Polypeptide variation in an N-CAM extracellular immunoglobulin-like fold is developmentally regulated through alternative splicing
Identifieur interne : 001853 ( Istex/Corpus ); précédent : 001852; suivant : 001854Polypeptide variation in an N-CAM extracellular immunoglobulin-like fold is developmentally regulated through alternative splicing
Auteurs : Stephen J. Small ; Susan L. Haines ; Richard A. AkesonSource :
- Neuron [ 0896-6273 ] ; 1988.
English descriptors
- Teeft :
- Acad, Acid, Acid sequences, Adhesion, Adult brain, Adult forms, Akeson, Amino, Amino acid, Amino acid cells, Amino acid insertion, Amino acid sequence, Amino acids, Base alternative exon, Base exon, Base region, Binding affinity, Binding sites, Biol, Brackenbury, Cdna, Cdna clone, Cdna clones, Cdna sequence, Cell adhesion molecule, Cell adhesion molecules, Cell biol, Cell lines, Cellular basis, Chick embryo, Clone, Coding region, Constant domains, Coverslips, Differential expression, Diffuse autofluorescence, Ecorl site, Edelman, Embryonic, Embryonic brain, Exon, Experimental procedures, Exposure times, Extracellular, Extracellular domain, Extracellular domains, Genomic, Genomic clones, Genomic fragments, Heparin, Heparin binding domains, Hoffman, Hybridization, Hybridization signals, Hypervariable regions, Immunofluorescence, Immunofluorescence experiments, Immunoglobulin, Immunoglobulin superfamily, Individual cells, Insertion, Major differences, Major forms, Major polypeptide forms, Major polypeptide size classes, Major size classes, Membrane attachment, Molecule, Monoclonal antibody, Monoclonal antibody epitopes, Mrna, Mrna size class, Mrna size classes, Mrna species, Mrnas code, Muscle cells, Natl, Ncam, Nervous system, Neural, Neural cell adhesion molecule, Neural cell adhesion molecule ncam, Neural cells, Neuron, Northern blots, Nucleotide sequence, Nylon membranes, Oligo, Oligonucleotide, Other cells, Other species, Parallel coverslips, Partial cdnas, Plasma membrane, Pleated sheets, Polyclonal antibody, Polypeptide, Polypeptide diversity, Polysialic acid, Positive control, Preimmune sera, Proc, Rabbit antibody, Restriction sites, Rna, Rutishauser, Secondary structure, Separate exons, Sequence analysis, Sequencing strategy, Several species, Similar results, Size class, Smooth muscle, Splice site, Synthetic oligonucleotide, Unpublished data, Variable domains, Whole brain.
Abstract
Abstract: The alternative splicing of a previously undiscovered 30 base exon confers a new level of polypeptide diversity on the N-CAM family of cell-surface glycoproteins. It results in the insertion of 10 amino acids into the fourth of five extracellular immunoglobulin-like folds. Each major size class of rat brain N-CAM mRNAs consists of members that contain or lack the exon. Furthermore, this splicing event is developmentally controlled: RNAs containing the inserted exon are expressed at extremely low levels (<3%) in embryonic brain but increase postnatally to 40%–45% of all N-CAM mRNAs in adult brain. Antibodies that recognize the alternative 10 amino acid segment react with a subset of N-CAM-expressing neurons in cultures of embryonic rat cells.
Url:
DOI: 10.1016/0896-6273(88)90158-4
Links to Exploration step
ISTEX:1B388B5907451A711992CF54611E0ECA778B073FLe document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>Polypeptide variation in an N-CAM extracellular immunoglobulin-like fold is developmentally regulated through alternative splicing</title><author><name sortKey="Small, Stephen J" sort="Small, Stephen J" uniqKey="Small S" first="Stephen J." last="Small">Stephen J. Small</name><affiliation><mods:affiliation>Division of Basic Research Children's Hospital Research Foundation Cincinnati, Ohio 45229, USA</mods:affiliation></affiliation></author><author><name sortKey="Haines, Susan L" sort="Haines, Susan L" uniqKey="Haines S" first="Susan L." last="Haines">Susan L. Haines</name><affiliation><mods:affiliation>Division of Basic Research Children's Hospital Research Foundation Cincinnati, Ohio 45229, USA</mods:affiliation></affiliation></author><author><name sortKey="Akeson, Richard A" sort="Akeson, Richard A" uniqKey="Akeson R" first="Richard A." last="Akeson">Richard A. Akeson</name><affiliation><mods:affiliation>Division of Basic Research Children's Hospital Research Foundation Cincinnati, Ohio 45229, USA</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:1B388B5907451A711992CF54611E0ECA778B073F</idno><date when="1988" year="1988">1988</date><idno type="doi">10.1016/0896-6273(88)90158-4</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-P0C6LK2F-F/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">001853</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001853</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Polypeptide variation in an N-CAM extracellular immunoglobulin-like fold is developmentally regulated through alternative splicing</title><author><name sortKey="Small, Stephen J" sort="Small, Stephen J" uniqKey="Small S" first="Stephen J." last="Small">Stephen J. Small</name><affiliation><mods:affiliation>Division of Basic Research Children's Hospital Research Foundation Cincinnati, Ohio 45229, USA</mods:affiliation></affiliation></author><author><name sortKey="Haines, Susan L" sort="Haines, Susan L" uniqKey="Haines S" first="Susan L." last="Haines">Susan L. Haines</name><affiliation><mods:affiliation>Division of Basic Research Children's Hospital Research Foundation Cincinnati, Ohio 45229, USA</mods:affiliation></affiliation></author><author><name sortKey="Akeson, Richard A" sort="Akeson, Richard A" uniqKey="Akeson R" first="Richard A." last="Akeson">Richard A. Akeson</name><affiliation><mods:affiliation>Division of Basic Research Children's Hospital Research Foundation Cincinnati, Ohio 45229, USA</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Neuron</title><title level="j" type="abbrev">NEURON</title><idno type="ISSN">0896-6273</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1988">1988</date><biblScope unit="volume">1</biblScope><biblScope unit="issue">10</biblScope><biblScope unit="page" from="1007">1007</biblScope><biblScope unit="page" to="1017">1017</biblScope></imprint><idno type="ISSN">0896-6273</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0896-6273</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acad</term><term>Acid</term><term>Acid sequences</term><term>Adhesion</term><term>Adult brain</term><term>Adult forms</term><term>Akeson</term><term>Amino</term><term>Amino acid</term><term>Amino acid cells</term><term>Amino acid insertion</term><term>Amino acid sequence</term><term>Amino acids</term><term>Base alternative exon</term><term>Base exon</term><term>Base region</term><term>Binding affinity</term><term>Binding sites</term><term>Biol</term><term>Brackenbury</term><term>Cdna</term><term>Cdna clone</term><term>Cdna clones</term><term>Cdna sequence</term><term>Cell adhesion molecule</term><term>Cell adhesion molecules</term><term>Cell biol</term><term>Cell lines</term><term>Cellular basis</term><term>Chick embryo</term><term>Clone</term><term>Coding region</term><term>Constant domains</term><term>Coverslips</term><term>Differential expression</term><term>Diffuse autofluorescence</term><term>Ecorl site</term><term>Edelman</term><term>Embryonic</term><term>Embryonic brain</term><term>Exon</term><term>Experimental procedures</term><term>Exposure times</term><term>Extracellular</term><term>Extracellular domain</term><term>Extracellular domains</term><term>Genomic</term><term>Genomic clones</term><term>Genomic fragments</term><term>Heparin</term><term>Heparin binding domains</term><term>Hoffman</term><term>Hybridization</term><term>Hybridization signals</term><term>Hypervariable regions</term><term>Immunofluorescence</term><term>Immunofluorescence experiments</term><term>Immunoglobulin</term><term>Immunoglobulin superfamily</term><term>Individual cells</term><term>Insertion</term><term>Major differences</term><term>Major forms</term><term>Major polypeptide forms</term><term>Major polypeptide size classes</term><term>Major size classes</term><term>Membrane attachment</term><term>Molecule</term><term>Monoclonal antibody</term><term>Monoclonal antibody epitopes</term><term>Mrna</term><term>Mrna size class</term><term>Mrna size classes</term><term>Mrna species</term><term>Mrnas code</term><term>Muscle cells</term><term>Natl</term><term>Ncam</term><term>Nervous system</term><term>Neural</term><term>Neural cell adhesion molecule</term><term>Neural cell adhesion molecule ncam</term><term>Neural cells</term><term>Neuron</term><term>Northern blots</term><term>Nucleotide sequence</term><term>Nylon membranes</term><term>Oligo</term><term>Oligonucleotide</term><term>Other cells</term><term>Other species</term><term>Parallel coverslips</term><term>Partial cdnas</term><term>Plasma membrane</term><term>Pleated sheets</term><term>Polyclonal antibody</term><term>Polypeptide</term><term>Polypeptide diversity</term><term>Polysialic acid</term><term>Positive control</term><term>Preimmune sera</term><term>Proc</term><term>Rabbit antibody</term><term>Restriction sites</term><term>Rna</term><term>Rutishauser</term><term>Secondary structure</term><term>Separate exons</term><term>Sequence analysis</term><term>Sequencing strategy</term><term>Several species</term><term>Similar results</term><term>Size class</term><term>Smooth muscle</term><term>Splice site</term><term>Synthetic oligonucleotide</term><term>Unpublished data</term><term>Variable domains</term><term>Whole brain</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The alternative splicing of a previously undiscovered 30 base exon confers a new level of polypeptide diversity on the N-CAM family of cell-surface glycoproteins. It results in the insertion of 10 amino acids into the fourth of five extracellular immunoglobulin-like folds. Each major size class of rat brain N-CAM mRNAs consists of members that contain or lack the exon. Furthermore, this splicing event is developmentally controlled: RNAs containing the inserted exon are expressed at extremely low levels (<3%) in embryonic brain but increase postnatally to 40%–45% of all N-CAM mRNAs in adult brain. Antibodies that recognize the alternative 10 amino acid segment react with a subset of N-CAM-expressing neurons in cultures of embryonic rat cells.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>exon</json:string><json:string>polypeptide</json:string><json:string>mrna</json:string><json:string>cdna</json:string><json:string>amino</json:string><json:string>amino acids</json:string><json:string>ncam</json:string><json:string>extracellular</json:string><json:string>edelman</json:string><json:string>biol</json:string><json:string>amino acid</json:string><json:string>rna</json:string><json:string>oligo</json:string><json:string>rutishauser</json:string><json:string>base exon</json:string><json:string>immunoglobulin</json:string><json:string>clone</json:string><json:string>hybridization</json:string><json:string>akeson</json:string><json:string>genomic</json:string><json:string>cell biol</json:string><json:string>neural cell adhesion molecule</json:string><json:string>oligonucleotide</json:string><json:string>adhesion</json:string><json:string>proc</json:string><json:string>immunofluorescence</json:string><json:string>acad</json:string><json:string>brackenbury</json:string><json:string>neuron</json:string><json:string>amino acid insertion</json:string><json:string>coverslips</json:string><json:string>heparin</json:string><json:string>natl</json:string><json:string>insertion</json:string><json:string>rabbit antibody</json:string><json:string>extracellular domain</json:string><json:string>embryonic</json:string><json:string>extracellular domains</json:string><json:string>immunoglobulin superfamily</json:string><json:string>polysialic acid</json:string><json:string>cell adhesion molecules</json:string><json:string>adult brain</json:string><json:string>experimental procedures</json:string><json:string>cell lines</json:string><json:string>neural</json:string><json:string>coding region</json:string><json:string>positive control</json:string><json:string>northern blots</json:string><json:string>amino acid sequence</json:string><json:string>binding affinity</json:string><json:string>constant domains</json:string><json:string>major size classes</json:string><json:string>variable domains</json:string><json:string>secondary structure</json:string><json:string>adult forms</json:string><json:string>neural cells</json:string><json:string>similar results</json:string><json:string>individual cells</json:string><json:string>genomic fragments</json:string><json:string>cell adhesion molecule</json:string><json:string>molecule</json:string><json:string>acid</json:string><json:string>sequencing strategy</json:string><json:string>embryonic brain</json:string><json:string>several species</json:string><json:string>separate exons</json:string><json:string>cdna sequence</json:string><json:string>sequence analysis</json:string><json:string>whole brain</json:string><json:string>base alternative exon</json:string><json:string>mrna species</json:string><json:string>polypeptide diversity</json:string><json:string>hybridization signals</json:string><json:string>major forms</json:string><json:string>smooth muscle</json:string><json:string>mrna size class</json:string><json:string>nylon membranes</json:string><json:string>mrna size classes</json:string><json:string>heparin binding domains</json:string><json:string>monoclonal antibody</json:string><json:string>preimmune sera</json:string><json:string>exposure times</json:string><json:string>other cells</json:string><json:string>cellular basis</json:string><json:string>differential expression</json:string><json:string>immunofluorescence experiments</json:string><json:string>polyclonal antibody</json:string><json:string>major polypeptide size classes</json:string><json:string>membrane attachment</json:string><json:string>diffuse autofluorescence</json:string><json:string>size class</json:string><json:string>parallel coverslips</json:string><json:string>amino acid cells</json:string><json:string>muscle cells</json:string><json:string>acid sequences</json:string><json:string>hypervariable regions</json:string><json:string>partial cdnas</json:string><json:string>unpublished data</json:string><json:string>other species</json:string><json:string>plasma membrane</json:string><json:string>restriction sites</json:string><json:string>pleated sheets</json:string><json:string>major differences</json:string><json:string>binding sites</json:string><json:string>cdna clone</json:string><json:string>major polypeptide forms</json:string><json:string>nucleotide sequence</json:string><json:string>chick embryo</json:string><json:string>base region</json:string><json:string>mrnas code</json:string><json:string>neural cell adhesion molecule ncam</json:string><json:string>splice site</json:string><json:string>cdna clones</json:string><json:string>monoclonal antibody epitopes</json:string><json:string>nervous system</json:string><json:string>genomic clones</json:string><json:string>synthetic oligonucleotide</json:string><json:string>ecorl site</json:string><json:string>hoffman</json:string></teeft></keywords><author><json:item><name>Stephen J. Small</name><affiliations><json:string>Division of Basic Research Children's Hospital Research Foundation Cincinnati, Ohio 45229, USA</json:string></affiliations></json:item><json:item><name>Susan L. Haines</name><affiliations><json:string>Division of Basic Research Children's Hospital Research Foundation Cincinnati, Ohio 45229, USA</json:string></affiliations></json:item><json:item><name>Richard A. Akeson</name><affiliations><json:string>Division of Basic Research Children's Hospital Research Foundation Cincinnati, Ohio 45229, USA</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-P0C6LK2F-F</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: The alternative splicing of a previously undiscovered 30 base exon confers a new level of polypeptide diversity on the N-CAM family of cell-surface glycoproteins. It results in the insertion of 10 amino acids into the fourth of five extracellular immunoglobulin-like folds. Each major size class of rat brain N-CAM mRNAs consists of members that contain or lack the exon. Furthermore, this splicing event is developmentally controlled: RNAs containing the inserted exon are expressed at extremely low levels (>3%) in embryonic brain but increase postnatally to 40%–45% of all N-CAM mRNAs in adult brain. Antibodies that recognize the alternative 10 amino acid segment react with a subset of N-CAM-expressing neurons in cultures of embryonic rat cells.</abstract><qualityIndicators><score>8.392</score><pdfWordCount>5046</pdfWordCount><pdfCharCount>48722</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>11</pdfPageCount><pdfPageSize>576 x 864 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>116</abstractWordCount><abstractCharCount>761</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Polypeptide variation in an N-CAM extracellular immunoglobulin-like fold is developmentally regulated through alternative splicing</title><pmid><json:string>2483093</json:string></pmid><pii><json:string>0896-6273(88)90158-4</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc. Natl. Acad. Sci. USA</title><language><json:string>unknown</json:string></language><volume>81</volume><pages><first>1460</first><last>1464</last></pages></serie><host><title>Neuron</title><language><json:string>unknown</json:string></language><publicationDate>1988</publicationDate><issn><json:string>0896-6273</json:string></issn><pii><json:string>S0896-6273(00)X0134-1</json:string></pii><volume>1</volume><issue>10</issue><pages><first>1007</first><last>1017</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1988</json:string></date><geogName></geogName><orgName><json:string>Organization</json:string><json:string>Biochem</json:string><json:string>Pharmacia LKB Biotechnology Inc.</json:string><json:string>Neurochem</json:string><json:string>Brochem</json:string><json:string>Biosearch</json:string><json:string>Phytogen Corp., Pasadena</json:string><json:string>Biotech Instruments</json:string><json:string>DNA STAR, Inc., Madison</json:string><json:string>National Institutes of Health</json:string></orgName><orgName_funder><json:string>National Institutes of Health</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>J. Neurosci</json:string><json:string>J. Biol</json:string><json:string>Constant Domains</json:string><json:string>Meg Frnne</json:string><json:string>J. Cell</json:string><json:string>CAM Contain</json:string><json:string>CAM Polypeptlde</json:string><json:string>Dot Blot</json:string><json:string>J. Virol</json:string><json:string>James Bonner</json:string><json:string>Northern</json:string><json:string>Dan Wiginton</json:string><json:string>Jerry Lingrel</json:string><json:string>Bob Brackenbury</json:string><json:string>Antonio Reyes</json:string><json:string>Polypeptlde</json:string><json:string>Brain Allen</json:string><json:string>Ken Blumenthal</json:string><json:string>Brian Key</json:string><json:string>CAM Is-Folds</json:string><json:string>CAM Table</json:string><json:string>CAM Ig</json:string><json:string>Brain Insert</json:string><json:string>I. Cell</json:string><json:string>Shirley Arnold</json:string><json:string>Donna Bernhard</json:string><json:string>Van Doren</json:string><json:string>Sein Figure</json:string><json:string>Jill Benavides</json:string><json:string>CAM Polypeptide</json:string></persName><placeName><json:string>Burlington</json:string><json:string>VT</json:string><json:string>Piscataway</json:string><json:string>Boston</json:string><json:string>Jordan</json:string><json:string>CA</json:string><json:string>MA</json:string><json:string>NJ</json:string><json:string>San Rafael</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Gennarini et al., 1986</json:string><json:string>Schwarzbauer et al., 1983</json:string><json:string>Williams, 1987</json:string><json:string>Edelman, 1984, 1988</json:string><json:string>Nybroe et al., 1985</json:string><json:string>Chuong and Edelman, 1984</json:string><json:string>Owens et al., 1987</json:string><json:string>Edmundson et al., 1974</json:string><json:string>Barthels et al., 1987</json:string><json:string>Dickson et al. (1987)</json:string><json:string>Small et al. (1987)</json:string><json:string>Akeson et al., 1988</json:string><json:string>Cole et al., 1986a</json:string><json:string>Fett and Deutsch, 1974</json:string><json:string>Allen and Akeson, 1985</json:string><json:string>Cole and Glaser, 1986</json:string><json:string>Linnemann et al., 1985</json:string><json:string>Rougon and Marshak, 1986</json:string><json:string>Lerner et al., 1981</json:string><json:string>Cunningham et al., 1987</json:string><json:string>Small et al., 1987</json:string><json:string>Research and Foundation 45229</json:string><json:string>Watanabe et al., 1986</json:string><json:string>Lyles et al., 1984</json:string><json:string>Murray et al., 1986</json:string><json:string>Gennarini et al., 1984</json:string><json:string>Friedlander et al., 1985</json:string><json:string>Van Doren et al., 1984</json:string><json:string>Garnier and Robson (1978)</json:string><json:string>He et al., 1986, 1987</json:string><json:string>Williams et al., 1985</json:string><json:string>Brackenbury et al., 1977</json:string><json:string>Covault et al., 1986</json:string><json:string>Sadoul et al., 1983</json:string><json:string>Amzel and Poljak (1979)</json:string><json:string>Cunnrngham et al., 1987</json:string><json:string>Figure 7; Amzel and Poljak, 1979</json:string><json:string>Finne et al., 1983</json:string><json:string>Hoffman et al., 1982, 1984</json:string><json:string>Brunner et al. (1986)</json:string><json:string>Chou and Fasman (1978)</json:string><json:string>Goridis et al., 1985</json:string><json:string>Frelinger and Rutishauser, 1986</json:string><json:string>Keilhauer et al., 1985</json:string><json:string>Liu et al., 1979</json:string><json:string>Rothbard et al., 1982</json:string><json:string>Littman and Gettner, 1987</json:string><json:string>Rutishauser et al., 1983</json:string><json:string>Hoffman and Edelman, 1983</json:string><json:string>Hall and Rutishauser, 1987</json:string><json:string>Rutishauser et al., 1988</json:string><json:string>Akeson and Warren, 1984</json:string><json:string>Santoni et al., 1987</json:string><json:string>Barbas et al., 1988</json:string><json:string>Varmtion et al. (1975)</json:string><json:string>Cole et al., 1986b</json:string><json:string>Regulated 1009</json:string><json:string>Hunkapiller and Hood, 1986</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-P0C6LK2F-F</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - neurosciences</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - clinical medicine</json:string><json:string>3 - neurology & neurosurgery</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Neuroscience</json:string><json:string>3 - General Neuroscience</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string></inist></categories><publicationDate>1988</publicationDate><copyrightDate>1988</copyrightDate><doi><json:string>10.1016/0896-6273(88)90158-4</json:string></doi><id>1B388B5907451A711992CF54611E0ECA778B073F</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-P0C6LK2F-F/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-P0C6LK2F-F/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-P0C6LK2F-F/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Polypeptide variation in an N-CAM extracellular immunoglobulin-like fold is developmentally regulated through alternative splicing</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>elsevier</p></licence></availability><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M"></p><date>1988</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note><note type="content">Section title: Article</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Polypeptide variation in an N-CAM extracellular immunoglobulin-like fold is developmentally regulated through alternative splicing</title><author xml:id="author-0000"><persName><forename type="first">Stephen J.</forename><surname>Small</surname></persName><affiliation>Division of Basic Research Children's Hospital Research Foundation Cincinnati, Ohio 45229, USA</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Susan L.</forename><surname>Haines</surname></persName><affiliation>Division of Basic Research Children's Hospital Research Foundation Cincinnati, Ohio 45229, USA</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Richard A.</forename><surname>Akeson</surname></persName><affiliation>Division of Basic Research Children's Hospital Research Foundation Cincinnati, Ohio 45229, USA</affiliation></author><idno type="istex">1B388B5907451A711992CF54611E0ECA778B073F</idno><idno type="ark">ark:/67375/6H6-P0C6LK2F-F</idno><idno type="DOI">10.1016/0896-6273(88)90158-4</idno><idno type="PII">0896-6273(88)90158-4</idno></analytic><monogr><title level="j">Neuron</title><title level="j" type="abbrev">NEURON</title><idno type="pISSN">0896-6273</idno><idno type="PII">S0896-6273(00)X0134-1</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1988"></date><biblScope unit="volume">1</biblScope><biblScope unit="issue">10</biblScope><biblScope unit="page" from="1007">1007</biblScope><biblScope unit="page" to="1017">1017</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1988</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: The alternative splicing of a previously undiscovered 30 base exon confers a new level of polypeptide diversity on the N-CAM family of cell-surface glycoproteins. It results in the insertion of 10 amino acids into the fourth of five extracellular immunoglobulin-like folds. Each major size class of rat brain N-CAM mRNAs consists of members that contain or lack the exon. Furthermore, this splicing event is developmentally controlled: RNAs containing the inserted exon are expressed at extremely low levels (<3%) in embryonic brain but increase postnatally to 40%–45% of all N-CAM mRNAs in adult brain. Antibodies that recognize the alternative 10 amino acid segment react with a subset of N-CAM-expressing neurons in cultures of embryonic rat cells.</p></abstract></profileDesc><revisionDesc><change when="1988-10-25">Modified</change><change when="1988">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-P0C6LK2F-F/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>NEURON</jid><aid>88901584</aid><ce:pii>0896-6273(88)90158-4</ce:pii><ce:doi>10.1016/0896-6273(88)90158-4</ce:doi><ce:copyright type="unknown" year="1988"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Article</ce:textfn></ce:dochead><ce:title>Polypeptide variation in an N-CAM extracellular immunoglobulin-like fold is developmentally regulated through alternative splicing</ce:title><ce:author-group><ce:author><ce:given-name>Stephen J.</ce:given-name><ce:surname>Small</ce:surname></ce:author><ce:author><ce:given-name>Susan L.</ce:given-name><ce:surname>Haines</ce:surname></ce:author><ce:author><ce:given-name>Richard A.</ce:given-name><ce:surname>Akeson</ce:surname></ce:author><ce:affiliation><ce:textfn>Division of Basic Research Children's Hospital Research Foundation Cincinnati, Ohio 45229, USA</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="2" month="8" year="1988"></ce:date-received><ce:date-revised day="25" month="10" year="1988"></ce:date-revised><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>The alternative splicing of a previously undiscovered 30 base exon confers a new level of polypeptide diversity on the N-CAM family of cell-surface glycoproteins. It results in the insertion of 10 amino acids into the fourth of five extracellular immunoglobulin-like folds. Each major size class of rat brain N-CAM mRNAs consists of members that contain or lack the exon. Furthermore, this splicing event is developmentally controlled: RNAs containing the inserted exon are expressed at extremely low levels (<3%) in embryonic brain but increase postnatally to 40%–45% of all N-CAM mRNAs in adult brain. Antibodies that recognize the alternative 10 amino acid segment react with a subset of N-CAM-expressing neurons in cultures of embryonic rat cells.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Polypeptide variation in an N-CAM extracellular immunoglobulin-like fold is developmentally regulated through alternative splicing</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Polypeptide variation in an N-CAM extracellular immunoglobulin-like fold is developmentally regulated through alternative splicing</title></titleInfo><name type="personal"><namePart type="given">Stephen J.</namePart><namePart type="family">Small</namePart><affiliation>Division of Basic Research Children's Hospital Research Foundation Cincinnati, Ohio 45229, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Susan L.</namePart><namePart type="family">Haines</namePart><affiliation>Division of Basic Research Children's Hospital Research Foundation Cincinnati, Ohio 45229, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Richard A.</namePart><namePart type="family">Akeson</namePart><affiliation>Division of Basic Research Children's Hospital Research Foundation Cincinnati, Ohio 45229, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1988</dateIssued><dateModified encoding="w3cdtf">1988-10-25</dateModified><copyrightDate encoding="w3cdtf">1988</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: The alternative splicing of a previously undiscovered 30 base exon confers a new level of polypeptide diversity on the N-CAM family of cell-surface glycoproteins. It results in the insertion of 10 amino acids into the fourth of five extracellular immunoglobulin-like folds. Each major size class of rat brain N-CAM mRNAs consists of members that contain or lack the exon. Furthermore, this splicing event is developmentally controlled: RNAs containing the inserted exon are expressed at extremely low levels (<3%) in embryonic brain but increase postnatally to 40%–45% of all N-CAM mRNAs in adult brain. Antibodies that recognize the alternative 10 amino acid segment react with a subset of N-CAM-expressing neurons in cultures of embryonic rat cells.</abstract><note type="content">Section title: Article</note><relatedItem type="host"><titleInfo><title>Neuron</title></titleInfo><titleInfo type="abbreviated"><title>NEURON</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1988</dateIssued></originInfo><identifier type="ISSN">0896-6273</identifier><identifier type="PII">S0896-6273(00)X0134-1</identifier><part><date>1988</date><detail type="volume"><number>1</number><caption>vol.</caption></detail><detail type="issue"><number>10</number><caption>no.</caption></detail><extent unit="issue-pages"><start>901</start><end>1017</end></extent><extent unit="pages"><start>1007</start><end>1017</end></extent></part></relatedItem><identifier type="istex">1B388B5907451A711992CF54611E0ECA778B073F</identifier><identifier type="ark">ark:/67375/6H6-P0C6LK2F-F</identifier><identifier type="DOI">10.1016/0896-6273(88)90158-4</identifier><identifier type="PII">0896-6273(88)90158-4</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-P0C6LK2F-F/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Istex/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001853 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Istex/Corpus/biblio.hfd -nk 001853 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= MersV1
|flux= Istex
|étape= Corpus
|type= RBID
|clé= ISTEX:1B388B5907451A711992CF54611E0ECA778B073F
|texte= Polypeptide variation in an N-CAM extracellular immunoglobulin-like fold is developmentally regulated through alternative splicing
}}
| This area was generated with Dilib version V0.6.33. |  |