Evidence for possible interactions between PLP and DM20 within the myelin sheath
PLP and its smaller DM20 isoform constitute the major proteins of CNS myelin. Previous studies indicated a role for the proteins in maintaining the intraperiod line of the myelin sheath and the integrity of axons and suggested that both isoforms were necessary to provide these functions. The present...
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| Veröffentlicht in: | Glia 2002-07, Vol.39 (1), p.31-36 |
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| creator | McLaughlin, M. Hunter, D.J.B. Thomson, C.E. Yool, D. Kirkham, D. Freer, A.A. Griffiths, I.R. |
| description | PLP and its smaller DM20 isoform constitute the major proteins of CNS myelin. Previous studies indicated a role for the proteins in maintaining the intraperiod line of the myelin sheath and the integrity of axons and suggested that both isoforms were necessary to provide these functions. The present study shows that each isoform is capable individually of inserting into compact myelin. Employing chromatographic extraction procedures designed to maintain the natural conformation of the proteins we found that most PLP and DM20 remained associated. Using an antibody specific to the PLP isoform, we were able to co‐immunoprecipitate DM20 from the major fraction of the extracted equine myelin and from mouse native whole myelin. We suggest that PLP and DM20 may form a hetero‐oligomeric complex within the myelin sheath, probably in association with specific lipids and that this arrangement is essential for the normal structure of myelin and axons. GLIA 39:31–36, 2002. © 2002 Wiley‐Liss, Inc. |
| doi_str_mv | 10.1002/glia.10091 |
| format | Article |
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Previous studies indicated a role for the proteins in maintaining the intraperiod line of the myelin sheath and the integrity of axons and suggested that both isoforms were necessary to provide these functions. The present study shows that each isoform is capable individually of inserting into compact myelin. Employing chromatographic extraction procedures designed to maintain the natural conformation of the proteins we found that most PLP and DM20 remained associated. Using an antibody specific to the PLP isoform, we were able to co‐immunoprecipitate DM20 from the major fraction of the extracted equine myelin and from mouse native whole myelin. We suggest that PLP and DM20 may form a hetero‐oligomeric complex within the myelin sheath, probably in association with specific lipids and that this arrangement is essential for the normal structure of myelin and axons. 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Neuroglia ; Male ; Mice ; Mice, Knockout ; Mice, Transgenic ; Myelin Proteolipid Protein - deficiency ; Myelin Proteolipid Protein - genetics ; Myelin Proteolipid Protein - metabolism ; Myelin Sheath - genetics ; Myelin Sheath - metabolism ; Nerve Tissue Proteins ; Protein Isoforms - genetics ; Protein Isoforms - metabolism ; transgenic complementation ; Vertebrates: nervous system and sense organs</subject><ispartof>Glia, 2002-07, Vol.39 (1), p.31-36</ispartof><rights>Copyright © 2002 Wiley‐Liss, Inc.</rights><rights>2002 INIST-CNRS</rights><rights>Copyright 2002 Wiley-Liss, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4241-9d19fdde7aafaa923a2d1352a53e3fe3e3c46589785fb7502442e3c1620bc5963</citedby><cites>FETCH-LOGICAL-c4241-9d19fdde7aafaa923a2d1352a53e3fe3e3c46589785fb7502442e3c1620bc5963</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fglia.10091$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fglia.10091$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=13742566$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12112373$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>McLaughlin, M.</creatorcontrib><creatorcontrib>Hunter, D.J.B.</creatorcontrib><creatorcontrib>Thomson, C.E.</creatorcontrib><creatorcontrib>Yool, D.</creatorcontrib><creatorcontrib>Kirkham, D.</creatorcontrib><creatorcontrib>Freer, A.A.</creatorcontrib><creatorcontrib>Griffiths, I.R.</creatorcontrib><title>Evidence for possible interactions between PLP and DM20 within the myelin sheath</title><title>Glia</title><addtitle>Glia</addtitle><description>PLP and its smaller DM20 isoform constitute the major proteins of CNS myelin. Previous studies indicated a role for the proteins in maintaining the intraperiod line of the myelin sheath and the integrity of axons and suggested that both isoforms were necessary to provide these functions. The present study shows that each isoform is capable individually of inserting into compact myelin. Employing chromatographic extraction procedures designed to maintain the natural conformation of the proteins we found that most PLP and DM20 remained associated. Using an antibody specific to the PLP isoform, we were able to co‐immunoprecipitate DM20 from the major fraction of the extracted equine myelin and from mouse native whole myelin. We suggest that PLP and DM20 may form a hetero‐oligomeric complex within the myelin sheath, probably in association with specific lipids and that this arrangement is essential for the normal structure of myelin and axons. GLIA 39:31–36, 2002. © 2002 Wiley‐Liss, Inc.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Brain - metabolism</subject><subject>co-immunoprecipitation</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Horses</subject><subject>intraperiod line</subject><subject>Isolated neuron and nerve. Neuroglia</subject><subject>Male</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Mice, Transgenic</subject><subject>Myelin Proteolipid Protein - deficiency</subject><subject>Myelin Proteolipid Protein - genetics</subject><subject>Myelin Proteolipid Protein - metabolism</subject><subject>Myelin Sheath - genetics</subject><subject>Myelin Sheath - metabolism</subject><subject>Nerve Tissue Proteins</subject><subject>Protein Isoforms - genetics</subject><subject>Protein Isoforms - metabolism</subject><subject>transgenic complementation</subject><subject>Vertebrates: nervous system and sense organs</subject><issn>0894-1491</issn><issn>1098-1136</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1v1DAQQC0EotvChR-AfIEDUlqPP-L4WJWyVF1KhECVuFiOM2EN2WRrZ7vsvydhF3qDiz0zejOjeYS8AHYKjPGzb21wU2TgEZkBM0UGIPLHZMYKIzOQBo7IcUrfGYMx0U_JEXAALrSYkfLyPtTYeaRNH-m6TylULdLQDRidH0LfJVrhsEXsaLkoqetq-vYDZ3QbhmXo6LBEutphO4ZpiW5YPiNPGtcmfH74T8iXd5efL95ni4_zq4vzReYll5CZGkxT16ida5wzXDheg1DcKYGiwfHxMleF0YVqKq0Yl5KPNcg5q7wyuTghr_dz17G_22Aa7Cokj23rOuw3yWowTHIm_gtCoYpR1wS-2YM-jhoiNnYdw8rFnQVmJ9F2Em1_ix7hl4epm2qF9QN6MDsCrw6AS961TXSdD-mBE1pylU93wJ7bhhZ3_1hp54ur8z_Ls31PSAP-_Nvj4g-ba6GVvb2Z29syF18_ldpei18OfqLl</recordid><startdate>200207</startdate><enddate>200207</enddate><creator>McLaughlin, M.</creator><creator>Hunter, D.J.B.</creator><creator>Thomson, C.E.</creator><creator>Yool, D.</creator><creator>Kirkham, D.</creator><creator>Freer, A.A.</creator><creator>Griffiths, I.R.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley-Liss</general><scope>BSCLL</scope><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>7TK</scope><scope>7X8</scope></search><sort><creationdate>200207</creationdate><title>Evidence for possible interactions between PLP and DM20 within the myelin sheath</title><author>McLaughlin, M. ; Hunter, D.J.B. ; Thomson, C.E. ; Yool, D. ; Kirkham, D. ; Freer, A.A. ; Griffiths, I.R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4241-9d19fdde7aafaa923a2d1352a53e3fe3e3c46589785fb7502442e3c1620bc5963</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Brain - metabolism</topic><topic>co-immunoprecipitation</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Horses</topic><topic>intraperiod line</topic><topic>Isolated neuron and nerve. Neuroglia</topic><topic>Male</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>Mice, Transgenic</topic><topic>Myelin Proteolipid Protein - deficiency</topic><topic>Myelin Proteolipid Protein - genetics</topic><topic>Myelin Proteolipid Protein - metabolism</topic><topic>Myelin Sheath - genetics</topic><topic>Myelin Sheath - metabolism</topic><topic>Nerve Tissue Proteins</topic><topic>Protein Isoforms - genetics</topic><topic>Protein Isoforms - metabolism</topic><topic>transgenic complementation</topic><topic>Vertebrates: nervous system and sense organs</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>McLaughlin, M.</creatorcontrib><creatorcontrib>Hunter, D.J.B.</creatorcontrib><creatorcontrib>Thomson, C.E.</creatorcontrib><creatorcontrib>Yool, D.</creatorcontrib><creatorcontrib>Kirkham, D.</creatorcontrib><creatorcontrib>Freer, A.A.</creatorcontrib><creatorcontrib>Griffiths, I.R.</creatorcontrib><collection>Istex</collection><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>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Glia</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>McLaughlin, M.</au><au>Hunter, D.J.B.</au><au>Thomson, C.E.</au><au>Yool, D.</au><au>Kirkham, D.</au><au>Freer, A.A.</au><au>Griffiths, I.R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evidence for possible interactions between PLP and DM20 within the myelin sheath</atitle><jtitle>Glia</jtitle><addtitle>Glia</addtitle><date>2002-07</date><risdate>2002</risdate><volume>39</volume><issue>1</issue><spage>31</spage><epage>36</epage><pages>31-36</pages><issn>0894-1491</issn><eissn>1098-1136</eissn><coden>GLIAEJ</coden><abstract>PLP and its smaller DM20 isoform constitute the major proteins of CNS myelin. Previous studies indicated a role for the proteins in maintaining the intraperiod line of the myelin sheath and the integrity of axons and suggested that both isoforms were necessary to provide these functions. The present study shows that each isoform is capable individually of inserting into compact myelin. Employing chromatographic extraction procedures designed to maintain the natural conformation of the proteins we found that most PLP and DM20 remained associated. Using an antibody specific to the PLP isoform, we were able to co‐immunoprecipitate DM20 from the major fraction of the extracted equine myelin and from mouse native whole myelin. We suggest that PLP and DM20 may form a hetero‐oligomeric complex within the myelin sheath, probably in association with specific lipids and that this arrangement is essential for the normal structure of myelin and axons. GLIA 39:31–36, 2002. © 2002 Wiley‐Liss, Inc.</abstract><cop>New York</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>12112373</pmid><doi>10.1002/glia.10091</doi><tpages>6</tpages></addata></record> |
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| subjects | Animals Biological and medical sciences Brain - metabolism co-immunoprecipitation Female Fundamental and applied biological sciences. Psychology Horses intraperiod line Isolated neuron and nerve. Neuroglia Male Mice Mice, Knockout Mice, Transgenic Myelin Proteolipid Protein - deficiency Myelin Proteolipid Protein - genetics Myelin Proteolipid Protein - metabolism Myelin Sheath - genetics Myelin Sheath - metabolism Nerve Tissue Proteins Protein Isoforms - genetics Protein Isoforms - metabolism transgenic complementation Vertebrates: nervous system and sense organs |
| title | Evidence for possible interactions between PLP and DM20 within the myelin sheath |
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