Members of the VAMP family of synaptic vesicle proteins are components of glucose transporter-containing vesicles from rat adipocytes
Existing data support the hypothesis that insulin triggers the exocytosis of small vesicles containing the GluT4 isoform of the glucose transporter. The data also suggest that these vesicles reform through endocytosis of GluT4. These processes resemble those described for synaptic vesicles after dep...
Gespeichert in:
| Veröffentlicht in: | The Journal of biological chemistry 1992-06, Vol.267 (17), p.11681-11684 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 11684 |
|---|---|
| container_issue | 17 |
| container_start_page | 11681 |
| container_title | The Journal of biological chemistry |
| container_volume | 267 |
| creator | CORLEY CAIN, C TRIMBLE, W. S LIENHARD, G. E |
| description | Existing data support the hypothesis that insulin triggers the exocytosis of small vesicles containing the GluT4 isoform of
the glucose transporter. The data also suggest that these vesicles reform through endocytosis of GluT4. These processes resemble
those described for synaptic vesicles after depolarization of nerve cells. To determine whether GluT4 vesicles are related
to synaptic vesicles, rat adipocyte low density microsomes (LDM), which are rich in GluT4 vesicles, were screened for the
synaptic vesicle proteins synaptotagmin, synaptophysin, SV2, p29, rab3, and VAMP (synaptobrevin) by immunoblotting. Two polypeptides
that reacted with antibodies against the VAMPs were identified, one with the same apparent size as the two isoforms of VAMP
in the brain (18 kDa) and one that was slightly smaller (17 kDa). These members of the VAMP family were highly enriched in
GluT4 vesicles isolated by immunoadsorption and translocated from the LDM to the plasma membrane in response to insulin. With
the exception of rab3, which was observed in the LDM but was not localized in the GluT4 vesicles, the other synaptic vesicle
proteins were not detected. The presence of the VAMPs in both GluT4 and synaptic vesicles suggests that the genesis and/or
exocytosis of these two types of vesicles involve shared processes. |
| doi_str_mv | 10.1016/S0021-9258(19)49748-2 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_highwire_biochem_267_17_11681</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>72997147</sourcerecordid><originalsourceid>FETCH-LOGICAL-c440t-2b9e78677a0c4071eb289ec8717d47d115bf19f9af6d35f7b3a217626808236f3</originalsourceid><addsrcrecordid>eNqFkduKFDEQhhtR1nH1ERZyIaIXral0OofLZVkPsIuCB7wL6XRlJtLdaZOMMg_ge9tzcPfSEAikvr-K5KuqC6CvgYJ485lSBrVmrXoJ-hXXkquaPahWQFVTNy18f1it7pDH1ZOcf9BlcQ1n1RkICoqzVfXnFscOUybRk7JB8u3y9hPxdgzDbn-Vd5OdS3DkF-bgBiRzigXDlIlNSFwc5zjhVA7x9bB1MSMpyU55jqlgql2cig1TmNb_OmTiUxxJsoXYPszR7Qrmp9Ujb4eMz07nefX17fWXq_f1zcd3H64ub2rHOS016zRKJaS01HEqATumNDolQfZc9gBt50F7bb3om9bLrrEMpGBCUcUa4Zvz6sWx7_KMn1vMxYwhOxwGO2HcZiOZ1hK4_C8IouGcQ7OA7RF0Keac0Js5hdGmnQFq9p7MwZPZSzCgzcGTYUvu4jRg243Y36eOYpb681PdZmcHv_ypC_kOa7nQUsh7bBPWm98hoelCdBscDRPSwLJBKGj-Ai5vqGk</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16344413</pqid></control><display><type>article</type><title>Members of the VAMP family of synaptic vesicle proteins are components of glucose transporter-containing vesicles from rat adipocytes</title><source>MEDLINE</source><source>Alma/SFX Local Collection</source><source>EZB Electronic Journals Library</source><creator>CORLEY CAIN, C ; TRIMBLE, W. S ; LIENHARD, G. E</creator><creatorcontrib>CORLEY CAIN, C ; TRIMBLE, W. S ; LIENHARD, G. E</creatorcontrib><description>Existing data support the hypothesis that insulin triggers the exocytosis of small vesicles containing the GluT4 isoform of
the glucose transporter. The data also suggest that these vesicles reform through endocytosis of GluT4. These processes resemble
those described for synaptic vesicles after depolarization of nerve cells. To determine whether GluT4 vesicles are related
to synaptic vesicles, rat adipocyte low density microsomes (LDM), which are rich in GluT4 vesicles, were screened for the
synaptic vesicle proteins synaptotagmin, synaptophysin, SV2, p29, rab3, and VAMP (synaptobrevin) by immunoblotting. Two polypeptides
that reacted with antibodies against the VAMPs were identified, one with the same apparent size as the two isoforms of VAMP
in the brain (18 kDa) and one that was slightly smaller (17 kDa). These members of the VAMP family were highly enriched in
GluT4 vesicles isolated by immunoadsorption and translocated from the LDM to the plasma membrane in response to insulin. With
the exception of rab3, which was observed in the LDM but was not localized in the GluT4 vesicles, the other synaptic vesicle
proteins were not detected. The presence of the VAMPs in both GluT4 and synaptic vesicles suggests that the genesis and/or
exocytosis of these two types of vesicles involve shared processes.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)49748-2</identifier><identifier>PMID: 1601842</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>adipocytes ; Adipose Tissue - chemistry ; Adipose Tissue - cytology ; Adipose Tissue - metabolism ; Animals ; Biological and medical sciences ; Cell Membrane - drug effects ; Cell Membrane - metabolism ; Cell physiology ; Electrophoresis, Polyacrylamide Gel ; Exocytosis ; Fundamental and applied biological sciences. Psychology ; glucose transporter ; Glucose Transporter Type 4 ; Insulin - pharmacology ; Membrane and intracellular transports ; Membrane Proteins - analysis ; Membrane Proteins - metabolism ; Microsomes - chemistry ; Microsomes - metabolism ; Molecular and cellular biology ; Monosaccharide Transport Proteins - chemistry ; Monosaccharide Transport Proteins - metabolism ; Muscle Proteins ; Nerve Tissue Proteins - analysis ; Nerve Tissue Proteins - metabolism ; R-SNARE Proteins ; Rats ; Rats, Inbred Strains ; synapses ; Synaptic Vesicles - chemistry ; Synaptic Vesicles - metabolism ; vesicle-associated membrane protein ; vesicles</subject><ispartof>The Journal of biological chemistry, 1992-06, Vol.267 (17), p.11681-11684</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c440t-2b9e78677a0c4071eb289ec8717d47d115bf19f9af6d35f7b3a217626808236f3</citedby><cites>FETCH-LOGICAL-c440t-2b9e78677a0c4071eb289ec8717d47d115bf19f9af6d35f7b3a217626808236f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5469767$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1601842$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>CORLEY CAIN, C</creatorcontrib><creatorcontrib>TRIMBLE, W. S</creatorcontrib><creatorcontrib>LIENHARD, G. E</creatorcontrib><title>Members of the VAMP family of synaptic vesicle proteins are components of glucose transporter-containing vesicles from rat adipocytes</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Existing data support the hypothesis that insulin triggers the exocytosis of small vesicles containing the GluT4 isoform of
the glucose transporter. The data also suggest that these vesicles reform through endocytosis of GluT4. These processes resemble
those described for synaptic vesicles after depolarization of nerve cells. To determine whether GluT4 vesicles are related
to synaptic vesicles, rat adipocyte low density microsomes (LDM), which are rich in GluT4 vesicles, were screened for the
synaptic vesicle proteins synaptotagmin, synaptophysin, SV2, p29, rab3, and VAMP (synaptobrevin) by immunoblotting. Two polypeptides
that reacted with antibodies against the VAMPs were identified, one with the same apparent size as the two isoforms of VAMP
in the brain (18 kDa) and one that was slightly smaller (17 kDa). These members of the VAMP family were highly enriched in
GluT4 vesicles isolated by immunoadsorption and translocated from the LDM to the plasma membrane in response to insulin. With
the exception of rab3, which was observed in the LDM but was not localized in the GluT4 vesicles, the other synaptic vesicle
proteins were not detected. The presence of the VAMPs in both GluT4 and synaptic vesicles suggests that the genesis and/or
exocytosis of these two types of vesicles involve shared processes.</description><subject>adipocytes</subject><subject>Adipose Tissue - chemistry</subject><subject>Adipose Tissue - cytology</subject><subject>Adipose Tissue - metabolism</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cell Membrane - drug effects</subject><subject>Cell Membrane - metabolism</subject><subject>Cell physiology</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Exocytosis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>glucose transporter</subject><subject>Glucose Transporter Type 4</subject><subject>Insulin - pharmacology</subject><subject>Membrane and intracellular transports</subject><subject>Membrane Proteins - analysis</subject><subject>Membrane Proteins - metabolism</subject><subject>Microsomes - chemistry</subject><subject>Microsomes - metabolism</subject><subject>Molecular and cellular biology</subject><subject>Monosaccharide Transport Proteins - chemistry</subject><subject>Monosaccharide Transport Proteins - metabolism</subject><subject>Muscle Proteins</subject><subject>Nerve Tissue Proteins - analysis</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>R-SNARE Proteins</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>synapses</subject><subject>Synaptic Vesicles - chemistry</subject><subject>Synaptic Vesicles - metabolism</subject><subject>vesicle-associated membrane protein</subject><subject>vesicles</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkduKFDEQhhtR1nH1ERZyIaIXral0OofLZVkPsIuCB7wL6XRlJtLdaZOMMg_ge9tzcPfSEAikvr-K5KuqC6CvgYJ485lSBrVmrXoJ-hXXkquaPahWQFVTNy18f1it7pDH1ZOcf9BlcQ1n1RkICoqzVfXnFscOUybRk7JB8u3y9hPxdgzDbn-Vd5OdS3DkF-bgBiRzigXDlIlNSFwc5zjhVA7x9bB1MSMpyU55jqlgql2cig1TmNb_OmTiUxxJsoXYPszR7Qrmp9Ujb4eMz07nefX17fWXq_f1zcd3H64ub2rHOS016zRKJaS01HEqATumNDolQfZc9gBt50F7bb3om9bLrrEMpGBCUcUa4Zvz6sWx7_KMn1vMxYwhOxwGO2HcZiOZ1hK4_C8IouGcQ7OA7RF0Keac0Js5hdGmnQFq9p7MwZPZSzCgzcGTYUvu4jRg243Y36eOYpb681PdZmcHv_ypC_kOa7nQUsh7bBPWm98hoelCdBscDRPSwLJBKGj-Ai5vqGk</recordid><startdate>19920615</startdate><enddate>19920615</enddate><creator>CORLEY CAIN, C</creator><creator>TRIMBLE, W. S</creator><creator>LIENHARD, G. E</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>IQODW</scope><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>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19920615</creationdate><title>Members of the VAMP family of synaptic vesicle proteins are components of glucose transporter-containing vesicles from rat adipocytes</title><author>CORLEY CAIN, C ; TRIMBLE, W. S ; LIENHARD, G. E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c440t-2b9e78677a0c4071eb289ec8717d47d115bf19f9af6d35f7b3a217626808236f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>adipocytes</topic><topic>Adipose Tissue - chemistry</topic><topic>Adipose Tissue - cytology</topic><topic>Adipose Tissue - metabolism</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cell Membrane - drug effects</topic><topic>Cell Membrane - metabolism</topic><topic>Cell physiology</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Exocytosis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>glucose transporter</topic><topic>Glucose Transporter Type 4</topic><topic>Insulin - pharmacology</topic><topic>Membrane and intracellular transports</topic><topic>Membrane Proteins - analysis</topic><topic>Membrane Proteins - metabolism</topic><topic>Microsomes - chemistry</topic><topic>Microsomes - metabolism</topic><topic>Molecular and cellular biology</topic><topic>Monosaccharide Transport Proteins - chemistry</topic><topic>Monosaccharide Transport Proteins - metabolism</topic><topic>Muscle Proteins</topic><topic>Nerve Tissue Proteins - analysis</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>R-SNARE Proteins</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>synapses</topic><topic>Synaptic Vesicles - chemistry</topic><topic>Synaptic Vesicles - metabolism</topic><topic>vesicle-associated membrane protein</topic><topic>vesicles</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>CORLEY CAIN, C</creatorcontrib><creatorcontrib>TRIMBLE, W. S</creatorcontrib><creatorcontrib>LIENHARD, G. E</creatorcontrib><collection>Pascal-Francis</collection><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>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering 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>CORLEY CAIN, C</au><au>TRIMBLE, W. S</au><au>LIENHARD, G. E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Members of the VAMP family of synaptic vesicle proteins are components of glucose transporter-containing vesicles from rat adipocytes</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-06-15</date><risdate>1992</risdate><volume>267</volume><issue>17</issue><spage>11681</spage><epage>11684</epage><pages>11681-11684</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Existing data support the hypothesis that insulin triggers the exocytosis of small vesicles containing the GluT4 isoform of
the glucose transporter. The data also suggest that these vesicles reform through endocytosis of GluT4. These processes resemble
those described for synaptic vesicles after depolarization of nerve cells. To determine whether GluT4 vesicles are related
to synaptic vesicles, rat adipocyte low density microsomes (LDM), which are rich in GluT4 vesicles, were screened for the
synaptic vesicle proteins synaptotagmin, synaptophysin, SV2, p29, rab3, and VAMP (synaptobrevin) by immunoblotting. Two polypeptides
that reacted with antibodies against the VAMPs were identified, one with the same apparent size as the two isoforms of VAMP
in the brain (18 kDa) and one that was slightly smaller (17 kDa). These members of the VAMP family were highly enriched in
GluT4 vesicles isolated by immunoadsorption and translocated from the LDM to the plasma membrane in response to insulin. With
the exception of rab3, which was observed in the LDM but was not localized in the GluT4 vesicles, the other synaptic vesicle
proteins were not detected. The presence of the VAMPs in both GluT4 and synaptic vesicles suggests that the genesis and/or
exocytosis of these two types of vesicles involve shared processes.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1601842</pmid><doi>10.1016/S0021-9258(19)49748-2</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1992-06, Vol.267 (17), p.11681-11684 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_highwire_biochem_267_17_11681 |
| source | MEDLINE; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | adipocytes Adipose Tissue - chemistry Adipose Tissue - cytology Adipose Tissue - metabolism Animals Biological and medical sciences Cell Membrane - drug effects Cell Membrane - metabolism Cell physiology Electrophoresis, Polyacrylamide Gel Exocytosis Fundamental and applied biological sciences. Psychology glucose transporter Glucose Transporter Type 4 Insulin - pharmacology Membrane and intracellular transports Membrane Proteins - analysis Membrane Proteins - metabolism Microsomes - chemistry Microsomes - metabolism Molecular and cellular biology Monosaccharide Transport Proteins - chemistry Monosaccharide Transport Proteins - metabolism Muscle Proteins Nerve Tissue Proteins - analysis Nerve Tissue Proteins - metabolism R-SNARE Proteins Rats Rats, Inbred Strains synapses Synaptic Vesicles - chemistry Synaptic Vesicles - metabolism vesicle-associated membrane protein vesicles |
| title | Members of the VAMP family of synaptic vesicle proteins are components of glucose transporter-containing vesicles from rat adipocytes |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-07T16%3A49%3A50IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Members%20of%20the%20VAMP%20family%20of%20synaptic%20vesicle%20proteins%20are%20components%20of%20glucose%20transporter-containing%20vesicles%20from%20rat%20adipocytes&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=CORLEY%20CAIN,%20C&rft.date=1992-06-15&rft.volume=267&rft.issue=17&rft.spage=11681&rft.epage=11684&rft.pages=11681-11684&rft.issn=0021-9258&rft.eissn=1083-351X&rft.coden=JBCHA3&rft_id=info:doi/10.1016/S0021-9258(19)49748-2&rft_dat=%3Cproquest_cross%3E72997147%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=16344413&rft_id=info:pmid/1601842&rfr_iscdi=true |