulin-responsive aminopeptidase (IRAP)
protein amount was decreased 35% in aP2-GLUT4-/- adipocytes and increased 45% in aP2-GLUT4-Tg adipocytes. VAMP2 protein was
also decreased by 60% in aP2-GLUT4-/- adipocytes and increased 2-fold in aP2-GLUT4-Tg adipocytes. IRAP and VAMP2 mRNA levels
were unaffected in aP2-GLUT4-Tg, suggesting that overexpression of GLUT4 affects IRAP and VAMP2 protein stability. The amount
and subcellular distribution of syntaxin4, SNAP23, Munc-18c, and GLUT1 were unchanged in either aP2-GLUT4-/- or aP2-GLUT4-Tg
adipocytes, but transferrin receptor was partially redistributed to the plasma membrane in aP2-GLUT4-Tg adipocytes. Immunogold
electron microscopy revealed that overexpression of GLUT4 in adipocytes increased the number of GLUT4 molecules per vesicle
nearly 2-fold and the number of GLUT4 and IRAP-containing vesicles per cell 3-fold. In addition, the proportion of cellular
GLUT4 and IRAP at the plasma membrane in unstimulated aP2-GLUT4-Tg adipocytes was increased 4- and 2-fold, respectively, suggesting
that sequestration of GLUT4 and IRAP is saturable. Our results show that GLUT4 overexpression or deficiency affects the amount
of other GLUT4-vesicle proteins including IRAP and VAMP2 and that GLUT4 sequestration is saturable.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>14985357</pmid><doi>10.1074/jbc.M312269200</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 2004-05, Vol.279 (20), p.21598-21605 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_71919948 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Adipocytes - drug effects Adipocytes - physiology Aminopeptidases - metabolism Animals Biological Transport Cystinyl Aminopeptidase Glucose - metabolism Glucose Transporter Type 4 Insulin - pharmacology Kinetics Membrane Proteins - metabolism Mice Mice, Knockout Mice, Transgenic Monosaccharide Transport Proteins - deficiency Monosaccharide Transport Proteins - genetics Monosaccharide Transport Proteins - metabolism Muscle Proteins R-SNARE Proteins Subcellular Fractions - metabolism |
| title | GLUT4 Overexpression or Deficiency in Adipocytes of Transgenic Mice Alters the Composition of GLUT4 Vesicles and the Subcellular Localization of GLUT4 and Insulin-responsive Aminopeptidase |
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