Effects of db-cAMP and theophylline on Concanavalin A binding site distribution on transformed and protease-treated cell lines
Identifieur interne : 001037 ( Istex/Corpus ); précédent : 001036; suivant : 001038Effects of db-cAMP and theophylline on Concanavalin A binding site distribution on transformed and protease-treated cell lines
Auteurs : Joan Z. Borysenko ; Th. E. Ukena ; M. J. KarnovskySource :
- Experimental Cell Research [ 0014-4827 ] ; 1977.
English descriptors
- Teeft :
- Acad, Binding site distribution, Brief trypsinization, Cabs distribution, Cars distribution, Cell cycle, Cell edges, Cell lines, Cell shape, Cells show, Chinese hamster ovary cells, Cona, Cona binding, Dbcamp treatment, High concentrations, Intracellular camp levels, Many microvilli, Microtubular protein, Microtubule, Microvilli, Morphological reversion, Mouse embryo fibroblasts, Natl, Normal cells, Proc, Proc natl acad, Proteolytic activity, Scanning micrograph, Sodium butyrate, Surface distribution, Theophylline, Theophylline treatment, Tufts university school, Ukena.
Abstract
Abstract: We have examined the effects of N6, O2-dibutyryl 3′: 5′ adenosine-cyclic monophosphate (db-cAMP) and theophylline treatment on the surface distribution of Concanavalin A-binding sites (CABS) on 3T3 cells, SV40-transformed 3T3 cells (SV3T3) and a line of SV40-transformed mouse embryo fibroblasts (VLM). Overnight incubation of VLM cells in medium containing db-cAMP and theophylline completely eliminated the lectin-induced clustering of CABS observed on many transformed cell lines. Similar treatment of SV3T3 cells caused a partial inhibition of clustering. A clone of 3T3 cells that did not normally show lectin-induced clustering could be caused to patch by brief trypsinization. Induction of clustering on these cells after trypsinization was likewise prevented by db-cAMP and theophylline.
Url:
DOI: 10.1016/0014-4827(77)90407-4
Links to Exploration step
ISTEX:176A7E8D0AF36D47D0165E0A83C7EB77EE12FB80Le document en format XML
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Borysenko</name><affiliation><mods:affiliation>Department of Anatomy, Tufts University School of Medicine, Boston, MA 02111, USA</mods:affiliation></affiliation></author><author><name sortKey="Ukena, Th E" sort="Ukena, Th E" uniqKey="Ukena T" first="Th. E." last="Ukena">Th. E. Ukena</name><affiliation><mods:affiliation>Department of Pathology, Harvard Medical School, Boston, MA 02115, USA</mods:affiliation></affiliation></author><author><name sortKey="Karnovsky, M J" sort="Karnovsky, M J" uniqKey="Karnovsky M" first="M. J." last="Karnovsky">M. J. 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Overnight incubation of VLM cells in medium containing db-cAMP and theophylline completely eliminated the lectin-induced clustering of CABS observed on many transformed cell lines. Similar treatment of SV3T3 cells caused a partial inhibition of clustering. A clone of 3T3 cells that did not normally show lectin-induced clustering could be caused to patch by brief trypsinization. Induction of clustering on these cells after trypsinization was likewise prevented by db-cAMP and theophylline.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>theophylline</json:string><json:string>cona</json:string><json:string>microvilli</json:string><json:string>natl</json:string><json:string>proc</json:string><json:string>proc natl acad</json:string><json:string>acad</json:string><json:string>microtubule</json:string><json:string>ukena</json:string><json:string>theophylline treatment</json:string><json:string>cell shape</json:string><json:string>cabs distribution</json:string><json:string>cell lines</json:string><json:string>binding site distribution</json:string><json:string>microtubular protein</json:string><json:string>many microvilli</json:string><json:string>brief trypsinization</json:string><json:string>mouse embryo fibroblasts</json:string><json:string>cell edges</json:string><json:string>cells show</json:string><json:string>normal cells</json:string><json:string>cars distribution</json:string><json:string>morphological reversion</json:string><json:string>sodium butyrate</json:string><json:string>intracellular camp levels</json:string><json:string>cell cycle</json:string><json:string>proteolytic activity</json:string><json:string>cona binding</json:string><json:string>chinese hamster ovary cells</json:string><json:string>high concentrations</json:string><json:string>scanning micrograph</json:string><json:string>tufts university school</json:string><json:string>surface distribution</json:string><json:string>dbcamp treatment</json:string></teeft></keywords><author><json:item><name>Joan Z. Borysenko</name><affiliations><json:string>Department of Anatomy, Tufts University School of Medicine, Boston, MA 02111, USA</json:string></affiliations></json:item><json:item><name>Th.E. Ukena</name><affiliations><json:string>Department of Pathology, Harvard Medical School, Boston, MA 02115, USA</json:string></affiliations></json:item><json:item><name>M.J. Karnovsky</name><affiliations><json:string>Department of Pathology, Harvard Medical School, Boston, MA 02115, USA</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-W8QK5Z95-J</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: We have examined the effects of N6, O2-dibutyryl 3′: 5′ adenosine-cyclic monophosphate (db-cAMP) and theophylline treatment on the surface distribution of Concanavalin A-binding sites (CABS) on 3T3 cells, SV40-transformed 3T3 cells (SV3T3) and a line of SV40-transformed mouse embryo fibroblasts (VLM). Overnight incubation of VLM cells in medium containing db-cAMP and theophylline completely eliminated the lectin-induced clustering of CABS observed on many transformed cell lines. Similar treatment of SV3T3 cells caused a partial inhibition of clustering. A clone of 3T3 cells that did not normally show lectin-induced clustering could be caused to patch by brief trypsinization. Induction of clustering on these cells after trypsinization was likewise prevented by db-cAMP and theophylline.</abstract><qualityIndicators><refBibsNative>true</refBibsNative><abstractWordCount>112</abstractWordCount><abstractCharCount>805</abstractCharCount><keywordCount>0</keywordCount><score>6.669</score><pdfWordCount>3325</pdfWordCount><pdfCharCount>19604</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>8</pdfPageCount><pdfPageSize>504 x 720 pts</pdfPageSize></qualityIndicators><title>Effects of db-cAMP and theophylline on Concanavalin A binding site distribution on transformed and protease-treated cell lines</title><pmid><json:string>194782</json:string></pmid><pii><json:string>0014-4827(77)90407-4</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>Experimental Cell Research</title><language><json:string>unknown</json:string></language><publicationDate>1977</publicationDate><issn><json:string>0014-4827</json:string></issn><pii><json:string>S0014-4827(00)X0333-3</json:string></pii><volume>107</volume><issue>1</issue><pages><first>253</first><last>260</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>10s</json:string><json:string>1977</json:string></date><geogName></geogName><orgName><json:string>Tousimis Research, Inc</json:string><json:string>Tufts University</json:string><json:string>Academic Press, Inc.</json:string><json:string>Massachusetts Institute of Technology</json:string><json:string>USPHS</json:string></orgName><orgName_funder><json:string>USPHS</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>William Woods</json:string><json:string>Puck</json:string><json:string>Satvir Tevethia</json:string><json:string>Kathy Boudrow</json:string><json:string>Smith L Revel</json:string><json:string>Edelman</json:string></persName><placeName><json:string>Boston</json:string><json:string>MA</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>[4]</json:string><json:string>[34]</json:string><json:string>[14, 15, 16,36,37,39]</json:string><json:string>[29]</json:string><json:string>[33]</json:string><json:string>[39]</json:string><json:string>[14-22]</json:string><json:string>[21]</json:string><json:string>[38]</json:string><json:string>[31]</json:string><json:string>[37]</json:string><json:string>[41]</json:string><json:string>[36]</json:string><json:string>[40]</json:string><json:string>Erlanger et al. [28]</json:string><json:string>[35]</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-W8QK5Z95-J</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - oncology</json:string><json:string>2 - cell biology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - biochemistry & molecular biology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Cell Biology</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>1977</publicationDate><copyrightDate>1977</copyrightDate><doi><json:string>10.1016/0014-4827(77)90407-4</json:string></doi><id>176A7E8D0AF36D47D0165E0A83C7EB77EE12FB80</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-W8QK5Z95-J/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-W8QK5Z95-J/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-W8QK5Z95-J/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a">Effects of db-cAMP and theophylline on Concanavalin A binding site distribution on transformed and protease-treated cell lines</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>1977</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>This study was supported by USPHS grants CA 17328 and CA 14732 from the NCI.</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Effects of db-cAMP and theophylline on Concanavalin A binding site distribution on transformed and protease-treated cell lines</title><author xml:id="author-0000"><persName><forename type="first">Joan Z.</forename><surname>Borysenko</surname></persName><affiliation>Department of Anatomy, Tufts University School of Medicine, Boston, MA 02111, USA</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Th.E.</forename><surname>Ukena</surname></persName><affiliation>Department of Pathology, Harvard Medical School, Boston, MA 02115, USA</affiliation></author><author xml:id="author-0002"><persName><forename type="first">M.J.</forename><surname>Karnovsky</surname></persName><affiliation>Department of Pathology, Harvard Medical School, Boston, MA 02115, USA</affiliation></author><idno type="istex">176A7E8D0AF36D47D0165E0A83C7EB77EE12FB80</idno><idno type="ark">ark:/67375/6H6-W8QK5Z95-J</idno><idno type="DOI">10.1016/0014-4827(77)90407-4</idno><idno type="PII">0014-4827(77)90407-4</idno></analytic><monogr><title level="j">Experimental Cell Research</title><title level="j" type="abbrev">YEXCR</title><idno type="pISSN">0014-4827</idno><idno type="PII">S0014-4827(00)X0333-3</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1977"></date><biblScope unit="volume">107</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="253">253</biblScope><biblScope unit="page" to="260">260</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1977</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: We have examined the effects of N6, O2-dibutyryl 3′: 5′ adenosine-cyclic monophosphate (db-cAMP) and theophylline treatment on the surface distribution of Concanavalin A-binding sites (CABS) on 3T3 cells, SV40-transformed 3T3 cells (SV3T3) and a line of SV40-transformed mouse embryo fibroblasts (VLM). Overnight incubation of VLM cells in medium containing db-cAMP and theophylline completely eliminated the lectin-induced clustering of CABS observed on many transformed cell lines. Similar treatment of SV3T3 cells caused a partial inhibition of clustering. A clone of 3T3 cells that did not normally show lectin-induced clustering could be caused to patch by brief trypsinization. Induction of clustering on these cells after trypsinization was likewise prevented by db-cAMP and theophylline.</p></abstract></profileDesc><revisionDesc><change when="1977">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-W8QK5Z95-J/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>YEXCR</jid><aid>77904074</aid><ce:pii>0014-4827(77)90407-4</ce:pii><ce:doi>10.1016/0014-4827(77)90407-4</ce:doi><ce:copyright type="unknown" year="1977"></ce:copyright></item-info><head><ce:article-footnote><ce:label>☆</ce:label><ce:note-para>This study was supported by USPHS grants CA 17328 and CA 14732 from the NCI.</ce:note-para></ce:article-footnote><ce:title>Effects of db-cAMP and theophylline on Concanavalin A binding site distribution on transformed and protease-treated cell lines</ce:title><ce:author-group><ce:author><ce:given-name>Joan Z.</ce:given-name><ce:surname>Borysenko</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Th.E.</ce:given-name><ce:surname>Ukena</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>M.J.</ce:given-name><ce:surname>Karnovsky</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>2</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>1</ce:label><ce:textfn>Department of Anatomy, Tufts University School of Medicine, Boston, MA 02111, USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>2</ce:label><ce:textfn>Department of Pathology, Harvard Medical School, Boston, MA 02115, USA</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="24" month="9" year="1976"></ce:date-received><ce:date-accepted day="2" month="2" year="1977"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>We have examined the effects of <ce:italic>N<ce:sup>6</ce:sup>, O<ce:sup>2</ce:sup></ce:italic>-dibutyryl 3′: 5′ adenosine-cyclic monophosphate (db-cAMP) and theophylline treatment on the surface distribution of Concanavalin A-binding sites (CABS) on 3T3 cells, SV40-transformed 3T3 cells (SV3T3) and a line of SV40-transformed mouse embryo fibroblasts (VLM). Overnight incubation of VLM cells in medium containing db-cAMP and theophylline completely eliminated the lectin-induced clustering of CABS observed on many transformed cell lines. Similar treatment of SV3T3 cells caused a partial inhibition of clustering. A clone of 3T3 cells that did not normally show lectin-induced clustering could be caused to patch by brief trypsinization. Induction of clustering on these cells after trypsinization was likewise prevented by db-cAMP and theophylline.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Effects of db-cAMP and theophylline on Concanavalin A binding site distribution on transformed and protease-treated cell lines</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Effects of db-cAMP and theophylline on Concanavalin A binding site distribution on transformed and protease-treated cell lines</title></titleInfo><name type="personal"><namePart type="given">Joan Z.</namePart><namePart type="family">Borysenko</namePart><affiliation>Department of Anatomy, Tufts University School of Medicine, Boston, MA 02111, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Th.E.</namePart><namePart type="family">Ukena</namePart><affiliation>Department of Pathology, Harvard Medical School, Boston, MA 02115, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M.J.</namePart><namePart type="family">Karnovsky</namePart><affiliation>Department of Pathology, Harvard Medical School, Boston, MA 02115, 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">1977</dateIssued><copyrightDate encoding="w3cdtf">1977</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: We have examined the effects of N6, O2-dibutyryl 3′: 5′ adenosine-cyclic monophosphate (db-cAMP) and theophylline treatment on the surface distribution of Concanavalin A-binding sites (CABS) on 3T3 cells, SV40-transformed 3T3 cells (SV3T3) and a line of SV40-transformed mouse embryo fibroblasts (VLM). Overnight incubation of VLM cells in medium containing db-cAMP and theophylline completely eliminated the lectin-induced clustering of CABS observed on many transformed cell lines. Similar treatment of SV3T3 cells caused a partial inhibition of clustering. A clone of 3T3 cells that did not normally show lectin-induced clustering could be caused to patch by brief trypsinization. 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