Characterization of the Shark Myelin Po Protein
Myelin, the insulating sheath made by extensive plasma membrane wrapping, is dependent on the presence of highly adhesive molecules that keep the two sides of the membrane in tight contact. The Po glycoprotein (Po) is the major component of the peripheral nervous system (PNS) myelin of mammals. The...
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| Veröffentlicht in: | Brain, behavior and evolution behavior and evolution, 2008-01, Vol.72 (1), p.48-58 |
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| creator | Rotenstein, L. Herath, K. Gould, R.M. de Bellard, M.E. |
| description | Myelin, the insulating sheath made by extensive plasma membrane wrapping, is dependent on the presence of highly adhesive molecules that keep the two sides of the membrane in tight contact. The Po glycoprotein (Po) is the major component of the peripheral nervous system (PNS) myelin of mammals. The exact role that Po protein has played in the evolution of myelin is still unclear, but several phylogenetic observations suggest that it is a crucial component in the development of myelin as a multi-lamellar membrane structure. Sharks, which appeared in the fossil record about 400 million years ago, are the first fully myelinated organisms. In this study we investigated the expression pattern of shark myelin Po to suggest a way it might have played a role in the evolution of myelin in the central nervous system. We found that sharks have more than two isoforms (32, 28 and 25 kD), and that some of these might not be fully functional because they lack the domains known for Po homophilic adhesion. |
| doi_str_mv | 10.1159/000145717 |
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The Po glycoprotein (Po) is the major component of the peripheral nervous system (PNS) myelin of mammals. The exact role that Po protein has played in the evolution of myelin is still unclear, but several phylogenetic observations suggest that it is a crucial component in the development of myelin as a multi-lamellar membrane structure. Sharks, which appeared in the fossil record about 400 million years ago, are the first fully myelinated organisms. In this study we investigated the expression pattern of shark myelin Po to suggest a way it might have played a role in the evolution of myelin in the central nervous system. We found that sharks have more than two isoforms (32, 28 and 25 kD), and that some of these might not be fully functional because they lack the domains known for Po homophilic adhesion.</description><identifier>ISSN: 0006-8977</identifier><identifier>EISSN: 1421-9743</identifier><identifier>DOI: 10.1159/000145717</identifier><identifier>PMID: 18635929</identifier><identifier>CODEN: BRBEBE</identifier><language>eng</language><publisher>Basel, Switzerland: S. Karger AG</publisher><subject>Amino Acid Sequence ; Animals ; Antibody Specificity ; Blotting, Western ; Central nervous system ; Central Nervous System - chemistry ; Central Nervous System - embryology ; Epitopes - immunology ; Evolution, Molecular ; Glycosylation ; Humans ; Marine ; Molecular Sequence Data ; Molecular Weight ; Myelin P0 Protein - analysis ; Myelin P0 Protein - chemistry ; Myelin P0 Protein - immunology ; Myelin P0 Protein - isolation & purification ; Original Paper ; Peripheral Nervous System - chemistry ; Peripheral Nervous System - embryology ; Protein Isoforms - analysis ; Protein Isoforms - immunology ; Protein Isoforms - isolation & purification ; Protein Processing, Post-Translational ; Protein Structure, Tertiary ; Rabbits ; Sequence Alignment ; Sequence Homology, Amino Acid ; Sharks ; Sharks - embryology ; Sharks - immunology ; Sharks - metabolism ; Species Specificity ; Squalus acanthias - immunology ; Squalus acanthias - metabolism ; Vertebrates - metabolism</subject><ispartof>Brain, behavior and evolution, 2008-01, Vol.72 (1), p.48-58</ispartof><rights>2008 S. Karger AG, Basel</rights><rights>Copyright 2008 S. Karger AG, Basel.</rights><rights>Copyright (c) 2008 S. Karger AG, Basel</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c518t-94b87402577aa3a6f9e40a854d08b3ed0757dea088b5ae5fb9112f7c204bba3</citedby><cites>FETCH-LOGICAL-c518t-94b87402577aa3a6f9e40a854d08b3ed0757dea088b5ae5fb9112f7c204bba3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,2423,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18635929$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rotenstein, L.</creatorcontrib><creatorcontrib>Herath, K.</creatorcontrib><creatorcontrib>Gould, R.M.</creatorcontrib><creatorcontrib>de Bellard, M.E.</creatorcontrib><title>Characterization of the Shark Myelin Po Protein</title><title>Brain, behavior and evolution</title><addtitle>Brain Behav Evol</addtitle><description>Myelin, the insulating sheath made by extensive plasma membrane wrapping, is dependent on the presence of highly adhesive molecules that keep the two sides of the membrane in tight contact. The Po glycoprotein (Po) is the major component of the peripheral nervous system (PNS) myelin of mammals. The exact role that Po protein has played in the evolution of myelin is still unclear, but several phylogenetic observations suggest that it is a crucial component in the development of myelin as a multi-lamellar membrane structure. Sharks, which appeared in the fossil record about 400 million years ago, are the first fully myelinated organisms. In this study we investigated the expression pattern of shark myelin Po to suggest a way it might have played a role in the evolution of myelin in the central nervous system. We found that sharks have more than two isoforms (32, 28 and 25 kD), and that some of these might not be fully functional because they lack the domains known for Po homophilic adhesion.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibody Specificity</subject><subject>Blotting, Western</subject><subject>Central nervous system</subject><subject>Central Nervous System - chemistry</subject><subject>Central Nervous System - embryology</subject><subject>Epitopes - immunology</subject><subject>Evolution, Molecular</subject><subject>Glycosylation</subject><subject>Humans</subject><subject>Marine</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Myelin P0 Protein - analysis</subject><subject>Myelin P0 Protein - chemistry</subject><subject>Myelin P0 Protein - immunology</subject><subject>Myelin P0 Protein - isolation & purification</subject><subject>Original Paper</subject><subject>Peripheral Nervous System - chemistry</subject><subject>Peripheral Nervous System - embryology</subject><subject>Protein Isoforms - analysis</subject><subject>Protein Isoforms - immunology</subject><subject>Protein Isoforms - isolation & purification</subject><subject>Protein Processing, Post-Translational</subject><subject>Protein Structure, Tertiary</subject><subject>Rabbits</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sharks</subject><subject>Sharks - embryology</subject><subject>Sharks - immunology</subject><subject>Sharks - metabolism</subject><subject>Species Specificity</subject><subject>Squalus acanthias - immunology</subject><subject>Squalus acanthias - metabolism</subject><subject>Vertebrates - metabolism</subject><issn>0006-8977</issn><issn>1421-9743</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><recordid>eNqF0c1LwzAUAPAgipvTg3eR4kHwUJekSZNcBBl-geJg3kPaplu2rplJK8y_3kjHpl48hbz88l5eHgCnCF4jRMUQQogIZYjtgT4iGMWCkWQf9EM8jblgrAeOvJ-HLcEEHYIe4mlCBRZ9MBzNlFN5o535VI2xdWTLqJnpaBLii-hlrStTR2MbjZ1ttKmPwUGpKq9PNusATO7v3kaP8fPrw9Po9jnOKeJNLEjGGYGYMqZUotJSaAIVp6SAPEt0ARllhVaQ84wqTctMIIRLlmNIskwlA3DTZV212VIXua4bpyq5cmap3FpaZeTvk9rM5NR-yFCQsND8AFxuEjj73mrfyKXxua4qVWvbepkKwhBO_4cYCsghZQFe_IFz27o6_IHECUYwEYgGdNWh3FnvnS63T0ZQfo9KbkcV7PnPHndyM5sAzjqwUG6q3Q50978AY9eWBg</recordid><startdate>20080101</startdate><enddate>20080101</enddate><creator>Rotenstein, L.</creator><creator>Herath, K.</creator><creator>Gould, R.M.</creator><creator>de Bellard, M.E.</creator><general>S. 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chemistry</topic><topic>Central Nervous System - embryology</topic><topic>Epitopes - immunology</topic><topic>Evolution, Molecular</topic><topic>Glycosylation</topic><topic>Humans</topic><topic>Marine</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Myelin P0 Protein - analysis</topic><topic>Myelin P0 Protein - chemistry</topic><topic>Myelin P0 Protein - immunology</topic><topic>Myelin P0 Protein - isolation & purification</topic><topic>Original Paper</topic><topic>Peripheral Nervous System - chemistry</topic><topic>Peripheral Nervous System - embryology</topic><topic>Protein Isoforms - analysis</topic><topic>Protein Isoforms - immunology</topic><topic>Protein Isoforms - isolation & purification</topic><topic>Protein Processing, Post-Translational</topic><topic>Protein Structure, Tertiary</topic><topic>Rabbits</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sharks</topic><topic>Sharks - embryology</topic><topic>Sharks - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Brain, behavior and evolution</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rotenstein, L.</au><au>Herath, K.</au><au>Gould, R.M.</au><au>de Bellard, M.E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of the Shark Myelin Po Protein</atitle><jtitle>Brain, behavior and evolution</jtitle><addtitle>Brain Behav Evol</addtitle><date>2008-01-01</date><risdate>2008</risdate><volume>72</volume><issue>1</issue><spage>48</spage><epage>58</epage><pages>48-58</pages><issn>0006-8977</issn><eissn>1421-9743</eissn><coden>BRBEBE</coden><abstract>Myelin, the insulating sheath made by extensive plasma membrane wrapping, is dependent on the presence of highly adhesive molecules that keep the two sides of the membrane in tight contact. The Po glycoprotein (Po) is the major component of the peripheral nervous system (PNS) myelin of mammals. The exact role that Po protein has played in the evolution of myelin is still unclear, but several phylogenetic observations suggest that it is a crucial component in the development of myelin as a multi-lamellar membrane structure. Sharks, which appeared in the fossil record about 400 million years ago, are the first fully myelinated organisms. In this study we investigated the expression pattern of shark myelin Po to suggest a way it might have played a role in the evolution of myelin in the central nervous system. We found that sharks have more than two isoforms (32, 28 and 25 kD), and that some of these might not be fully functional because they lack the domains known for Po homophilic adhesion.</abstract><cop>Basel, Switzerland</cop><pub>S. Karger AG</pub><pmid>18635929</pmid><doi>10.1159/000145717</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Animals Antibody Specificity Blotting, Western Central nervous system Central Nervous System - chemistry Central Nervous System - embryology Epitopes - immunology Evolution, Molecular Glycosylation Humans Marine Molecular Sequence Data Molecular Weight Myelin P0 Protein - analysis Myelin P0 Protein - chemistry Myelin P0 Protein - immunology Myelin P0 Protein - isolation & purification Original Paper Peripheral Nervous System - chemistry Peripheral Nervous System - embryology Protein Isoforms - analysis Protein Isoforms - immunology Protein Isoforms - isolation & purification Protein Processing, Post-Translational Protein Structure, Tertiary Rabbits Sequence Alignment Sequence Homology, Amino Acid Sharks Sharks - embryology Sharks - immunology Sharks - metabolism Species Specificity Squalus acanthias - immunology Squalus acanthias - metabolism Vertebrates - metabolism |
| title | Characterization of the Shark Myelin Po Protein |
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