Acylation of the lymphoma transmembrane glycoprotein, GP85, may be required for GP85-ankyrin interaction
The lymphoma plasma membrane glycoprotein, GP85, is a transmembrane glycoprotein that binds directly to ankyrin, a molecule known to link the plasma membrane with the underlying cytoskeleton. In this study, we have demonstrated that palmitic acid is incorporated into GP85 in vivo and that the amount...
Gespeichert in:
| Veröffentlicht in: | The Journal of biological chemistry 1991-06, Vol.266 (18), p.11761-11765 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 11765 |
|---|---|
| container_issue | 18 |
| container_start_page | 11761 |
| container_title | The Journal of biological chemistry |
| container_volume | 266 |
| creator | BOURGUIGNON, L. Y. W KALOMIRIS, E. L LOKESHWAR, V. B |
| description | The lymphoma plasma membrane glycoprotein, GP85, is a transmembrane glycoprotein that binds directly to ankyrin, a molecule
known to link the plasma membrane with the underlying cytoskeleton. In this study, we have demonstrated that palmitic acid
is incorporated into GP85 in vivo and that the amount of palmitic acid incorporated is greatly stimulated during lymphoma
cap formation. The majority of the incorporated palmitic acid appears to be strongly linked to GP85 since it is not dissociated
by strong detergents (e.g. sodium dodecyl sulfate) or by chloroform/methanol extraction, but is labile to alkaline or acid
hydrolysis. Furthermore, we have established that deacylation of GP85 (i.e. removal of the palmitic acid moiety from GP85
by 1 M hydroxylamine treatment) significantly reduces the binding affinity between GP85 and ankyrin, and reacylation of GP85
restores the binding affinity. These findings suggest that fatty acid acylation of GP85 by palmitic acid may be required for
the stable attachment of the cytoskeleton to the lymphoma plasma membrane. |
| doi_str_mv | 10.1016/S0021-9258(18)99022-8 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_80620981</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>80620981</sourcerecordid><originalsourceid>FETCH-LOGICAL-c440t-98a93badc9684f0a234e36350db3c3372d776aabb507fe31ca3906731e6d73cf3</originalsourceid><addsrcrecordid>eNqFUU1v1TAQtBCoPAo_oZIPCIHUgNdOHPtYVVCQKoEESNwsx9k0hjh-tfOE8u_x-1B7ZC97mNmd3RlCLoC9Bwbyw3fGOFSaN-otqHdaM84r9YRsgClRiQZ-PSWbB8pz8iLn36xUreGMnIHiSjG5IeOVWye7-DjTONBlRDqtYTvGYOmS7JwDhq50pHfT6uI2xQX9fElvvqnmkga70g5pwvudT9jTIaYDUtn5z5r8TP28YLJuv_4leTbYKeOrUz8nPz99_HH9ubr9evPl-uq2cnXNlkorq0Vne6elqgdmuahRSNGwvhNOiJb3bSut7bqGtQMKcFZoJlsBKPtWuEGckzfHveXW-x3mxQSfHU5TeSLusilfc6YV_JcIEhgvgoXYHIkuxZwTDmabfLBpNcDMPgpziMLsfTagzCEKo8rcxUlg1wXsH6eO3hf89Qm32dlpKDY7nx9otW7KBfUjbfR349_is-l8dCMGw6Xc6wG0EsQ_LvGcpA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16102372</pqid></control><display><type>article</type><title>Acylation of the lymphoma transmembrane glycoprotein, GP85, may be required for GP85-ankyrin interaction</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>BOURGUIGNON, L. Y. W ; KALOMIRIS, E. L ; LOKESHWAR, V. B</creator><creatorcontrib>BOURGUIGNON, L. Y. W ; KALOMIRIS, E. L ; LOKESHWAR, V. B</creatorcontrib><description>The lymphoma plasma membrane glycoprotein, GP85, is a transmembrane glycoprotein that binds directly to ankyrin, a molecule
known to link the plasma membrane with the underlying cytoskeleton. In this study, we have demonstrated that palmitic acid
is incorporated into GP85 in vivo and that the amount of palmitic acid incorporated is greatly stimulated during lymphoma
cap formation. The majority of the incorporated palmitic acid appears to be strongly linked to GP85 since it is not dissociated
by strong detergents (e.g. sodium dodecyl sulfate) or by chloroform/methanol extraction, but is labile to alkaline or acid
hydrolysis. Furthermore, we have established that deacylation of GP85 (i.e. removal of the palmitic acid moiety from GP85
by 1 M hydroxylamine treatment) significantly reduces the binding affinity between GP85 and ankyrin, and reacylation of GP85
restores the binding affinity. These findings suggest that fatty acid acylation of GP85 by palmitic acid may be required for
the stable attachment of the cytoskeleton to the lymphoma plasma membrane.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)99022-8</identifier><identifier>PMID: 1828806</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; ankyrin ; Ankyrins ; Biological and medical sciences ; Blood Proteins - isolation & purification ; Blood Proteins - metabolism ; Chromatography, High Pressure Liquid ; Electrophoresis, Gel, Two-Dimensional ; Electrophoresis, Polyacrylamide Gel ; Fatty Acids - metabolism ; Fundamental and applied biological sciences. Psychology ; glycoprotein GP85 ; Glycoproteins ; Lymphoma - metabolism ; Membrane Glycoproteins - metabolism ; Membrane Proteins - isolation & purification ; Membrane Proteins - metabolism ; Mice ; Palmitic Acid ; Palmitic Acids - chemistry ; Proteins ; Tumor Cells, Cultured</subject><ispartof>The Journal of biological chemistry, 1991-06, Vol.266 (18), p.11761-11765</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c440t-98a93badc9684f0a234e36350db3c3372d776aabb507fe31ca3906731e6d73cf3</citedby><cites>FETCH-LOGICAL-c440t-98a93badc9684f0a234e36350db3c3372d776aabb507fe31ca3906731e6d73cf3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4956104$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1828806$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>BOURGUIGNON, L. Y. W</creatorcontrib><creatorcontrib>KALOMIRIS, E. L</creatorcontrib><creatorcontrib>LOKESHWAR, V. B</creatorcontrib><title>Acylation of the lymphoma transmembrane glycoprotein, GP85, may be required for GP85-ankyrin interaction</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The lymphoma plasma membrane glycoprotein, GP85, is a transmembrane glycoprotein that binds directly to ankyrin, a molecule
known to link the plasma membrane with the underlying cytoskeleton. In this study, we have demonstrated that palmitic acid
is incorporated into GP85 in vivo and that the amount of palmitic acid incorporated is greatly stimulated during lymphoma
cap formation. The majority of the incorporated palmitic acid appears to be strongly linked to GP85 since it is not dissociated
by strong detergents (e.g. sodium dodecyl sulfate) or by chloroform/methanol extraction, but is labile to alkaline or acid
hydrolysis. Furthermore, we have established that deacylation of GP85 (i.e. removal of the palmitic acid moiety from GP85
by 1 M hydroxylamine treatment) significantly reduces the binding affinity between GP85 and ankyrin, and reacylation of GP85
restores the binding affinity. These findings suggest that fatty acid acylation of GP85 by palmitic acid may be required for
the stable attachment of the cytoskeleton to the lymphoma plasma membrane.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>ankyrin</subject><subject>Ankyrins</subject><subject>Biological and medical sciences</subject><subject>Blood Proteins - isolation & purification</subject><subject>Blood Proteins - metabolism</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fatty Acids - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>glycoprotein GP85</subject><subject>Glycoproteins</subject><subject>Lymphoma - metabolism</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Membrane Proteins - isolation & purification</subject><subject>Membrane Proteins - metabolism</subject><subject>Mice</subject><subject>Palmitic Acid</subject><subject>Palmitic Acids - chemistry</subject><subject>Proteins</subject><subject>Tumor Cells, Cultured</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUU1v1TAQtBCoPAo_oZIPCIHUgNdOHPtYVVCQKoEESNwsx9k0hjh-tfOE8u_x-1B7ZC97mNmd3RlCLoC9Bwbyw3fGOFSaN-otqHdaM84r9YRsgClRiQZ-PSWbB8pz8iLn36xUreGMnIHiSjG5IeOVWye7-DjTONBlRDqtYTvGYOmS7JwDhq50pHfT6uI2xQX9fElvvqnmkga70g5pwvudT9jTIaYDUtn5z5r8TP28YLJuv_4leTbYKeOrUz8nPz99_HH9ubr9evPl-uq2cnXNlkorq0Vne6elqgdmuahRSNGwvhNOiJb3bSut7bqGtQMKcFZoJlsBKPtWuEGckzfHveXW-x3mxQSfHU5TeSLusilfc6YV_JcIEhgvgoXYHIkuxZwTDmabfLBpNcDMPgpziMLsfTagzCEKo8rcxUlg1wXsH6eO3hf89Qm32dlpKDY7nx9otW7KBfUjbfR349_is-l8dCMGw6Xc6wG0EsQ_LvGcpA</recordid><startdate>19910625</startdate><enddate>19910625</enddate><creator>BOURGUIGNON, L. Y. W</creator><creator>KALOMIRIS, E. L</creator><creator>LOKESHWAR, V. B</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>19910625</creationdate><title>Acylation of the lymphoma transmembrane glycoprotein, GP85, may be required for GP85-ankyrin interaction</title><author>BOURGUIGNON, L. Y. W ; KALOMIRIS, E. L ; LOKESHWAR, V. B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c440t-98a93badc9684f0a234e36350db3c3372d776aabb507fe31ca3906731e6d73cf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>ankyrin</topic><topic>Ankyrins</topic><topic>Biological and medical sciences</topic><topic>Blood Proteins - isolation & purification</topic><topic>Blood Proteins - metabolism</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fatty Acids - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>glycoprotein GP85</topic><topic>Glycoproteins</topic><topic>Lymphoma - metabolism</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Membrane Proteins - isolation & purification</topic><topic>Membrane Proteins - metabolism</topic><topic>Mice</topic><topic>Palmitic Acid</topic><topic>Palmitic Acids - chemistry</topic><topic>Proteins</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>BOURGUIGNON, L. Y. W</creatorcontrib><creatorcontrib>KALOMIRIS, E. L</creatorcontrib><creatorcontrib>LOKESHWAR, V. B</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>BOURGUIGNON, L. Y. W</au><au>KALOMIRIS, E. L</au><au>LOKESHWAR, V. B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Acylation of the lymphoma transmembrane glycoprotein, GP85, may be required for GP85-ankyrin interaction</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1991-06-25</date><risdate>1991</risdate><volume>266</volume><issue>18</issue><spage>11761</spage><epage>11765</epage><pages>11761-11765</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The lymphoma plasma membrane glycoprotein, GP85, is a transmembrane glycoprotein that binds directly to ankyrin, a molecule
known to link the plasma membrane with the underlying cytoskeleton. In this study, we have demonstrated that palmitic acid
is incorporated into GP85 in vivo and that the amount of palmitic acid incorporated is greatly stimulated during lymphoma
cap formation. The majority of the incorporated palmitic acid appears to be strongly linked to GP85 since it is not dissociated
by strong detergents (e.g. sodium dodecyl sulfate) or by chloroform/methanol extraction, but is labile to alkaline or acid
hydrolysis. Furthermore, we have established that deacylation of GP85 (i.e. removal of the palmitic acid moiety from GP85
by 1 M hydroxylamine treatment) significantly reduces the binding affinity between GP85 and ankyrin, and reacylation of GP85
restores the binding affinity. These findings suggest that fatty acid acylation of GP85 by palmitic acid may be required for
the stable attachment of the cytoskeleton to the lymphoma plasma membrane.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1828806</pmid><doi>10.1016/S0021-9258(18)99022-8</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1991-06, Vol.266 (18), p.11761-11765 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80620981 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Analytical, structural and metabolic biochemistry Animals ankyrin Ankyrins Biological and medical sciences Blood Proteins - isolation & purification Blood Proteins - metabolism Chromatography, High Pressure Liquid Electrophoresis, Gel, Two-Dimensional Electrophoresis, Polyacrylamide Gel Fatty Acids - metabolism Fundamental and applied biological sciences. Psychology glycoprotein GP85 Glycoproteins Lymphoma - metabolism Membrane Glycoproteins - metabolism Membrane Proteins - isolation & purification Membrane Proteins - metabolism Mice Palmitic Acid Palmitic Acids - chemistry Proteins Tumor Cells, Cultured |
| title | Acylation of the lymphoma transmembrane glycoprotein, GP85, may be required for GP85-ankyrin interaction |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-28T04%3A03%3A45IST&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=Acylation%20of%20the%20lymphoma%20transmembrane%20glycoprotein,%20GP85,%20may%20be%20required%20for%20GP85-ankyrin%20interaction&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=BOURGUIGNON,%20L.%20Y.%20W&rft.date=1991-06-25&rft.volume=266&rft.issue=18&rft.spage=11761&rft.epage=11765&rft.pages=11761-11765&rft.issn=0021-9258&rft.eissn=1083-351X&rft.coden=JBCHA3&rft_id=info:doi/10.1016/S0021-9258(18)99022-8&rft_dat=%3Cproquest_cross%3E80620981%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=16102372&rft_id=info:pmid/1828806&rfr_iscdi=true |