Inhibitory effect of platelet factor 4 on human erythroleukemic cells is dependent on cell surface heparan sulfate
Identifieur interne : 001C44 ( Istex/Corpus ); précédent : 001C43; suivant : 001C45Inhibitory effect of platelet factor 4 on human erythroleukemic cells is dependent on cell surface heparan sulfate
Auteurs : Anne-Marie Maurer ; Zhong Chao Han ; Didier Dhermy ; Jean BriereSource :
- The Journal of Laboratory and Clinical Medicine [ 0022-2143 ] ; 1996.
Abstract
We have previously reported that platelet factor 4 (PF4) inhibits human erythroleukemic (HEL) cell growth in a dose-dependent fashion in vitro and that PF4 binds to HEL cells in a specific, saturable, and concentration-dependent manner. In this article we demonstrate that the binding of PF4 on HEL cells and its inhibitiroy effect on HEL cell growth were mediated by heparan sulfate. We found that binding of iodine 125-labeled PF4 to HEL cells was inhibited by heparin, heparan sulfate, and dermatan sulfate and to a smaller extent by chondroitin sulfate. Ninety percent of 125I-labeled PF4 bound to HEL cells was released by cells after exposure to heparin and heparan sulfate. Treatment of cells with heparitinase and heparinase induced a decrease in the binding of 125I-labeled PF4 to cells. Binding of 125I-labeled PF4 was partially inhibited by the presence of increasing concentrations of protamine sulfate and basic fibroblast growth factor. To test whether PF4 bound to cell surface proteoglycans, proteoglycan synthesis was inhibited by using 4-methylumbelliferyl-β-D-xyloside. The binding of 125I-labeled PF4 on treated cells was decreased, and xyloside treatment of cells abrogated the biologic activity of PF4 in a plasma clot culture system. The inhibitory effect of PF4 was retained in a serum-free agar culture system, which indicates that the binding of PF4 to HEL cells induces cell growth inhibition in a direct fashion. Taken together, these findings suggest that PF4 directly acts on HEL cell growth by fixation on heparan sulfate proteoglycans on the HEL cell surface.
Url:
DOI: 10.1016/S0022-2143(96)90186-9
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<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>Inhibitory effect of platelet factor 4 on human erythroleukemic cells is dependent on cell surface heparan sulfate</title><author><name sortKey="Maurer, Anne Marie" sort="Maurer, Anne Marie" uniqKey="Maurer A" first="Anne-Marie" last="Maurer">Anne-Marie Maurer</name><affiliation><mods:affiliation>INSERM U 409, Hôpital Beaujon, Clichy, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</mods:affiliation></affiliation></author><author><name sortKey="Han, Zhong Chao" sort="Han, Zhong Chao" uniqKey="Han Z" first="Zhong Chao" last="Han">Zhong Chao Han</name><affiliation><mods:affiliation>INSERM U 409, Hôpital Beaujon, Clichy, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</mods:affiliation></affiliation></author><author><name sortKey="Dhermy, Didier" sort="Dhermy, Didier" uniqKey="Dhermy D" first="Didier" last="Dhermy">Didier Dhermy</name><affiliation><mods:affiliation>INSERM U 409, Hôpital Beaujon, Clichy, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</mods:affiliation></affiliation></author><author><name sortKey="Briere, Jean" sort="Briere, Jean" uniqKey="Briere J" first="Jean" last="Briere">Jean Briere</name><affiliation><mods:affiliation>Reprint requests: Professor Jean Brière, Service d'hématologie clinique, Hôpital Beaujon, 100, Boulevard du Général Leclerc, 92118 Clichy Cédex, France.</mods:affiliation></affiliation><affiliation><mods:affiliation>INSERM U 409, Hôpital Beaujon, Clichy, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:BE8E1B2D601E90039E3349EB6C2A299D7FD5DD5A</idno><date when="1996" year="1996">1996</date><idno type="doi">10.1016/S0022-2143(96)90186-9</idno><idno type="url">https://api.istex.fr/document/BE8E1B2D601E90039E3349EB6C2A299D7FD5DD5A/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">001C44</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001C44</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Inhibitory effect of platelet factor 4 on human erythroleukemic cells is dependent on cell surface heparan sulfate</title><author><name sortKey="Maurer, Anne Marie" sort="Maurer, Anne Marie" uniqKey="Maurer A" first="Anne-Marie" last="Maurer">Anne-Marie Maurer</name><affiliation><mods:affiliation>INSERM U 409, Hôpital Beaujon, Clichy, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</mods:affiliation></affiliation></author><author><name sortKey="Han, Zhong Chao" sort="Han, Zhong Chao" uniqKey="Han Z" first="Zhong Chao" last="Han">Zhong Chao Han</name><affiliation><mods:affiliation>INSERM U 409, Hôpital Beaujon, Clichy, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</mods:affiliation></affiliation></author><author><name sortKey="Dhermy, Didier" sort="Dhermy, Didier" uniqKey="Dhermy D" first="Didier" last="Dhermy">Didier Dhermy</name><affiliation><mods:affiliation>INSERM U 409, Hôpital Beaujon, Clichy, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</mods:affiliation></affiliation></author><author><name sortKey="Briere, Jean" sort="Briere, Jean" uniqKey="Briere J" first="Jean" last="Briere">Jean Briere</name><affiliation><mods:affiliation>Reprint requests: Professor Jean Brière, Service d'hématologie clinique, Hôpital Beaujon, 100, Boulevard du Général Leclerc, 92118 Clichy Cédex, France.</mods:affiliation></affiliation><affiliation><mods:affiliation>INSERM U 409, Hôpital Beaujon, Clichy, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</mods:affiliation></affiliation><affiliation><mods:affiliation>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">The Journal of Laboratory and Clinical Medicine</title><title level="j" type="abbrev">YMLC</title><idno type="ISSN">0022-2143</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1996">1996</date><biblScope unit="volume">127</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="382">382</biblScope><biblScope unit="page" to="390">390</biblScope></imprint><idno type="ISSN">0022-2143</idno></series><idno type="istex">BE8E1B2D601E90039E3349EB6C2A299D7FD5DD5A</idno><idno type="DOI">10.1016/S0022-2143(96)90186-9</idno><idno type="PII">S0022-2143(96)90186-9</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0022-2143</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We have previously reported that platelet factor 4 (PF4) inhibits human erythroleukemic (HEL) cell growth in a dose-dependent fashion in vitro and that PF4 binds to HEL cells in a specific, saturable, and concentration-dependent manner. In this article we demonstrate that the binding of PF4 on HEL cells and its inhibitiroy effect on HEL cell growth were mediated by heparan sulfate. We found that binding of iodine 125-labeled PF4 to HEL cells was inhibited by heparin, heparan sulfate, and dermatan sulfate and to a smaller extent by chondroitin sulfate. Ninety percent of 125I-labeled PF4 bound to HEL cells was released by cells after exposure to heparin and heparan sulfate. Treatment of cells with heparitinase and heparinase induced a decrease in the binding of 125I-labeled PF4 to cells. Binding of 125I-labeled PF4 was partially inhibited by the presence of increasing concentrations of protamine sulfate and basic fibroblast growth factor. To test whether PF4 bound to cell surface proteoglycans, proteoglycan synthesis was inhibited by using 4-methylumbelliferyl-β-D-xyloside. The binding of 125I-labeled PF4 on treated cells was decreased, and xyloside treatment of cells abrogated the biologic activity of PF4 in a plasma clot culture system. The inhibitory effect of PF4 was retained in a serum-free agar culture system, which indicates that the binding of PF4 to HEL cells induces cell growth inhibition in a direct fashion. Taken together, these findings suggest that PF4 directly acts on HEL cell growth by fixation on heparan sulfate proteoglycans on the HEL cell surface.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>Anne-Marie Maurer</name><affiliations><json:string>INSERM U 409, Hôpital Beaujon, Clichy, France</json:string><json:string>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</json:string><json:string>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</json:string></affiliations></json:item><json:item><name>Zhong Chao Han</name><affiliations><json:string>INSERM U 409, Hôpital Beaujon, Clichy, France</json:string><json:string>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</json:string><json:string>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</json:string></affiliations></json:item><json:item><name>Didier Dhermy</name><affiliations><json:string>INSERM U 409, Hôpital Beaujon, Clichy, France</json:string><json:string>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</json:string><json:string>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</json:string></affiliations></json:item><json:item><name>Jean Briere</name><affiliations><json:string>Reprint requests: Professor Jean Brière, Service d'hématologie clinique, Hôpital Beaujon, 100, Boulevard du Général Leclerc, 92118 Clichy Cédex, France.</json:string><json:string>INSERM U 409, Hôpital Beaujon, Clichy, France</json:string><json:string>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</json:string><json:string>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>bFGF = basic fibroblast growth factor</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>BSA = bovine serum albumin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>CS = chondroitin sulfate</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>DS = dermatan sulfate</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>FCS = fetal calf serum</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>GAG = glycosaminoglycan</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>HEL = human erythroleukemic</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>HEPES = N-2-hydroxyethylpiperazine-N-2-ethanesulfonic acid</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>HS = heparan sulfate</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>PBS = phosphate-buffered saline solution</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>PF4 = platelet factor 4</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>TBS = Tris-buffered saline solution</value></json:item></subject><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>We have previously reported that platelet factor 4 (PF4) inhibits human erythroleukemic (HEL) cell growth in a dose-dependent fashion in vitro and that PF4 binds to HEL cells in a specific, saturable, and concentration-dependent manner. In this article we demonstrate that the binding of PF4 on HEL cells and its inhibitiroy effect on HEL cell growth were mediated by heparan sulfate. We found that binding of iodine 125-labeled PF4 to HEL cells was inhibited by heparin, heparan sulfate, and dermatan sulfate and to a smaller extent by chondroitin sulfate. Ninety percent of 125I-labeled PF4 bound to HEL cells was released by cells after exposure to heparin and heparan sulfate. Treatment of cells with heparitinase and heparinase induced a decrease in the binding of 125I-labeled PF4 to cells. Binding of 125I-labeled PF4 was partially inhibited by the presence of increasing concentrations of protamine sulfate and basic fibroblast growth factor. To test whether PF4 bound to cell surface proteoglycans, proteoglycan synthesis was inhibited by using 4-methylumbelliferyl-β-D-xyloside. The binding of 125I-labeled PF4 on treated cells was decreased, and xyloside treatment of cells abrogated the biologic activity of PF4 in a plasma clot culture system. The inhibitory effect of PF4 was retained in a serum-free agar culture system, which indicates that the binding of PF4 to HEL cells induces cell growth inhibition in a direct fashion. 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Medicine</title><publicationDate>1996</publicationDate></host><categories><wos></wos><scienceMetrix><json:string>health sciences</json:string><json:string>clinical medicine</json:string><json:string>general clinical medicine</json:string></scienceMetrix></categories><publicationDate>1996</publicationDate><copyrightDate>1996</copyrightDate><doi><json:string>10.1016/S0022-2143(96)90186-9</json:string></doi><id>BE8E1B2D601E90039E3349EB6C2A299D7FD5DD5A</id><score>0.14996392</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/BE8E1B2D601E90039E3349EB6C2A299D7FD5DD5A/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/BE8E1B2D601E90039E3349EB6C2A299D7FD5DD5A/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/BE8E1B2D601E90039E3349EB6C2A299D7FD5DD5A/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a">Inhibitory effect of platelet factor 4 on human erythroleukemic cells is dependent on cell surface heparan sulfate</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>ELSEVIER</publisher><availability><p>ELSEVIER</p></availability><date>1996</date></publicationStmt><notesStmt><note>Supported by the Caisse Nationale de l'Assurance Maladie des Travailleurs Salariés (CNAMTS) in association with the Institut National de la Santé etde la Recherche Médicale. A-M. M. is a recipient of a studentship from La Ligue Contre Le Cancer de La Manche, France.</note><note type="content">Section title: Original article</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Inhibitory effect of platelet factor 4 on human erythroleukemic cells is dependent on cell surface heparan sulfate</title><author xml:id="author-1"><persName><forename type="first">Anne-Marie</forename><surname>Maurer</surname></persName><affiliation>INSERM U 409, Hôpital Beaujon, Clichy, France</affiliation><affiliation>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</affiliation><affiliation>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</affiliation></author><author xml:id="author-2"><persName><forename type="first">Zhong Chao</forename><surname>Han</surname></persName><affiliation>INSERM U 409, Hôpital Beaujon, Clichy, France</affiliation><affiliation>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</affiliation><affiliation>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</affiliation></author><author xml:id="author-3"><persName><forename type="first">Didier</forename><surname>Dhermy</surname></persName><affiliation>INSERM U 409, Hôpital Beaujon, Clichy, France</affiliation><affiliation>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</affiliation><affiliation>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</affiliation></author><author xml:id="author-4"><persName><forename type="first">Jean</forename><surname>Briere</surname></persName><affiliation>Reprint requests: Professor Jean Brière, Service d'hématologie clinique, Hôpital Beaujon, 100, Boulevard du Général Leclerc, 92118 Clichy Cédex, France.</affiliation><affiliation>INSERM U 409, Hôpital Beaujon, Clichy, France</affiliation><affiliation>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</affiliation><affiliation>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</affiliation></author></analytic><monogr><title level="j">The Journal of Laboratory and Clinical Medicine</title><title level="j" type="abbrev">YMLC</title><idno type="pISSN">0022-2143</idno><idno type="PII">S0022-2143(00)X0079-0</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1996"></date><biblScope unit="volume">127</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="382">382</biblScope><biblScope unit="page" to="390">390</biblScope></imprint></monogr><idno type="istex">BE8E1B2D601E90039E3349EB6C2A299D7FD5DD5A</idno><idno type="DOI">10.1016/S0022-2143(96)90186-9</idno><idno type="PII">S0022-2143(96)90186-9</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1996</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>We have previously reported that platelet factor 4 (PF4) inhibits human erythroleukemic (HEL) cell growth in a dose-dependent fashion in vitro and that PF4 binds to HEL cells in a specific, saturable, and concentration-dependent manner. In this article we demonstrate that the binding of PF4 on HEL cells and its inhibitiroy effect on HEL cell growth were mediated by heparan sulfate. We found that binding of iodine 125-labeled PF4 to HEL cells was inhibited by heparin, heparan sulfate, and dermatan sulfate and to a smaller extent by chondroitin sulfate. Ninety percent of 125I-labeled PF4 bound to HEL cells was released by cells after exposure to heparin and heparan sulfate. Treatment of cells with heparitinase and heparinase induced a decrease in the binding of 125I-labeled PF4 to cells. Binding of 125I-labeled PF4 was partially inhibited by the presence of increasing concentrations of protamine sulfate and basic fibroblast growth factor. To test whether PF4 bound to cell surface proteoglycans, proteoglycan synthesis was inhibited by using 4-methylumbelliferyl-β-D-xyloside. The binding of 125I-labeled PF4 on treated cells was decreased, and xyloside treatment of cells abrogated the biologic activity of PF4 in a plasma clot culture system. The inhibitory effect of PF4 was retained in a serum-free agar culture system, which indicates that the binding of PF4 to HEL cells induces cell growth inhibition in a direct fashion. Taken together, these findings suggest that PF4 directly acts on HEL cell growth by fixation on heparan sulfate proteoglycans on the HEL cell surface.</p></abstract><textClass><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>bFGF = basic fibroblast growth factor</term></item><item><term>BSA = bovine serum albumin</term></item><item><term>CS = chondroitin sulfate</term></item><item><term>DS = dermatan sulfate</term></item><item><term>FCS = fetal calf serum</term></item><item><term>GAG = glycosaminoglycan</term></item><item><term>HEL = human erythroleukemic</term></item><item><term>HEPES = N-2-hydroxyethylpiperazine-N-2-ethanesulfonic acid</term></item><item><term>HS = heparan sulfate</term></item><item><term>PBS = phosphate-buffered saline solution</term></item><item><term>PF4 = platelet factor 4</term></item><item><term>TBS = Tris-buffered saline solution</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1995-11-07">Modified</change><change when="1996">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/BE8E1B2D601E90039E3349EB6C2A299D7FD5DD5A/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>YMLC</jid><aid>96901869</aid><ce:pii>S0022-2143(96)90186-9</ce:pii><ce:doi>10.1016/S0022-2143(96)90186-9</ce:doi><ce:copyright type="unknown" year="1996"></ce:copyright></item-info><head><ce:article-footnote><ce:label>☆</ce:label><ce:note-para>Supported by the Caisse Nationale de l'Assurance Maladie des Travailleurs Salariés (CNAMTS) in association with the Institut National de la Santé etde la Recherche Médicale. A-M. M. is a recipient of a studentship from La Ligue Contre Le Cancer de La Manche, France.</ce:note-para></ce:article-footnote><ce:dochead><ce:textfn>Original article</ce:textfn></ce:dochead><ce:title>Inhibitory effect of platelet factor 4 on human erythroleukemic cells is dependent on cell surface heparan sulfate</ce:title><ce:author-group><ce:author><ce:given-name>Anne-Marie</ce:given-name><ce:surname>Maurer</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF3"><ce:sup>c</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Zhong Chao</ce:given-name><ce:surname>Han</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF3"><ce:sup>c</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Didier</ce:given-name><ce:surname>Dhermy</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF3"><ce:sup>c</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Jean</ce:given-name><ce:surname>Briere</ce:surname><ce:cross-ref refid="COR1"><ce:sup>∗</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF3"><ce:sup>c</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>INSERM U 409, Hôpital Beaujon, Clichy, France</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</ce:textfn></ce:affiliation><ce:affiliation id="AFF3"><ce:label>c</ce:label><ce:textfn>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>∗</ce:label><ce:text>Reprint requests: Professor Jean Brière, Service d'hématologie clinique, Hôpital Beaujon, 100, Boulevard du Général Leclerc, 92118 Clichy Cédex, France.</ce:text></ce:correspondence></ce:author-group><ce:date-received day="1" month="8" year="1994"></ce:date-received><ce:date-revised day="7" month="11" year="1995"></ce:date-revised><ce:date-accepted day="29" month="11" year="1995"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>We have previously reported that platelet factor 4 (PF4) inhibits human erythroleukemic (HEL) cell growth in a dose-dependent fashion in vitro and that PF4 binds to HEL cells in a specific, saturable, and concentration-dependent manner. In this article we demonstrate that the binding of PF4 on HEL cells and its inhibitiroy effect on HEL cell growth were mediated by heparan sulfate. We found that binding of iodine 125-labeled PF4 to HEL cells was inhibited by heparin, heparan sulfate, and dermatan sulfate and to a smaller extent by chondroitin sulfate. Ninety percent of <ce:sup loc="pre">125</ce:sup>I-labeled PF4 bound to HEL cells was released by cells after exposure to heparin and heparan sulfate. Treatment of cells with heparitinase and heparinase induced a decrease in the binding of <ce:sup>125</ce:sup>I-labeled PF4 to cells. Binding of <ce:sup loc="pre">125</ce:sup>I-labeled PF4 was partially inhibited by the presence of increasing concentrations of protamine sulfate and basic fibroblast growth factor. To test whether PF4 bound to cell surface proteoglycans, proteoglycan synthesis was inhibited by using 4-methylumbelliferyl-β-D-xyloside. The binding of <ce:sup loc="pre">125</ce:sup>I-labeled PF4 on treated cells was decreased, and xyloside treatment of cells abrogated the biologic activity of PF4 in a plasma clot culture system. The inhibitory effect of PF4 was retained in a serum-free agar culture system, which indicates that the binding of PF4 to HEL cells induces cell growth inhibition in a direct fashion. Taken together, these findings suggest that PF4 directly acts on HEL cell growth by fixation on heparan sulfate proteoglycans on the HEL cell surface.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title><ce:keyword><ce:text>bFGF = basic fibroblast growth factor</ce:text></ce:keyword><ce:keyword><ce:text>BSA = bovine serum albumin</ce:text></ce:keyword><ce:keyword><ce:text>CS = chondroitin sulfate</ce:text></ce:keyword><ce:keyword><ce:text>DS = dermatan sulfate</ce:text></ce:keyword><ce:keyword><ce:text>FCS = fetal calf serum</ce:text></ce:keyword><ce:keyword><ce:text>GAG = glycosaminoglycan</ce:text></ce:keyword><ce:keyword><ce:text>HEL = human erythroleukemic</ce:text></ce:keyword><ce:keyword><ce:text>HEPES = N-2-hydroxyethylpiperazine-N-2-ethanesulfonic acid</ce:text></ce:keyword><ce:keyword><ce:text>HS = heparan sulfate</ce:text></ce:keyword><ce:keyword><ce:text>PBS = phosphate-buffered saline solution</ce:text></ce:keyword><ce:keyword><ce:text>PF4 = platelet factor 4</ce:text></ce:keyword><ce:keyword><ce:text>TBS = Tris-buffered saline solution</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Inhibitory effect of platelet factor 4 on human erythroleukemic cells is dependent on cell surface heparan sulfate</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Inhibitory effect of platelet factor 4 on human erythroleukemic cells is dependent on cell surface heparan sulfate</title></titleInfo><name type="personal"><namePart type="given">Anne-Marie</namePart><namePart type="family">Maurer</namePart><affiliation>INSERM U 409, Hôpital Beaujon, Clichy, France</affiliation><affiliation>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</affiliation><affiliation>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Zhong Chao</namePart><namePart type="family">Han</namePart><affiliation>INSERM U 409, Hôpital Beaujon, Clichy, France</affiliation><affiliation>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</affiliation><affiliation>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Didier</namePart><namePart type="family">Dhermy</namePart><affiliation>INSERM U 409, Hôpital Beaujon, Clichy, France</affiliation><affiliation>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</affiliation><affiliation>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jean</namePart><namePart type="family">Briere</namePart><affiliation>Reprint requests: Professor Jean Brière, Service d'hématologie clinique, Hôpital Beaujon, 100, Boulevard du Général Leclerc, 92118 Clichy Cédex, France.</affiliation><affiliation>INSERM U 409, Hôpital Beaujon, Clichy, France</affiliation><affiliation>Institut des Vaisseaux et du Sang, Hôpital Lariboisière, Paris, France</affiliation><affiliation>Service d'hématologie clinique, Hôpital Beaujon, Clichy, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article"></genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1996</dateIssued><dateModified encoding="w3cdtf">1995-11-07</dateModified><copyrightDate encoding="w3cdtf">1996</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="en">We have previously reported that platelet factor 4 (PF4) inhibits human erythroleukemic (HEL) cell growth in a dose-dependent fashion in vitro and that PF4 binds to HEL cells in a specific, saturable, and concentration-dependent manner. In this article we demonstrate that the binding of PF4 on HEL cells and its inhibitiroy effect on HEL cell growth were mediated by heparan sulfate. We found that binding of iodine 125-labeled PF4 to HEL cells was inhibited by heparin, heparan sulfate, and dermatan sulfate and to a smaller extent by chondroitin sulfate. Ninety percent of 125I-labeled PF4 bound to HEL cells was released by cells after exposure to heparin and heparan sulfate. Treatment of cells with heparitinase and heparinase induced a decrease in the binding of 125I-labeled PF4 to cells. Binding of 125I-labeled PF4 was partially inhibited by the presence of increasing concentrations of protamine sulfate and basic fibroblast growth factor. To test whether PF4 bound to cell surface proteoglycans, proteoglycan synthesis was inhibited by using 4-methylumbelliferyl-β-D-xyloside. The binding of 125I-labeled PF4 on treated cells was decreased, and xyloside treatment of cells abrogated the biologic activity of PF4 in a plasma clot culture system. The inhibitory effect of PF4 was retained in a serum-free agar culture system, which indicates that the binding of PF4 to HEL cells induces cell growth inhibition in a direct fashion. Taken together, these findings suggest that PF4 directly acts on HEL cell growth by fixation on heparan sulfate proteoglycans on the HEL cell surface.</abstract><note>Supported by the Caisse Nationale de l'Assurance Maladie des Travailleurs Salariés (CNAMTS) in association with the Institut National de la Santé etde la Recherche Médicale. A-M. M. is a recipient of a studentship from La Ligue Contre Le Cancer de La Manche, France.</note><note type="content">Section title: Original article</note><subject><genre>Abbreviations</genre><topic>bFGF = basic fibroblast growth factor</topic><topic>BSA = bovine serum albumin</topic><topic>CS = chondroitin sulfate</topic><topic>DS = dermatan sulfate</topic><topic>FCS = fetal calf serum</topic><topic>GAG = glycosaminoglycan</topic><topic>HEL = human erythroleukemic</topic><topic>HEPES = N-2-hydroxyethylpiperazine-N-2-ethanesulfonic acid</topic><topic>HS = heparan sulfate</topic><topic>PBS = phosphate-buffered saline solution</topic><topic>PF4 = platelet factor 4</topic><topic>TBS = Tris-buffered saline solution</topic></subject><relatedItem type="host"><titleInfo><title>The Journal of Laboratory and Clinical Medicine</title></titleInfo><titleInfo type="abbreviated"><title>YMLC</title></titleInfo><genre type="journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">199604</dateIssued></originInfo><identifier type="ISSN">0022-2143</identifier><identifier type="PII">S0022-2143(00)X0079-0</identifier><part><date>199604</date><detail type="volume"><number>127</number><caption>vol.</caption></detail><detail type="issue"><number>4</number><caption>no.</caption></detail><extent unit="issue pages"><start>A1</start><end>A8</end></extent><extent unit="issue pages"><start>317</start><end>410</end></extent><extent unit="pages"><start>382</start><end>390</end></extent></part></relatedItem><identifier type="istex">BE8E1B2D601E90039E3349EB6C2A299D7FD5DD5A</identifier><identifier type="DOI">10.1016/S0022-2143(96)90186-9</identifier><identifier type="PII">S0022-2143(96)90186-9</identifier><recordInfo><recordContentSource>ELSEVIER</recordContentSource></recordInfo></mods></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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