Ezrin and moesin expression within the developing human cerebrum and tuberous sclerosis-associated cortical tubers
The ERM (ezrin, radixin, and moesin) proteins belong to the band-4.1 superfamily of membrane-cytoskeleton-linking proteins which bind to the actin cytoskeleton via their C-terminal sequences and bind ERM binding membrane proteins (ERMBMPs). We investigated the immunohistochemical expression of two o...
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| Veröffentlicht in: | Acta neuropathologica 2002-08, Vol.104 (2), p.188-196 |
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| description | The ERM (ezrin, radixin, and moesin) proteins belong to the band-4.1 superfamily of membrane-cytoskeleton-linking proteins which bind to the actin cytoskeleton via their C-terminal sequences and bind ERM binding membrane proteins (ERMBMPs). We investigated the immunohistochemical expression of two of the ERM proteins (ezrin and moesin) in developing human cerebral cortex and in cortical tubers from patients with tuberous sclerosis (TSC), to assess possible consequences of TSC gene product malfunction or inactivation in the developing brain in relation to ERM protein expression. Ezrin is abundantly expressed within radial glia and migrating cells in the intermediate zone in the prenatal human cerebrum, while moesin is primarily expressed in vascular endothelial cells in developing and adult human brain and scattered microglia in adult brain. In addition, both ezrin and moesin are abundantly co-expressed with hamartin and tuberin within a population of abnormal cells in TSC-associated cortical tubers. The expression of these two proteins--primarily ezrin--suggests that they are developmentally regulated and abundantly expressed in germinal matrix and/or migrating cells during cerebral cortical development. In TSC-associated cortical tubers, both proteins appeared to be up-regulated and are co-localized within a population of abnormal neuroglial cells typical of those seen in tubers. Expression of these proteins and their co-localization with tuberin and hamartin in these cells may suggest a compensatory up-regulation in response to TSC gene mutation. |
| doi_str_mv | 10.1007/s00401-002-0540-x |
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We investigated the immunohistochemical expression of two of the ERM proteins (ezrin and moesin) in developing human cerebral cortex and in cortical tubers from patients with tuberous sclerosis (TSC), to assess possible consequences of TSC gene product malfunction or inactivation in the developing brain in relation to ERM protein expression. Ezrin is abundantly expressed within radial glia and migrating cells in the intermediate zone in the prenatal human cerebrum, while moesin is primarily expressed in vascular endothelial cells in developing and adult human brain and scattered microglia in adult brain. In addition, both ezrin and moesin are abundantly co-expressed with hamartin and tuberin within a population of abnormal cells in TSC-associated cortical tubers. The expression of these two proteins--primarily ezrin--suggests that they are developmentally regulated and abundantly expressed in germinal matrix and/or migrating cells during cerebral cortical development. In TSC-associated cortical tubers, both proteins appeared to be up-regulated and are co-localized within a population of abnormal neuroglial cells typical of those seen in tubers. Expression of these proteins and their co-localization with tuberin and hamartin in these cells may suggest a compensatory up-regulation in response to TSC gene mutation.</description><identifier>ISSN: 0001-6322</identifier><identifier>EISSN: 1432-0533</identifier><identifier>DOI: 10.1007/s00401-002-0540-x</identifier><identifier>PMID: 12111362</identifier><identifier>CODEN: ANPTAL</identifier><language>eng</language><publisher>Berlin: Springer</publisher><subject>Actin ; Biological and medical sciences ; Brain research ; Cell cycle ; Cerebral cortex ; Cerebrum ; Cloning ; Cytoskeletal Proteins ; Cytoskeleton ; Endothelial cells ; ERM protein ; Ezrin ; Genes ; Glial cells ; Glial Fibrillary Acidic Protein - analysis ; Glial Fibrillary Acidic Protein - biosynthesis ; Humans ; Immunohistochemistry ; Infant ; Infant, Newborn ; Laboratories ; Localization ; Medical sciences ; Membrane proteins ; Microfilament Proteins - analysis ; Microfilament Proteins - biosynthesis ; Microglia ; Moesin ; Monoclonal antibodies ; Mutation ; Neurology ; Neuropathology ; Phosphoproteins - analysis ; Phosphoproteins - biosynthesis ; Point mutation ; Protein expression ; Proteins ; Radial glial cells ; Radixin ; Repressor Proteins - analysis ; Repressor Proteins - biosynthesis ; Telencephalon - abnormalities ; Telencephalon - metabolism ; Telencephalon - pathology ; Tuberous sclerosis ; Tuberous Sclerosis - pathology ; Tuberous Sclerosis Complex 1 ; Tuberous Sclerosis Complex 2 ; Tumor Suppressor Proteins ; Tumors of the nervous system. Phacomatoses</subject><ispartof>Acta neuropathologica, 2002-08, Vol.104 (2), p.188-196</ispartof><rights>2002 INIST-CNRS</rights><rights>Springer-Verlag 2002.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c421t-c53fcaf0d2ab1749ce1d285664078820c083d077829339a5281650e346ae4d193</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=13956395$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12111362$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>JOHNSON, Michael W</creatorcontrib><creatorcontrib>MIYATA, Hajime</creatorcontrib><creatorcontrib>VINTERS, Harry V</creatorcontrib><title>Ezrin and moesin expression within the developing human cerebrum and tuberous sclerosis-associated cortical tubers</title><title>Acta neuropathologica</title><addtitle>Acta Neuropathol</addtitle><description>The ERM (ezrin, radixin, and moesin) proteins belong to the band-4.1 superfamily of membrane-cytoskeleton-linking proteins which bind to the actin cytoskeleton via their C-terminal sequences and bind ERM binding membrane proteins (ERMBMPs). We investigated the immunohistochemical expression of two of the ERM proteins (ezrin and moesin) in developing human cerebral cortex and in cortical tubers from patients with tuberous sclerosis (TSC), to assess possible consequences of TSC gene product malfunction or inactivation in the developing brain in relation to ERM protein expression. Ezrin is abundantly expressed within radial glia and migrating cells in the intermediate zone in the prenatal human cerebrum, while moesin is primarily expressed in vascular endothelial cells in developing and adult human brain and scattered microglia in adult brain. In addition, both ezrin and moesin are abundantly co-expressed with hamartin and tuberin within a population of abnormal cells in TSC-associated cortical tubers. The expression of these two proteins--primarily ezrin--suggests that they are developmentally regulated and abundantly expressed in germinal matrix and/or migrating cells during cerebral cortical development. In TSC-associated cortical tubers, both proteins appeared to be up-regulated and are co-localized within a population of abnormal neuroglial cells typical of those seen in tubers. Expression of these proteins and their co-localization with tuberin and hamartin in these cells may suggest a compensatory up-regulation in response to TSC gene mutation.</description><subject>Actin</subject><subject>Biological and medical sciences</subject><subject>Brain research</subject><subject>Cell cycle</subject><subject>Cerebral cortex</subject><subject>Cerebrum</subject><subject>Cloning</subject><subject>Cytoskeletal Proteins</subject><subject>Cytoskeleton</subject><subject>Endothelial cells</subject><subject>ERM protein</subject><subject>Ezrin</subject><subject>Genes</subject><subject>Glial cells</subject><subject>Glial Fibrillary Acidic Protein - analysis</subject><subject>Glial Fibrillary Acidic Protein - biosynthesis</subject><subject>Humans</subject><subject>Immunohistochemistry</subject><subject>Infant</subject><subject>Infant, Newborn</subject><subject>Laboratories</subject><subject>Localization</subject><subject>Medical sciences</subject><subject>Membrane proteins</subject><subject>Microfilament Proteins - analysis</subject><subject>Microfilament Proteins - biosynthesis</subject><subject>Microglia</subject><subject>Moesin</subject><subject>Monoclonal antibodies</subject><subject>Mutation</subject><subject>Neurology</subject><subject>Neuropathology</subject><subject>Phosphoproteins - analysis</subject><subject>Phosphoproteins - biosynthesis</subject><subject>Point mutation</subject><subject>Protein expression</subject><subject>Proteins</subject><subject>Radial glial cells</subject><subject>Radixin</subject><subject>Repressor Proteins - analysis</subject><subject>Repressor Proteins - biosynthesis</subject><subject>Telencephalon - abnormalities</subject><subject>Telencephalon - metabolism</subject><subject>Telencephalon - pathology</subject><subject>Tuberous sclerosis</subject><subject>Tuberous Sclerosis - pathology</subject><subject>Tuberous Sclerosis Complex 1</subject><subject>Tuberous Sclerosis Complex 2</subject><subject>Tumor Suppressor Proteins</subject><subject>Tumors of the nervous system. Phacomatoses</subject><issn>0001-6322</issn><issn>1432-0533</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNpdkU1rHDEMhk1oaTZJf0AvZaA0t2kk2zP2HENIPyDQS3M2Xo-m6zAfW2sm2fbXx5tdCPRgLNnPKyS9QnxA-IIA5ooBNGAJIEuoNJS7E7FCrfaZUm_ECiD_1krKU3HG_JAzaXT1TpyiRERVy5VIt_9SHAs_tsUwEeeQdttEzHEai6c4b_LLvKGipUfqp20cfxebZfBjESjROi3Di3Re1pSmhQsOfQ44cumZpxD9TG0RpjTH4PsDxhfibed7pvfH-1zcf739dfO9vPv57cfN9V0ZtMS5DJXqgu-glX6NRjeBsJW2qmsNxloJAaxqwRgrG6UaX0mLdQWkdO1Jt9ioc3F5qLtN05-FeHZD5EB970fKvTqDttHS7MFP_4EP05LG3JuTWhuLVmnIFB6okAfkRJ3bpjj49NchuL0d7mCHy3a4vR1ulzUfj5WX9UDtq-K4_wx8PgKe84a65McQ-ZVTTVXno54Bnf2TPQ</recordid><startdate>20020801</startdate><enddate>20020801</enddate><creator>JOHNSON, Michael W</creator><creator>MIYATA, Hajime</creator><creator>VINTERS, Harry V</creator><general>Springer</general><general>Springer Nature B.V</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>3V.</scope><scope>7TK</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88G</scope><scope>8AO</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PSYQQ</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20020801</creationdate><title>Ezrin and moesin expression within the developing human cerebrum and tuberous sclerosis-associated cortical tubers</title><author>JOHNSON, Michael W ; MIYATA, Hajime ; VINTERS, Harry V</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c421t-c53fcaf0d2ab1749ce1d285664078820c083d077829339a5281650e346ae4d193</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Actin</topic><topic>Biological and medical sciences</topic><topic>Brain research</topic><topic>Cell cycle</topic><topic>Cerebral cortex</topic><topic>Cerebrum</topic><topic>Cloning</topic><topic>Cytoskeletal Proteins</topic><topic>Cytoskeleton</topic><topic>Endothelial cells</topic><topic>ERM protein</topic><topic>Ezrin</topic><topic>Genes</topic><topic>Glial cells</topic><topic>Glial Fibrillary Acidic Protein - analysis</topic><topic>Glial Fibrillary Acidic Protein - biosynthesis</topic><topic>Humans</topic><topic>Immunohistochemistry</topic><topic>Infant</topic><topic>Infant, Newborn</topic><topic>Laboratories</topic><topic>Localization</topic><topic>Medical sciences</topic><topic>Membrane proteins</topic><topic>Microfilament Proteins - analysis</topic><topic>Microfilament Proteins - biosynthesis</topic><topic>Microglia</topic><topic>Moesin</topic><topic>Monoclonal antibodies</topic><topic>Mutation</topic><topic>Neurology</topic><topic>Neuropathology</topic><topic>Phosphoproteins - analysis</topic><topic>Phosphoproteins - biosynthesis</topic><topic>Point mutation</topic><topic>Protein expression</topic><topic>Proteins</topic><topic>Radial glial cells</topic><topic>Radixin</topic><topic>Repressor Proteins - analysis</topic><topic>Repressor Proteins - biosynthesis</topic><topic>Telencephalon - abnormalities</topic><topic>Telencephalon - metabolism</topic><topic>Telencephalon - pathology</topic><topic>Tuberous sclerosis</topic><topic>Tuberous Sclerosis - pathology</topic><topic>Tuberous Sclerosis Complex 1</topic><topic>Tuberous Sclerosis Complex 2</topic><topic>Tumor Suppressor Proteins</topic><topic>Tumors of the nervous system. Phacomatoses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>JOHNSON, Michael W</creatorcontrib><creatorcontrib>MIYATA, Hajime</creatorcontrib><creatorcontrib>VINTERS, Harry V</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>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Psychology Database (Alumni)</collection><collection>ProQuest Pharma Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>ProQuest Psychology</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest One Psychology</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Acta neuropathologica</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>JOHNSON, Michael W</au><au>MIYATA, Hajime</au><au>VINTERS, Harry V</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ezrin and moesin expression within the developing human cerebrum and tuberous sclerosis-associated cortical tubers</atitle><jtitle>Acta neuropathologica</jtitle><addtitle>Acta Neuropathol</addtitle><date>2002-08-01</date><risdate>2002</risdate><volume>104</volume><issue>2</issue><spage>188</spage><epage>196</epage><pages>188-196</pages><issn>0001-6322</issn><eissn>1432-0533</eissn><coden>ANPTAL</coden><abstract>The ERM (ezrin, radixin, and moesin) proteins belong to the band-4.1 superfamily of membrane-cytoskeleton-linking proteins which bind to the actin cytoskeleton via their C-terminal sequences and bind ERM binding membrane proteins (ERMBMPs). We investigated the immunohistochemical expression of two of the ERM proteins (ezrin and moesin) in developing human cerebral cortex and in cortical tubers from patients with tuberous sclerosis (TSC), to assess possible consequences of TSC gene product malfunction or inactivation in the developing brain in relation to ERM protein expression. Ezrin is abundantly expressed within radial glia and migrating cells in the intermediate zone in the prenatal human cerebrum, while moesin is primarily expressed in vascular endothelial cells in developing and adult human brain and scattered microglia in adult brain. In addition, both ezrin and moesin are abundantly co-expressed with hamartin and tuberin within a population of abnormal cells in TSC-associated cortical tubers. The expression of these two proteins--primarily ezrin--suggests that they are developmentally regulated and abundantly expressed in germinal matrix and/or migrating cells during cerebral cortical development. In TSC-associated cortical tubers, both proteins appeared to be up-regulated and are co-localized within a population of abnormal neuroglial cells typical of those seen in tubers. Expression of these proteins and their co-localization with tuberin and hamartin in these cells may suggest a compensatory up-regulation in response to TSC gene mutation.</abstract><cop>Berlin</cop><pub>Springer</pub><pmid>12111362</pmid><doi>10.1007/s00401-002-0540-x</doi><tpages>9</tpages></addata></record> |
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| subjects | Actin Biological and medical sciences Brain research Cell cycle Cerebral cortex Cerebrum Cloning Cytoskeletal Proteins Cytoskeleton Endothelial cells ERM protein Ezrin Genes Glial cells Glial Fibrillary Acidic Protein - analysis Glial Fibrillary Acidic Protein - biosynthesis Humans Immunohistochemistry Infant Infant, Newborn Laboratories Localization Medical sciences Membrane proteins Microfilament Proteins - analysis Microfilament Proteins - biosynthesis Microglia Moesin Monoclonal antibodies Mutation Neurology Neuropathology Phosphoproteins - analysis Phosphoproteins - biosynthesis Point mutation Protein expression Proteins Radial glial cells Radixin Repressor Proteins - analysis Repressor Proteins - biosynthesis Telencephalon - abnormalities Telencephalon - metabolism Telencephalon - pathology Tuberous sclerosis Tuberous Sclerosis - pathology Tuberous Sclerosis Complex 1 Tuberous Sclerosis Complex 2 Tumor Suppressor Proteins Tumors of the nervous system. Phacomatoses |
| title | Ezrin and moesin expression within the developing human cerebrum and tuberous sclerosis-associated cortical tubers |
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