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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Na-butyrate increases the production and α2,6-sialylation of recombinant interferon-γ expressed by α2,6- sialyltransferase engineered CHO cells</title><author><name sortKey="Lamotte, Damien" sort="Lamotte, Damien" uniqKey="Lamotte D" first="Damien" last="Lamotte">Damien Lamotte</name><affiliation><nlm:aff id="Aff1">Laboratoire des Sciences du Génie Chimique, CNRS-ENSIC, 1, rue Grandville, BP 451, 54001 Nancy Cedex, France</nlm:aff></affiliation></author><author><name sortKey="Buckberry, Lorraine" sort="Buckberry, Lorraine" uniqKey="Buckberry L" first="Lorraine" last="Buckberry">Lorraine Buckberry</name><affiliation><nlm:aff id="Aff2">Department of Biological Sciences, De Montfort University, Leicester, LEI 9BH UK</nlm:aff></affiliation></author><author><name sortKey="Monaco, Lucia" sort="Monaco, Lucia" uniqKey="Monaco L" first="Lucia" last="Monaco">Lucia Monaco</name><affiliation><nlm:aff id="Aff3">San Raffaele Scientific Institute, DIBIT, via Olgettina 60, 20132 Milano, Italy</nlm:aff></affiliation></author><author><name sortKey="Soria, Marco" sort="Soria, Marco" uniqKey="Soria M" first="Marco" last="Soria">Marco Soria</name><affiliation><nlm:aff id="Aff3">San Raffaele Scientific Institute, DIBIT, via Olgettina 60, 20132 Milano, Italy</nlm:aff></affiliation></author><author><name sortKey="Jenkins, Nigel" sort="Jenkins, Nigel" uniqKey="Jenkins N" first="Nigel" last="Jenkins">Nigel Jenkins</name><affiliation><nlm:aff id="Aff2">Department of Biological Sciences, De Montfort University, Leicester, LEI 9BH UK</nlm:aff></affiliation></author><author><name sortKey="Engasser, Jean Marc" sort="Engasser, Jean Marc" uniqKey="Engasser J" first="Jean-Marc" last="Engasser">Jean-Marc Engasser</name><affiliation><nlm:aff id="Aff1">Laboratoire des Sciences du Génie Chimique, CNRS-ENSIC, 1, rue Grandville, BP 451, 54001 Nancy Cedex, France</nlm:aff></affiliation></author><author><name sortKey="Marc, Annie" sort="Marc, Annie" uniqKey="Marc A" first="Annie" last="Marc">Annie Marc</name><affiliation><nlm:aff id="Aff1">Laboratoire des Sciences du Génie Chimique, CNRS-ENSIC, 1, rue Grandville, BP 451, 54001 Nancy Cedex, France</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">19003337</idno><idno type="pmc">3449462</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3449462</idno><idno type="RBID">PMC:3449462</idno><idno type="doi">10.1023/A:1008080432681</idno><date when="1999">1999</date><idno type="wicri:Area/Pmc/Corpus">000019</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000019</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Na-butyrate increases the production and α2,6-sialylation of recombinant interferon-γ expressed by α2,6- sialyltransferase engineered CHO cells</title><author><name sortKey="Lamotte, Damien" sort="Lamotte, Damien" uniqKey="Lamotte D" first="Damien" last="Lamotte">Damien Lamotte</name><affiliation><nlm:aff id="Aff1">Laboratoire des Sciences du Génie Chimique, CNRS-ENSIC, 1, rue Grandville, BP 451, 54001 Nancy Cedex, France</nlm:aff></affiliation></author><author><name sortKey="Buckberry, Lorraine" sort="Buckberry, Lorraine" uniqKey="Buckberry L" first="Lorraine" last="Buckberry">Lorraine Buckberry</name><affiliation><nlm:aff id="Aff2">Department of Biological Sciences, De Montfort University, Leicester, LEI 9BH UK</nlm:aff></affiliation></author><author><name sortKey="Monaco, Lucia" sort="Monaco, Lucia" uniqKey="Monaco L" first="Lucia" last="Monaco">Lucia Monaco</name><affiliation><nlm:aff id="Aff3">San Raffaele Scientific Institute, DIBIT, via Olgettina 60, 20132 Milano, Italy</nlm:aff></affiliation></author><author><name sortKey="Soria, Marco" sort="Soria, Marco" uniqKey="Soria M" first="Marco" last="Soria">Marco Soria</name><affiliation><nlm:aff id="Aff3">San Raffaele Scientific Institute, DIBIT, via Olgettina 60, 20132 Milano, Italy</nlm:aff></affiliation></author><author><name sortKey="Jenkins, Nigel" sort="Jenkins, Nigel" uniqKey="Jenkins N" first="Nigel" last="Jenkins">Nigel Jenkins</name><affiliation><nlm:aff id="Aff2">Department of Biological Sciences, De Montfort University, Leicester, LEI 9BH UK</nlm:aff></affiliation></author><author><name sortKey="Engasser, Jean Marc" sort="Engasser, Jean Marc" uniqKey="Engasser J" first="Jean-Marc" last="Engasser">Jean-Marc Engasser</name><affiliation><nlm:aff id="Aff1">Laboratoire des Sciences du Génie Chimique, CNRS-ENSIC, 1, rue Grandville, BP 451, 54001 Nancy Cedex, France</nlm:aff></affiliation></author><author><name sortKey="Marc, Annie" sort="Marc, Annie" uniqKey="Marc A" first="Annie" last="Marc">Annie Marc</name><affiliation><nlm:aff id="Aff1">Laboratoire des Sciences du Génie Chimique, CNRS-ENSIC, 1, rue Grandville, BP 451, 54001 Nancy Cedex, France</nlm:aff></affiliation></author></analytic><series><title level="j">Cytotechnology</title><idno type="ISSN">0920-9069</idno><idno type="eISSN">1573-0778</idno><imprint><date when="1999">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>A non-human like glycosylation pattern in human recombinant glycoproteins expressed by animal cells may compromise their use as therapeutic drugs. In order to correct the CHO glycosylation machinery, a CHO cell line producing recombinant human interferon- γ (IFN) was transformed to replace the endogenous pseudogene with a functional copy of the enzyme α2,6-sialyltransferase (α2,6-ST). Both the parental and the modified CHO cell line were propagated in serum-free batch culture with or without 1 mM sodium butyrate. Although Na-butyrate inhibited cell growth, IFN concentration was increased twofold. The IFN sialylation status was determined using linkage specific sialidases and HPLC. Under non- induced conditions, IFN expressed by α2,6-engineered cells contained 68% of the total sialic acids in the α2,6- conformation and the overall molar ratio of sialic acids to IFN was 2.3. Sodium butyrate addition increased twofold the molar ratio of total sialic acids to IFN and 82% of total sialic acids on IFN were in the α2,6-conformation. In contrast, no effect of the sodium butyrate was noticed on the sialylation of the IFN secreted by the α2,6-ST deficient parental cell line. This study deals for the first time with the effect of Na-butyrate on CHO cells engineered to produce human like sialylation.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Cytotechnology</journal-id><journal-id journal-id-type="iso-abbrev">Cytotechnology</journal-id><journal-title-group><journal-title>Cytotechnology</journal-title></journal-title-group><issn pub-type="ppub">0920-9069</issn><issn pub-type="epub">1573-0778</issn><publisher><publisher-name>Kluwer Academic Publishers</publisher-name><publisher-loc>Dordrecht</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">19003337</article-id><article-id pub-id-type="pmc">3449462</article-id><article-id pub-id-type="publisher-id">168634</article-id><article-id pub-id-type="doi">10.1023/A:1008080432681</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Na-butyrate increases the production and α2,6-sialylation of recombinant interferon-γ expressed by α2,6- sialyltransferase engineered CHO cells</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Lamotte</surname><given-names>Damien</given-names></name><xref ref-type="aff" rid="Aff1">1</xref></contrib><contrib contrib-type="author"><name><surname>Buckberry</surname><given-names>Lorraine</given-names></name><xref ref-type="aff" rid="Aff2">2</xref></contrib><contrib contrib-type="author"><name><surname>Monaco</surname><given-names>Lucia</given-names></name><xref ref-type="aff" rid="Aff3">3</xref></contrib><contrib contrib-type="author"><name><surname>Soria</surname><given-names>Marco</given-names></name><xref ref-type="aff" rid="Aff3">3</xref></contrib><contrib contrib-type="author"><name><surname>Jenkins</surname><given-names>Nigel</given-names></name><xref ref-type="aff" rid="Aff2">2</xref></contrib><contrib contrib-type="author"><name><surname>Engasser</surname><given-names>Jean-Marc</given-names></name><xref ref-type="aff" rid="Aff1">1</xref></contrib><contrib contrib-type="author"><name><surname>Marc</surname><given-names>Annie</given-names></name><address><email>amarc@ensic.u-nancy.fr</email></address><xref ref-type="aff" rid="Aff1">1</xref></contrib><aff id="Aff1"><label>1</label>Laboratoire des Sciences du Génie Chimique, CNRS-ENSIC, 1, rue Grandville, BP 451, 54001 Nancy Cedex, France</aff><aff id="Aff2"><label>2</label>Department of Biological Sciences, De Montfort University, Leicester, LEI 9BH UK</aff><aff id="Aff3"><label>3</label>San Raffaele Scientific Institute, DIBIT, via Olgettina 60, 20132 Milano, Italy</aff></contrib-group><pub-date pub-type="ppub"><month>1</month><year>1999</year></pub-date><volume>29</volume><issue>1</issue><fpage>55</fpage><lpage>64</lpage><permissions><copyright-statement>© Kluwer Academic Publishers 1999</copyright-statement></permissions><abstract id="Abs1"><p>A non-human like glycosylation pattern in human recombinant glycoproteins expressed by animal cells may compromise their use as therapeutic drugs. In order to correct the CHO glycosylation machinery, a CHO cell line producing recombinant human interferon- γ (IFN) was transformed to replace the endogenous pseudogene with a functional copy of the enzyme α2,6-sialyltransferase (α2,6-ST). Both the parental and the modified CHO cell line were propagated in serum-free batch culture with or without 1 mM sodium butyrate. Although Na-butyrate inhibited cell growth, IFN concentration was increased twofold. The IFN sialylation status was determined using linkage specific sialidases and HPLC. Under non- induced conditions, IFN expressed by α2,6-engineered cells contained 68% of the total sialic acids in the α2,6- conformation and the overall molar ratio of sialic acids to IFN was 2.3. Sodium butyrate addition increased twofold the molar ratio of total sialic acids to IFN and 82% of total sialic acids on IFN were in the α2,6-conformation. In contrast, no effect of the sodium butyrate was noticed on the sialylation of the IFN secreted by the α2,6-ST deficient parental cell line. This study deals for the first time with the effect of Na-butyrate on CHO cells engineered to produce human like sialylation.</p></abstract><kwd-group xml:lang="en"><kwd>α2,6-sialyltransferase</kwd><kwd>CHO cells</kwd><kwd>interferon-γ</kwd><kwd>sialylation</kwd><kwd>sodium butyrate</kwd></kwd-group><custom-meta-group><custom-meta><meta-name>issue-copyright-statement</meta-name><meta-value>© Kluwer Academic Publishers 1999</meta-value></custom-meta></custom-meta-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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