Myelin Tetraspan Family Proteins but No Non-Tetraspan Family Proteins Are Present in the Ascidian (Ciona intestinalis) Genome
Several of the proteins used to form and maintain myelin sheaths in the central nervous system (CNS) and the peripheral nervous system (PNS) are shared among different vertebrate classes. These proteins include one-to-several alternatively spliced myelin basic protein (MBP) isoforms in all sheaths,...
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| Veröffentlicht in: | The Biological bulletin (Lancaster) 2005-08, Vol.209 (1), p.49-66 |
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| creator | Gould, Robert M. Morrison, Hilary G. Gilland, Edwin Campbell, Robert K. |
| description | Several of the proteins used to form and maintain myelin sheaths in the central nervous system (CNS) and the peripheral nervous system (PNS) are shared among different vertebrate classes. These proteins include one-to-several alternatively spliced myelin basic protein (MBP) isoforms in all sheaths, proteolipid protein (PLP) and DM20 (except in amphibians) in tetrapod CNS sheaths, and one or two protein zero (P0) isoforms in fish CNS and in all vertebrate PNS sheaths. Several other proteins, including 2', 3'-cyclic nucleotide 3'-phosphodiesterase (CNP), myelin and lymphocyte protein (MAL), plasmolipin, and peripheral myelin protein 22 (PMP22; prominent in PNS myelin), are localized to myelin and myelin-associated membranes, though class distributions are less well studied. Databases with known and identified sequences of these proteins from cartilaginous and teleost fishes, amphibians, reptiles, birds, and mammals were prepared and used to search for potential homologs in the basal vertebrate, Ciona intestinalis. Homologs of lipophilin proteins, MAL/plasmolipin, and PMP22 were identified in the Ciona genome. In contrast, no MBP, P0, or CNP homologs were found. These studies provide a framework for understanding how myelin proteins were recruited during evolution and how structural adaptations enabled them to play key roles in myelination. |
| doi_str_mv | 10.2307/3593141 |
| format | Article |
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These proteins include one-to-several alternatively spliced myelin basic protein (MBP) isoforms in all sheaths, proteolipid protein (PLP) and DM20 (except in amphibians) in tetrapod CNS sheaths, and one or two protein zero (P0) isoforms in fish CNS and in all vertebrate PNS sheaths. Several other proteins, including 2', 3'-cyclic nucleotide 3'-phosphodiesterase (CNP), myelin and lymphocyte protein (MAL), plasmolipin, and peripheral myelin protein 22 (PMP22; prominent in PNS myelin), are localized to myelin and myelin-associated membranes, though class distributions are less well studied. Databases with known and identified sequences of these proteins from cartilaginous and teleost fishes, amphibians, reptiles, birds, and mammals were prepared and used to search for potential homologs in the basal vertebrate, Ciona intestinalis. Homologs of lipophilin proteins, MAL/plasmolipin, and PMP22 were identified in the Ciona genome. In contrast, no MBP, P0, or CNP homologs were found. These studies provide a framework for understanding how myelin proteins were recruited during evolution and how structural adaptations enabled them to play key roles in myelination.</description><identifier>ISSN: 0006-3185</identifier><identifier>EISSN: 1939-8697</identifier><identifier>DOI: 10.2307/3593141</identifier><identifier>PMID: 16110093</identifier><language>eng</language><publisher>United States: Marine Biological Laboratory</publisher><subject>Amino Acid Sequence ; Amino acids ; Animals ; Ascidiacea ; Cellular biology ; Central nervous system ; Ciona intestinalis - chemistry ; Ciona intestinalis - genetics ; Gene Expression Profiling ; Genetic aspects ; Genome ; Genomes ; Genomics ; Marine ; Molecular Sequence Data ; Multigene Family ; Myelin ; Myelin proteins ; Myelin Proteins - analysis ; Myelin Proteins - chemistry ; Myelin Proteins - genetics ; Myelin sheath ; Neurobiology and Behavior ; Neurons ; Phylogeny ; Proteins ; Sea squirts ; Sequence Alignment ; Sequence Homology, Amino Acid ; Tunicates ; Vertebrates</subject><ispartof>The Biological bulletin (Lancaster), 2005-08, Vol.209 (1), p.49-66</ispartof><rights>Copyright 2005 Marine Biological Laboratory</rights><rights>COPYRIGHT 2005 University of Chicago Press</rights><rights>Copyright Marine Biological Laboratory Aug 2005</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c642t-7ec15ec72d4564381f8dbac70b46591d812fcbb3563ddc1a90fc9f18a936f4283</citedby><cites>FETCH-LOGICAL-c642t-7ec15ec72d4564381f8dbac70b46591d812fcbb3563ddc1a90fc9f18a936f4283</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3593141$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3593141$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16110093$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gould, Robert M.</creatorcontrib><creatorcontrib>Morrison, Hilary G.</creatorcontrib><creatorcontrib>Gilland, Edwin</creatorcontrib><creatorcontrib>Campbell, Robert K.</creatorcontrib><title>Myelin Tetraspan Family Proteins but No Non-Tetraspan Family Proteins Are Present in the Ascidian (Ciona intestinalis) Genome</title><title>The Biological bulletin (Lancaster)</title><addtitle>Biol Bull</addtitle><description>Several of the proteins used to form and maintain myelin sheaths in the central nervous system (CNS) and the peripheral nervous system (PNS) are shared among different vertebrate classes. These proteins include one-to-several alternatively spliced myelin basic protein (MBP) isoforms in all sheaths, proteolipid protein (PLP) and DM20 (except in amphibians) in tetrapod CNS sheaths, and one or two protein zero (P0) isoforms in fish CNS and in all vertebrate PNS sheaths. Several other proteins, including 2', 3'-cyclic nucleotide 3'-phosphodiesterase (CNP), myelin and lymphocyte protein (MAL), plasmolipin, and peripheral myelin protein 22 (PMP22; prominent in PNS myelin), are localized to myelin and myelin-associated membranes, though class distributions are less well studied. Databases with known and identified sequences of these proteins from cartilaginous and teleost fishes, amphibians, reptiles, birds, and mammals were prepared and used to search for potential homologs in the basal vertebrate, Ciona intestinalis. Homologs of lipophilin proteins, MAL/plasmolipin, and PMP22 were identified in the Ciona genome. In contrast, no MBP, P0, or CNP homologs were found. These studies provide a framework for understanding how myelin proteins were recruited during evolution and how structural adaptations enabled them to play key roles in myelination.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Ascidiacea</subject><subject>Cellular biology</subject><subject>Central nervous system</subject><subject>Ciona intestinalis - chemistry</subject><subject>Ciona intestinalis - genetics</subject><subject>Gene Expression Profiling</subject><subject>Genetic aspects</subject><subject>Genome</subject><subject>Genomes</subject><subject>Genomics</subject><subject>Marine</subject><subject>Molecular Sequence Data</subject><subject>Multigene Family</subject><subject>Myelin</subject><subject>Myelin proteins</subject><subject>Myelin Proteins - analysis</subject><subject>Myelin Proteins - chemistry</subject><subject>Myelin Proteins - genetics</subject><subject>Myelin sheath</subject><subject>Neurobiology and Behavior</subject><subject>Neurons</subject><subject>Phylogeny</subject><subject>Proteins</subject><subject>Sea squirts</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Tunicates</subject><subject>Vertebrates</subject><issn>0006-3185</issn><issn>1939-8697</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqN0luL1DAUAOAiijuu4j-QIt72oWsubdo8DoM7Loy7gutzSNPT2QxpMiYpOA_-dyMdGEZmURIICV9OkpOTZS8xuiQU1R9pxSku8aNshjnlRcN4_TibIYRYQXFTnWXPQtikKSK4fJqdYYYxQpzOsl9fdmC0ze8gehm20uZXctBml3_1LoK2IW_HmN-41G3xMJp7SBMIYGOeosV7yOdB6U4n-2GhnZVpOUKI2kqjw0W-BOsGeJ496aUJ8GI_nmffrz7dLT4Xq9vl9WK-KhQrSSxqULgCVZOurFhJG9w3XStVjdqSVRx3DSa9altaMdp1CkuOesV73EhOWV-Shp5n76a4W-9-jOkaYtBBgTHSghuDYE3Ja8T5PyGuWYURIQm-_gtu3OjT44IgJEVCtEIJFRNaSwNC296l_Kk1WPDSOAu9TstzTBmrSsKq5C9P-NQ6GLQ6ueHiaEMyEX7GtRxDENffbv7bNsvVsS1OWeWMgTWI9DeL22P_fvLKuxA89GLr9SD9TmAk_hSo2Bdokq_2eRvbAbqD21dkAm8nMKp7reTabVNZhUN2D4HeTG4TovMPnvcbck3zMg</recordid><startdate>20050801</startdate><enddate>20050801</enddate><creator>Gould, Robert M.</creator><creator>Morrison, Hilary G.</creator><creator>Gilland, Edwin</creator><creator>Campbell, Robert K.</creator><general>Marine Biological Laboratory</general><general>University of Chicago Press</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>8GL</scope><scope>ISN</scope><scope>3V.</scope><scope>7QG</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TN</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>F1W</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H95</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L.G</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20050801</creationdate><title>Myelin Tetraspan Family Proteins but No Non-Tetraspan Family Proteins Are Present in the Ascidian (Ciona intestinalis) Genome</title><author>Gould, Robert M. ; Morrison, Hilary G. ; Gilland, Edwin ; Campbell, Robert K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c642t-7ec15ec72d4564381f8dbac70b46591d812fcbb3563ddc1a90fc9f18a936f4283</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Ascidiacea</topic><topic>Cellular biology</topic><topic>Central nervous system</topic><topic>Ciona intestinalis - 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Academic</collection><jtitle>The Biological bulletin (Lancaster)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gould, Robert M.</au><au>Morrison, Hilary G.</au><au>Gilland, Edwin</au><au>Campbell, Robert K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Myelin Tetraspan Family Proteins but No Non-Tetraspan Family Proteins Are Present in the Ascidian (Ciona intestinalis) Genome</atitle><jtitle>The Biological bulletin (Lancaster)</jtitle><addtitle>Biol Bull</addtitle><date>2005-08-01</date><risdate>2005</risdate><volume>209</volume><issue>1</issue><spage>49</spage><epage>66</epage><pages>49-66</pages><issn>0006-3185</issn><eissn>1939-8697</eissn><abstract>Several of the proteins used to form and maintain myelin sheaths in the central nervous system (CNS) and the peripheral nervous system (PNS) are shared among different vertebrate classes. These proteins include one-to-several alternatively spliced myelin basic protein (MBP) isoforms in all sheaths, proteolipid protein (PLP) and DM20 (except in amphibians) in tetrapod CNS sheaths, and one or two protein zero (P0) isoforms in fish CNS and in all vertebrate PNS sheaths. Several other proteins, including 2', 3'-cyclic nucleotide 3'-phosphodiesterase (CNP), myelin and lymphocyte protein (MAL), plasmolipin, and peripheral myelin protein 22 (PMP22; prominent in PNS myelin), are localized to myelin and myelin-associated membranes, though class distributions are less well studied. Databases with known and identified sequences of these proteins from cartilaginous and teleost fishes, amphibians, reptiles, birds, and mammals were prepared and used to search for potential homologs in the basal vertebrate, Ciona intestinalis. Homologs of lipophilin proteins, MAL/plasmolipin, and PMP22 were identified in the Ciona genome. In contrast, no MBP, P0, or CNP homologs were found. These studies provide a framework for understanding how myelin proteins were recruited during evolution and how structural adaptations enabled them to play key roles in myelination.</abstract><cop>United States</cop><pub>Marine Biological Laboratory</pub><pmid>16110093</pmid><doi>10.2307/3593141</doi><tpages>18</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; JSTOR Archive Collection A-Z Listing |
| subjects | Amino Acid Sequence Amino acids Animals Ascidiacea Cellular biology Central nervous system Ciona intestinalis - chemistry Ciona intestinalis - genetics Gene Expression Profiling Genetic aspects Genome Genomes Genomics Marine Molecular Sequence Data Multigene Family Myelin Myelin proteins Myelin Proteins - analysis Myelin Proteins - chemistry Myelin Proteins - genetics Myelin sheath Neurobiology and Behavior Neurons Phylogeny Proteins Sea squirts Sequence Alignment Sequence Homology, Amino Acid Tunicates Vertebrates |
| title | Myelin Tetraspan Family Proteins but No Non-Tetraspan Family Proteins Are Present in the Ascidian (Ciona intestinalis) Genome |
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