Synthesis of membrane‐ and matrix‐bound colony‐stimulating factor‐1 by cultured osteoblasts
Identifieur interne : 002628 ( Istex/Corpus ); précédent : 002627; suivant : 002629Synthesis of membrane‐ and matrix‐bound colony‐stimulating factor‐1 by cultured osteoblasts
Auteurs : Rolf Felix ; Judit Halasy-Nagy ; Antoinette Wetterwald ; Marco G. Cecchini ; Herbert Fleisch ; Willy HofstetterSource :
- Journal of Cellular Physiology [ 0021-9541 ] ; 1996-02.
English descriptors
- KwdEn :
- Antiserum, Antonioli corboz, Ascorbate, Biol, Bone resorption, Cecchini, Cell layer, Cell layers, Cell line, Cell lines, Cell membrane, Cell number, Confluence, Control serum, Cydmet, Cytokine, Encoding, Exon, Exposure time, Extracellular matrix, Fleisch, Glycosaminoglycan chain, Growth factor, Hofstetter, Human cells, Hybridization, Macrophage, Macrophage cell line, Macrophage colony, Macrophage factor, Matrix, Mature osteoclasts, Membrane, Membrane fractions, Molecular forms, Murine, Nacl, Nonreducing, Nonreducing conditions, Ohtsuki, Oplop mouse, Osteoblast, Osteoblastic, Osteoblastic cells, Osteoclast, Osteoclast formation, Precursor, Present study, Primary osteoblasts, Primer, Primer pairs, Proteoglycan, Proteoglycan form, Receptor, Resorption, Rettenmier, Southern hybridization, Stromal cells, Supernatant, Suzu, Transcript, Transcripts encoding, Trypsin.
- Teeft :
- Antiserum, Antonioli corboz, Ascorbate, Biol, Bone resorption, Cecchini, Cell layer, Cell layers, Cell line, Cell lines, Cell membrane, Cell number, Confluence, Control serum, Cydmet, Cytokine, Encoding, Exon, Exposure time, Extracellular matrix, Fleisch, Glycosaminoglycan chain, Growth factor, Hofstetter, Human cells, Hybridization, Macrophage, Macrophage cell line, Macrophage colony, Macrophage factor, Matrix, Mature osteoclasts, Membrane, Membrane fractions, Molecular forms, Murine, Nacl, Nonreducing, Nonreducing conditions, Ohtsuki, Oplop mouse, Osteoblast, Osteoblastic, Osteoblastic cells, Osteoclast, Osteoclast formation, Precursor, Present study, Primary osteoblasts, Primer, Primer pairs, Proteoglycan, Proteoglycan form, Receptor, Resorption, Rettenmier, Southern hybridization, Stromal cells, Supernatant, Suzu, Transcript, Transcripts encoding, Trypsin.
Abstract
Colony‐stimulating factor‐1 (CSF‐1) is synthesized as a secreted or membrane‐bound molecule. We investigated whether osteoblastic cells produce these forms of CSF‐1. Glutaraldehyde‐fixed cell layers supported proliferation of the macrophage cell line BAC1.2F5, suggesting the presence of membrane‐ or/and matrix‐associated CSF‐1. Furthermore, CSF‐1 activity could be either extracted from the matrix or released from the cell membrane. A neutralizing antiserum against CSF‐1 inhibited these activities. After labeling the cellular proteins with [35S] met/cys or [35S] SO2−4, CSF‐1 was immunoprecipitated and analyzed by SDS‐PAGE. Under nonreducing conditions, bands with MW more than 200, 200, 100, and 50 kd were detected. These bands shifted to lower MW under reducing conditions. Treatment with chondroitin lyase ABC decreased the MW of the 200 kd monomer, proving the proteoglycan structure. Much smaller quantities of CSF‐1 were found in the matrix extract than in the conditioned medium. Transforming growth factor β (TGF‐β) increased both the synthesis of CSF‐1 and its accumulation in the matrix. CSF‐1 released with trypsin from the membrane fraction yielded on SDS‐PAGE a band with MW of 60 and 30 kd under nonreducing and reducing conditions, respectively. Transcripts encoding both the secreted and the membrane‐associated forms of the cytokine were detected in osteoblasts by reverse transcription polymerase chain reaction. These data indicate that osteoblastic cells produce the secreted forms, either remaining in the culture supernatant, or being associated to the matrix, and the membrane associated form of CSF‐1. © 1996 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/(SICI)1097-4652(199602)166:2<311::AID-JCP9>3.0.CO;2-S
Links to Exploration step
ISTEX:4DDD30574F738F22FF7A54ACB6BBE13CA40BB1C9Le document en format XML
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Cecchini</name><affiliation><mods:affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</mods:affiliation></affiliation></author><author><name sortKey="Fleisch, Herbert" sort="Fleisch, Herbert" uniqKey="Fleisch H" first="Herbert" last="Fleisch">Herbert Fleisch</name><affiliation><mods:affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</mods:affiliation></affiliation></author><author><name sortKey="Hofstetter, Willy" sort="Hofstetter, Willy" uniqKey="Hofstetter W" first="Willy" last="Hofstetter">Willy Hofstetter</name><affiliation><mods:affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:4DDD30574F738F22FF7A54ACB6BBE13CA40BB1C9</idno><date when="1996" year="1996">1996</date><idno type="doi">10.1002/(SICI)1097-4652(199602)166:2<311::AID-JCP9>3.0.CO;2-S</idno><idno type="url">https://api.istex.fr/document/4DDD30574F738F22FF7A54ACB6BBE13CA40BB1C9/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">002628</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">002628</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Synthesis of membrane‐ and matrix‐bound colony‐stimulating factor‐1 by cultured osteoblasts</title><author><name sortKey="Felix, Rolf" sort="Felix, Rolf" uniqKey="Felix R" first="Rolf" last="Felix">Rolf Felix</name><affiliation><mods:affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</mods:affiliation></affiliation><affiliation><mods:affiliation>Correspondence address: Department of Pathophysiology, University of Berne, Murtenstrasse 35, CH‐3010 Berne, Switzerland</mods:affiliation></affiliation></author><author><name sortKey="Halasy Agy, Judit" sort="Halasy Agy, Judit" uniqKey="Halasy Agy J" first="Judit" last="Halasy-Nagy">Judit Halasy-Nagy</name><affiliation><mods:affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</mods:affiliation></affiliation></author><author><name sortKey="Wetterwald, Antoinette" sort="Wetterwald, Antoinette" uniqKey="Wetterwald A" first="Antoinette" last="Wetterwald">Antoinette Wetterwald</name><affiliation><mods:affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</mods:affiliation></affiliation></author><author><name sortKey="Cecchini, Marco G" sort="Cecchini, Marco G" uniqKey="Cecchini M" first="Marco G." last="Cecchini">Marco G. Cecchini</name><affiliation><mods:affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</mods:affiliation></affiliation></author><author><name sortKey="Fleisch, Herbert" sort="Fleisch, Herbert" uniqKey="Fleisch H" first="Herbert" last="Fleisch">Herbert Fleisch</name><affiliation><mods:affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</mods:affiliation></affiliation></author><author><name sortKey="Hofstetter, Willy" sort="Hofstetter, Willy" uniqKey="Hofstetter W" first="Willy" last="Hofstetter">Willy Hofstetter</name><affiliation><mods:affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Journal of Cellular Physiology</title><title level="j" type="alt">JOURNAL OF CELLULAR PHYSIOLOGY</title><idno type="ISSN">0021-9541</idno><idno type="eISSN">1097-4652</idno><imprint><biblScope unit="vol">166</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="311">311</biblScope><biblScope unit="page" to="322">322</biblScope><biblScope unit="page-count">12</biblScope><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="1996-02">1996-02</date></imprint><idno type="ISSN">0021-9541</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0021-9541</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antiserum</term><term>Antonioli corboz</term><term>Ascorbate</term><term>Biol</term><term>Bone resorption</term><term>Cecchini</term><term>Cell layer</term><term>Cell layers</term><term>Cell line</term><term>Cell lines</term><term>Cell membrane</term><term>Cell number</term><term>Confluence</term><term>Control serum</term><term>Cydmet</term><term>Cytokine</term><term>Encoding</term><term>Exon</term><term>Exposure time</term><term>Extracellular matrix</term><term>Fleisch</term><term>Glycosaminoglycan chain</term><term>Growth factor</term><term>Hofstetter</term><term>Human cells</term><term>Hybridization</term><term>Macrophage</term><term>Macrophage cell line</term><term>Macrophage colony</term><term>Macrophage factor</term><term>Matrix</term><term>Mature osteoclasts</term><term>Membrane</term><term>Membrane fractions</term><term>Molecular forms</term><term>Murine</term><term>Nacl</term><term>Nonreducing</term><term>Nonreducing conditions</term><term>Ohtsuki</term><term>Oplop mouse</term><term>Osteoblast</term><term>Osteoblastic</term><term>Osteoblastic cells</term><term>Osteoclast</term><term>Osteoclast formation</term><term>Precursor</term><term>Present study</term><term>Primary osteoblasts</term><term>Primer</term><term>Primer pairs</term><term>Proteoglycan</term><term>Proteoglycan form</term><term>Receptor</term><term>Resorption</term><term>Rettenmier</term><term>Southern hybridization</term><term>Stromal cells</term><term>Supernatant</term><term>Suzu</term><term>Transcript</term><term>Transcripts encoding</term><term>Trypsin</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Antiserum</term><term>Antonioli corboz</term><term>Ascorbate</term><term>Biol</term><term>Bone resorption</term><term>Cecchini</term><term>Cell layer</term><term>Cell layers</term><term>Cell line</term><term>Cell lines</term><term>Cell membrane</term><term>Cell number</term><term>Confluence</term><term>Control serum</term><term>Cydmet</term><term>Cytokine</term><term>Encoding</term><term>Exon</term><term>Exposure time</term><term>Extracellular matrix</term><term>Fleisch</term><term>Glycosaminoglycan chain</term><term>Growth factor</term><term>Hofstetter</term><term>Human cells</term><term>Hybridization</term><term>Macrophage</term><term>Macrophage cell line</term><term>Macrophage colony</term><term>Macrophage factor</term><term>Matrix</term><term>Mature osteoclasts</term><term>Membrane</term><term>Membrane fractions</term><term>Molecular forms</term><term>Murine</term><term>Nacl</term><term>Nonreducing</term><term>Nonreducing conditions</term><term>Ohtsuki</term><term>Oplop mouse</term><term>Osteoblast</term><term>Osteoblastic</term><term>Osteoblastic cells</term><term>Osteoclast</term><term>Osteoclast formation</term><term>Precursor</term><term>Present study</term><term>Primary osteoblasts</term><term>Primer</term><term>Primer pairs</term><term>Proteoglycan</term><term>Proteoglycan form</term><term>Receptor</term><term>Resorption</term><term>Rettenmier</term><term>Southern hybridization</term><term>Stromal cells</term><term>Supernatant</term><term>Suzu</term><term>Transcript</term><term>Transcripts encoding</term><term>Trypsin</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Colony‐stimulating factor‐1 (CSF‐1) is synthesized as a secreted or membrane‐bound molecule. We investigated whether osteoblastic cells produce these forms of CSF‐1. Glutaraldehyde‐fixed cell layers supported proliferation of the macrophage cell line BAC1.2F5, suggesting the presence of membrane‐ or/and matrix‐associated CSF‐1. Furthermore, CSF‐1 activity could be either extracted from the matrix or released from the cell membrane. A neutralizing antiserum against CSF‐1 inhibited these activities. After labeling the cellular proteins with [35S] met/cys or [35S] SO2−4, CSF‐1 was immunoprecipitated and analyzed by SDS‐PAGE. Under nonreducing conditions, bands with MW more than 200, 200, 100, and 50 kd were detected. These bands shifted to lower MW under reducing conditions. Treatment with chondroitin lyase ABC decreased the MW of the 200 kd monomer, proving the proteoglycan structure. Much smaller quantities of CSF‐1 were found in the matrix extract than in the conditioned medium. Transforming growth factor β (TGF‐β) increased both the synthesis of CSF‐1 and its accumulation in the matrix. CSF‐1 released with trypsin from the membrane fraction yielded on SDS‐PAGE a band with MW of 60 and 30 kd under nonreducing and reducing conditions, respectively. Transcripts encoding both the secreted and the membrane‐associated forms of the cytokine were detected in osteoblasts by reverse transcription polymerase chain reaction. These data indicate that osteoblastic cells produce the secreted forms, either remaining in the culture supernatant, or being associated to the matrix, and the membrane associated form of CSF‐1. © 1996 Wiley‐Liss, Inc.</div></front></TEI><istex><corpusName>wiley</corpusName><keywords><teeft><json:string>osteoblast</json:string><json:string>macrophage</json:string><json:string>matrix</json:string><json:string>osteoclast</json:string><json:string>cytokine</json:string><json:string>osteoblastic</json:string><json:string>trypsin</json:string><json:string>proteoglycan</json:string><json:string>exon</json:string><json:string>primer</json:string><json:string>encoding</json:string><json:string>ascorbate</json:string><json:string>primary osteoblasts</json:string><json:string>murine</json:string><json:string>cecchini</json:string><json:string>cydmet</json:string><json:string>nonreducing</json:string><json:string>growth factor</json:string><json:string>control serum</json:string><json:string>osteoblastic cells</json:string><json:string>receptor</json:string><json:string>resorption</json:string><json:string>confluence</json:string><json:string>hofstetter</json:string><json:string>fleisch</json:string><json:string>nacl</json:string><json:string>bone resorption</json:string><json:string>cell layer</json:string><json:string>suzu</json:string><json:string>rettenmier</json:string><json:string>hybridization</json:string><json:string>biol</json:string><json:string>transcripts encoding</json:string><json:string>precursor</json:string><json:string>ohtsuki</json:string><json:string>nonreducing conditions</json:string><json:string>cell layers</json:string><json:string>exposure time</json:string><json:string>membrane fractions</json:string><json:string>extracellular matrix</json:string><json:string>supernatant</json:string><json:string>transcript</json:string><json:string>mature osteoclasts</json:string><json:string>glycosaminoglycan chain</json:string><json:string>cell membrane</json:string><json:string>cell number</json:string><json:string>osteoclast formation</json:string><json:string>macrophage factor</json:string><json:string>macrophage colony</json:string><json:string>antiserum</json:string><json:string>antonioli corboz</json:string><json:string>macrophage cell line</json:string><json:string>primer pairs</json:string><json:string>southern hybridization</json:string><json:string>molecular forms</json:string><json:string>cell lines</json:string><json:string>cell line</json:string><json:string>stromal cells</json:string><json:string>present study</json:string><json:string>oplop mouse</json:string><json:string>human cells</json:string><json:string>proteoglycan form</json:string><json:string>membrane</json:string></teeft></keywords><author><json:item><name>Rolf Felix</name><affiliations><json:string>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</json:string><json:string>Correspondence address: Department of Pathophysiology, University of Berne, Murtenstrasse 35, CH‐3010 Berne, Switzerland</json:string></affiliations></json:item><json:item><name>Judit Halasy‐Nagy</name><affiliations><json:string>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</json:string></affiliations></json:item><json:item><name>Antoinette Wetterwald</name><affiliations><json:string>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</json:string></affiliations></json:item><json:item><name>Marco G. Cecchini</name><affiliations><json:string>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</json:string></affiliations></json:item><json:item><name>Herbert Fleisch</name><affiliations><json:string>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</json:string></affiliations></json:item><json:item><name>Willy Hofstetter</name><affiliations><json:string>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</json:string></affiliations></json:item></author><articleId><json:string>JCP9</json:string></articleId><arkIstex>ark:/67375/WNG-BPKK34T7-Z</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>Colony‐stimulating factor‐1 (CSF‐1) is synthesized as a secreted or membrane‐bound molecule. We investigated whether osteoblastic cells produce these forms of CSF‐1. Glutaraldehyde‐fixed cell layers supported proliferation of the macrophage cell line BAC1.2F5, suggesting the presence of membrane‐ or/and matrix‐associated CSF‐1. Furthermore, CSF‐1 activity could be either extracted from the matrix or released from the cell membrane. A neutralizing antiserum against CSF‐1 inhibited these activities. After labeling the cellular proteins with [35S] met/cys or [35S] SO2−4, CSF‐1 was immunoprecipitated and analyzed by SDS‐PAGE. Under nonreducing conditions, bands with MW more than 200, 200, 100, and 50 kd were detected. These bands shifted to lower MW under reducing conditions. Treatment with chondroitin lyase ABC decreased the MW of the 200 kd monomer, proving the proteoglycan structure. Much smaller quantities of CSF‐1 were found in the matrix extract than in the conditioned medium. Transforming growth factor β (TGF‐β) increased both the synthesis of CSF‐1 and its accumulation in the matrix. CSF‐1 released with trypsin from the membrane fraction yielded on SDS‐PAGE a band with MW of 60 and 30 kd under nonreducing and reducing conditions, respectively. Transcripts encoding both the secreted and the membrane‐associated forms of the cytokine were detected in osteoblasts by reverse transcription polymerase chain reaction. These data indicate that osteoblastic cells produce the secreted forms, either remaining in the culture supernatant, or being associated to the matrix, and the membrane associated form of CSF‐1. © 1996 Wiley‐Liss, Inc.</abstract><qualityIndicators><refBibsNative>true</refBibsNative><abstractWordCount>238</abstractWordCount><abstractCharCount>1656</abstractCharCount><keywordCount>0</keywordCount><score>9.856</score><pdfWordCount>8420</pdfWordCount><pdfCharCount>51539</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>12</pdfPageCount><pdfPageSize>594 x 792 pts</pdfPageSize></qualityIndicators><title>Synthesis of membrane‐ and matrix‐bound colony‐stimulating factor‐1 by cultured osteoblasts</title><genre><json:string>article</json:string></genre><host><title>Journal of Cellular Physiology</title><language><json:string>unknown</json:string></language><doi><json:string>10.1002/(ISSN)1097-4652</json:string></doi><issn><json:string>0021-9541</json:string></issn><eissn><json:string>1097-4652</json:string></eissn><publisherId><json:string>JCP</json:string></publisherId><volume>166</volume><issue>2</issue><pages><first>311</first><last>322</last><total>12</total></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>35S</json:string><json:string>1996</json:string></date><geogName></geogName><orgName><json:string>Chiron Corporation</json:string><json:string>American Type Culture Collection, Rockville, MD</json:string><json:string>Showa University</json:string><json:string>Millipore Corporation</json:string><json:string>Academic Press Ltd., London</json:string><json:string>Bachem</json:string><json:string>Department of Developmental and Molecular Biology</json:string><json:string>A Laboratory Manual</json:string><json:string>Ohu University</json:string><json:string>Biochem</json:string><json:string>Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY</json:string><json:string>Switzerland Colony</json:string><json:string>Wiley-Liss, Inc</json:string><json:string>Department of Pathophysiology, University of Berne, Murtenstrasse</json:string><json:string>LISS, INC.</json:string><json:string>Medicine Yeshiva University</json:string><json:string>Celtrix Laboratories, Palo Alto</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Albert Einstein</json:string><json:string>J. 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Haematol</json:string></persName><placeName><json:string>Bubendorf</json:string><json:string>M.E.</json:string><json:string>Switzerland</json:string><json:string>Germany</json:string><json:string>Emeryville</json:string><json:string>Makishima</json:string><json:string>Martin</json:string><json:string>Boston</json:string><json:string>Kawashima</json:string><json:string>Jackson</json:string><json:string>Japan</json:string><json:string>Kawasaki</json:string><json:string>G.A.</json:string><json:string>Tokyo</json:string><json:string>CA</json:string><json:string>MA</json:string><json:string>C.A.</json:string><json:string>Sweden</json:string><json:string>MacKay</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Yamashita et al., 1990</json:string><json:string>Antonioli Corboz et al., 1992</json:string><json:string>Shiina-Ishimi et al., 1986</json:string><json:string>Marks et al., 1993</json:string><json:string>Marks and Lane, 1976</json:string><json:string>Felix et al.</json:string><json:string>Wiktor-Jedrzejczak et al., 1982</json:string><json:string>Ohtsuki et al., 1993</json:string><json:string>Uemura et al., 1993</json:string><json:string>Kodama et al., 1981</json:string><json:string>Halenbeck et al.</json:string><json:string>Takeuchi et al., 1993</json:string><json:string>Felix et al., 1989</json:string><json:string>Hofstetter et al., 1992, 1995</json:string><json:string>Wiktor-Jedrzejczak et al., 19901</json:string><json:string>Moskalewski et al. 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1990</json:string><json:string>Takaishi et al., 1994</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/WNG-BPKK34T7-Z</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - physiology</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><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Clinical Biochemistry</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - 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uri="https://api.istex.fr/document/4DDD30574F738F22FF7A54ACB6BBE13CA40BB1C9/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Synthesis of membrane‐ and matrix‐bound colony‐stimulating factor‐1 by cultured osteoblasts</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><availability><licence>Copyright © 1996 Wiley‐Liss, Inc.</licence></availability><date type="published" when="1996-02"></date></publicationStmt><notesStmt><note type="content-type" subtype="article" source="article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</note><note type="publication-type" subtype="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note></notesStmt><sourceDesc><biblStruct type="article"><analytic><title level="a" type="main" xml:lang="en">Synthesis of membrane‐ and matrix‐bound colony‐stimulating factor‐1 by cultured osteoblasts</title><author xml:id="author-0000" role="corresp"><persName><forename type="first">Rolf</forename><surname>Felix</surname></persName><affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland<address><country key="CH"></country></address></affiliation><affiliation>Department of Pathophysiology, University of Berne, Murtenstrasse 35, CH‐3010 Berne, Switzerland</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Judit</forename><surname>Halasy‐Nagy</surname></persName><affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland<address><country key="CH"></country></address></affiliation></author><author xml:id="author-0002"><persName><forename type="first">Antoinette</forename><surname>Wetterwald</surname></persName><affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland<address><country key="CH"></country></address></affiliation></author><author xml:id="author-0003"><persName><forename type="first">Marco G.</forename><surname>Cecchini</surname></persName><affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland<address><country key="CH"></country></address></affiliation></author><author xml:id="author-0004"><persName><forename type="first">Herbert</forename><surname>Fleisch</surname></persName><affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland<address><country key="CH"></country></address></affiliation></author><author xml:id="author-0005"><persName><forename type="first">Willy</forename><surname>Hofstetter</surname></persName><affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland<address><country key="CH"></country></address></affiliation></author><idno type="istex">4DDD30574F738F22FF7A54ACB6BBE13CA40BB1C9</idno><idno type="ark">ark:/67375/WNG-BPKK34T7-Z</idno><idno type="DOI">10.1002/(SICI)1097-4652(199602)166:2<311::AID-JCP9>3.0.CO;2-S</idno><idno type="unit">JCP9</idno><idno type="toTypesetVersion">file:JCP.JCP9.pdf</idno></analytic><monogr><title level="j" type="main">Journal of Cellular Physiology</title><title level="j" type="alt">JOURNAL OF CELLULAR PHYSIOLOGY</title><idno type="pISSN">0021-9541</idno><idno type="eISSN">1097-4652</idno><idno type="book-DOI">10.1002/(ISSN)1097-4652</idno><idno type="book-part-DOI">10.1002/(SICI)1097-4652(199602)166:2<>1.0.CO;2-Z</idno><idno type="product">JCP</idno><imprint><biblScope unit="vol">166</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="311">311</biblScope><biblScope unit="page" to="322">322</biblScope><biblScope unit="page-count">12</biblScope><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="1996-02"></date></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><abstract xml:lang="en" style="main"><head>Abstract</head><p>Colony‐stimulating factor‐1 (CSF‐1) is synthesized as a secreted or membrane‐bound molecule. We investigated whether osteoblastic cells produce these forms of CSF‐1. Glutaraldehyde‐fixed cell layers supported proliferation of the macrophage cell line BAC1.2F5, suggesting the presence of membrane‐ or/and matrix‐associated CSF‐1. Furthermore, CSF‐1 activity could be either extracted from the matrix or released from the cell membrane. A neutralizing antiserum against CSF‐1 inhibited these activities. After labeling the cellular proteins with [<hi rend="superscript">35</hi>S] met/cys or [<hi rend="superscript">35</hi>S] SO<hi rend="superscript">2−</hi><hi rend="subscript">4</hi>, CSF‐1 was immunoprecipitated and analyzed by SDS‐PAGE. Under nonreducing conditions, bands with MW more than 200, 200, 100, and 50 kd were detected. These bands shifted to lower MW under reducing conditions. Treatment with chondroitin lyase ABC decreased the MW of the 200 kd monomer, proving the proteoglycan structure. Much smaller quantities of CSF‐1 were found in the matrix extract than in the conditioned medium. Transforming growth factor β (TGF‐β) increased both the synthesis of CSF‐1 and its accumulation in the matrix. CSF‐1 released with trypsin from the membrane fraction yielded on SDS‐PAGE a band with MW of 60 and 30 kd under nonreducing and reducing conditions, respectively. Transcripts encoding both the secreted and the membrane‐associated forms of the cytokine were detected in osteoblasts by reverse transcription polymerase chain reaction. These data indicate that osteoblastic cells produce the secreted forms, either remaining in the culture supernatant, or being associated to the matrix, and the membrane associated form of CSF‐1. © 1996 Wiley‐Liss, Inc.</p></abstract><langUsage><language ident="en"></language></langUsage></profileDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/4DDD30574F738F22FF7A54ACB6BBE13CA40BB1C9/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>Wiley Subscription Services, Inc., A Wiley Company</publisherName><publisherLoc>Hoboken</publisherLoc></publisherInfo><doi registered="yes">10.1002/(ISSN)1097-4652</doi><issn type="print">0021-9541</issn><issn type="electronic">1097-4652</issn><idGroup><id type="product" value="JCP"></id></idGroup><titleGroup><title type="main" xml:lang="en" sort="JOURNAL OF CELLULAR PHYSIOLOGY">Journal of Cellular Physiology</title><title type="short">J. 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We investigated whether osteoblastic cells produce these forms of CSF‐1. Glutaraldehyde‐fixed cell layers supported proliferation of the macrophage cell line BAC1.2F5, suggesting the presence of membrane‐ or/and matrix‐associated CSF‐1. Furthermore, CSF‐1 activity could be either extracted from the matrix or released from the cell membrane. A neutralizing antiserum against CSF‐1 inhibited these activities. After labeling the cellular proteins with [<sup>35</sup>S] met/cys or [<sup>35</sup>S] SO<sup>2−</sup><sub>4</sub>, CSF‐1 was immunoprecipitated and analyzed by SDS‐PAGE. Under nonreducing conditions, bands with MW more than 200, 200, 100, and 50 kd were detected. These bands shifted to lower MW under reducing conditions. Treatment with chondroitin lyase ABC decreased the MW of the 200 kd monomer, proving the proteoglycan structure. Much smaller quantities of CSF‐1 were found in the matrix extract than in the conditioned medium. Transforming growth factor β (TGF‐β) increased both the synthesis of CSF‐1 and its accumulation in the matrix. CSF‐1 released with trypsin from the membrane fraction yielded on SDS‐PAGE a band with MW of 60 and 30 kd under nonreducing and reducing conditions, respectively. Transcripts encoding both the secreted and the membrane‐associated forms of the cytokine were detected in osteoblasts by reverse transcription polymerase chain reaction. These data indicate that osteoblastic cells produce the secreted forms, either remaining in the culture supernatant, or being associated to the matrix, and the membrane associated form of CSF‐1. © 1996 Wiley‐Liss, Inc.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Synthesis of membrane‐ and matrix‐bound colony‐stimulating factor‐1 by cultured osteoblasts</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Synthesis of membrane‐ and matrix‐bound colony‐stimulating factor‐1 by cultured osteoblasts</title></titleInfo><name type="personal"><namePart type="given">Rolf</namePart><namePart type="family">Felix</namePart><affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</affiliation><affiliation>Correspondence address: Department of Pathophysiology, University of Berne, Murtenstrasse 35, CH‐3010 Berne, Switzerland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Judit</namePart><namePart type="family">Halasy‐Nagy</namePart><affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Antoinette</namePart><namePart type="family">Wetterwald</namePart><affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Marco G.</namePart><namePart type="family">Cecchini</namePart><affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Herbert</namePart><namePart type="family">Fleisch</namePart><affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Willy</namePart><namePart type="family">Hofstetter</namePart><affiliation>Department of Pathophysiology, University of Berne, CH‐3010 Berne, Switzerland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</genre><originInfo><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><place><placeTerm type="text">Hoboken</placeTerm></place><dateIssued encoding="w3cdtf">1996-02</dateIssued><dateCaptured encoding="w3cdtf">1995-04-06</dateCaptured><dateValid encoding="w3cdtf">1995-07-28</dateValid><copyrightDate encoding="w3cdtf">1996</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><extent unit="figures">10</extent><extent unit="tables">1</extent><extent unit="references">52</extent></physicalDescription><abstract lang="en">Colony‐stimulating factor‐1 (CSF‐1) is synthesized as a secreted or membrane‐bound molecule. We investigated whether osteoblastic cells produce these forms of CSF‐1. Glutaraldehyde‐fixed cell layers supported proliferation of the macrophage cell line BAC1.2F5, suggesting the presence of membrane‐ or/and matrix‐associated CSF‐1. Furthermore, CSF‐1 activity could be either extracted from the matrix or released from the cell membrane. A neutralizing antiserum against CSF‐1 inhibited these activities. After labeling the cellular proteins with [35S] met/cys or [35S] SO2−4, CSF‐1 was immunoprecipitated and analyzed by SDS‐PAGE. Under nonreducing conditions, bands with MW more than 200, 200, 100, and 50 kd were detected. These bands shifted to lower MW under reducing conditions. Treatment with chondroitin lyase ABC decreased the MW of the 200 kd monomer, proving the proteoglycan structure. Much smaller quantities of CSF‐1 were found in the matrix extract than in the conditioned medium. Transforming growth factor β (TGF‐β) increased both the synthesis of CSF‐1 and its accumulation in the matrix. CSF‐1 released with trypsin from the membrane fraction yielded on SDS‐PAGE a band with MW of 60 and 30 kd under nonreducing and reducing conditions, respectively. Transcripts encoding both the secreted and the membrane‐associated forms of the cytokine were detected in osteoblasts by reverse transcription polymerase chain reaction. These data indicate that osteoblastic cells produce the secreted forms, either remaining in the culture supernatant, or being associated to the matrix, and the membrane associated form of CSF‐1. © 1996 Wiley‐Liss, Inc.</abstract><note type="funding">Swiss National Science Fdn. - No. 31‐39185.93; No. 31‐36506.92; </note><relatedItem type="host"><titleInfo><title>Journal of Cellular Physiology</title></titleInfo><titleInfo type="abbreviated"><title>J. Cell. 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