Model SV40-transformed fibroblast lines for metabolic studies of human prosaposin and acid ceramidase deficiencies
Identifieur interne : 002929 ( Istex/Corpus ); précédent : 002928; suivant : 002930Model SV40-transformed fibroblast lines for metabolic studies of human prosaposin and acid ceramidase deficiencies
Auteurs : Martine Chatelut ; Klaus Harzer ; Helen Christomanou ; Jean Feunteun ; Marie-Thérèse Pieraggi ; Barbara C. Paton ; Yasuo Kishimoto ; John S. O'Brien ; Jean-Pierre Basile ; Jean-Claude Thiers ; Robert Salvayre ; Thierry LevadeSource :
- Clinica Chimica Acta [ 0009-8981 ] ; 1997.
English descriptors
- KwdEn :
- Acid ceramidase, Acid ceramidase activity, Acid sphingomyelinase, Acta, Activator, Assay, Biochem, Biol, Biol chem, Cell lines, Ceramidase, Ceramide, Chatelut, Chem, Chimica, Clinica, Clinica chimica acta, Control cells, Degradation, Farber, Farber disease, Fetal, Fetal sibling, Fibroblast, Gaucher, Gaucher spleen, Harzer, Human prosaposin deficiency, Initiation codon, Kishimoto, Lipid, Liquid scintillation, Loading test, Lysosomal, Lysosomal degradation, Prosaposin, Prosaposin deficiency, Prosaposin gene, Pure saposin, Sandhoff, Saposin, Saposins, Sibling, Skin fibroblasts, Sphingolipid, Sphingolipid activator protein, Sphingomyelin, Sphingomyelinase, Untransformed, Untransformed cells.
- Teeft :
- Acid ceramidase, Acid ceramidase activity, Acid sphingomyelinase, Acta, Activator, Assay, Biochem, Biol, Biol chem, Cell lines, Ceramidase, Ceramide, Chatelut, Chem, Chimica, Clinica, Clinica chimica acta, Control cells, Degradation, Farber, Farber disease, Fetal, Fetal sibling, Fibroblast, Gaucher, Gaucher spleen, Harzer, Human prosaposin deficiency, Initiation codon, Kishimoto, Lipid, Liquid scintillation, Loading test, Lysosomal, Lysosomal degradation, Prosaposin, Prosaposin deficiency, Prosaposin gene, Pure saposin, Sandhoff, Saposin, Saposins, Sibling, Skin fibroblasts, Sphingolipid, Sphingolipid activator protein, Sphingomyelin, Sphingomyelinase, Untransformed, Untransformed cells.
Abstract
Abstract: Skin fibroblasts from patients with Farber disease (acid ceramidase deficiency) and from two siblings of the only known family affected with prosaposin deficiency were transformed by transfection with a plasmid carrying the SV40 large T antigen. The prosaposin-deficient transformed cell lines conserved their original metabolic defects, and in particular they were free of detectable immunoreactivity when using anti-saposin B and anti-saposin C antisera. Ultrastructurally, the cells contained heterogeneous lysosomal storage products. As found for their parental cell lines, the SV40-transformed fibroblasts exhibited deficient in vitro activities of lysosomal ceramidase and β-galactosylceramidase, but a normal activity of acid sphingomyelinase. As observed for SV40-transformed fibroblasts from Farber disease, degradation of radioactive glucosylceramide or low density lipoprotein-associated radiolabelled sphingomyelin by the prosaposin-deficient cells in situ showed a clear impairment in the turnover of lysosomal ceramide. Ceramide storage in prosaposin-deficient cells was also demonstrated by ceramide mass determination. In contrast to acid ceramidase deficient cells, both the accumulation of ceramide and the reduced in vitro activity of acid ceramidase in cells from prosaposin deficiency could be corrected by addition of purified saposin D. The data confirm that prosaposin is required for lysosomal ceramide degradation, but not for sphingomyelin turnover. The SV40-transformed fibroblasts will be useful for pathophysiological studies on human prosaposin deficiency.
Url:
DOI: 10.1016/S0009-8981(97)06527-3
Links to Exploration step
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Rangueil, F-31403 Toulouse, France</mods:affiliation></affiliation></author><author><name sortKey="Harzer, Klaus" sort="Harzer, Klaus" uniqKey="Harzer K" first="Klaus" last="Harzer">Klaus Harzer</name><affiliation><mods:affiliation>Neurochemical Laboratory, Institut für Hirnforschung, University of Tübingen, Tübingen, Germany</mods:affiliation></affiliation></author><author><name sortKey="Christomanou, Helen" sort="Christomanou, Helen" uniqKey="Christomanou H" first="Helen" last="Christomanou">Helen Christomanou</name><affiliation><mods:affiliation>Laboratory of Neurochemistry and Molecular Biology, Athens, Greece</mods:affiliation></affiliation></author><author><name sortKey="Feunteun, Jean" sort="Feunteun, Jean" uniqKey="Feunteun J" first="Jean" last="Feunteun">Jean Feunteun</name><affiliation><mods:affiliation>Laboratoire de Génétique Oncologique, U.R.A. 1967 CNRS, Institut Gustave Roussy, Villejuif, France</mods:affiliation></affiliation></author><author><name sortKey="Pieraggi, Marie Therese" sort="Pieraggi, Marie Therese" uniqKey="Pieraggi M" first="Marie-Thérèse" last="Pieraggi">Marie-Thérèse Pieraggi</name><affiliation><mods:affiliation>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</mods:affiliation></affiliation></author><author><name sortKey="Paton, Barbara C" sort="Paton, Barbara C" uniqKey="Paton B" first="Barbara C." last="Paton">Barbara C. Paton</name><affiliation><mods:affiliation>Department of Chemical Pathology, Women's and Children's Hospital, North Adelaide, Australia</mods:affiliation></affiliation></author><author><name sortKey="Kishimoto, Yasuo" sort="Kishimoto, Yasuo" uniqKey="Kishimoto Y" first="Yasuo" last="Kishimoto">Yasuo Kishimoto</name><affiliation><mods:affiliation>Department of Neurosciences, University of California-San Diego, Center for Molecular Genetics, La Jolla, CA, USA</mods:affiliation></affiliation></author><author><name sortKey="O Brien, John S" sort="O Brien, John S" uniqKey="O Brien J" first="John S." last="O'Brien">John S. O'Brien</name><affiliation><mods:affiliation>Department of Neurosciences, University of California-San Diego, Center for Molecular Genetics, La Jolla, CA, USA</mods:affiliation></affiliation></author><author><name sortKey="Basile, Jean Pierre" sort="Basile, Jean Pierre" uniqKey="Basile J" first="Jean-Pierre" last="Basile">Jean-Pierre Basile</name><affiliation><mods:affiliation>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</mods:affiliation></affiliation></author><author><name sortKey="Thiers, Jean Claude" sort="Thiers, Jean Claude" uniqKey="Thiers J" first="Jean-Claude" last="Thiers">Jean-Claude Thiers</name><affiliation><mods:affiliation>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</mods:affiliation></affiliation></author><author><name sortKey="Salvayre, Robert" sort="Salvayre, Robert" uniqKey="Salvayre R" first="Robert" last="Salvayre">Robert Salvayre</name><affiliation><mods:affiliation>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</mods:affiliation></affiliation></author><author><name sortKey="Levade, Thierry" sort="Levade, Thierry" uniqKey="Levade T" first="Thierry" last="Levade">Thierry Levade</name><affiliation><mods:affiliation>Corresponding author: Tel.: (33) 05.61.32.20.60. Fax: (33) 05.61.32.29.53.</mods:affiliation></affiliation><affiliation><mods:affiliation>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</mods:affiliation></affiliation><affiliation><mods:affiliation>E-mail: levade@rangueil.inserm.fr</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Clinica Chimica Acta</title><title level="j" type="abbrev">CCA</title><idno type="ISSN">0009-8981</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1997">1997</date><biblScope unit="volume">262</biblScope><biblScope unit="issue">1–2</biblScope><biblScope unit="page" from="61">61</biblScope><biblScope unit="page" to="76">76</biblScope></imprint><idno type="ISSN">0009-8981</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0009-8981</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acid ceramidase</term><term>Acid ceramidase activity</term><term>Acid sphingomyelinase</term><term>Acta</term><term>Activator</term><term>Assay</term><term>Biochem</term><term>Biol</term><term>Biol chem</term><term>Cell lines</term><term>Ceramidase</term><term>Ceramide</term><term>Chatelut</term><term>Chem</term><term>Chimica</term><term>Clinica</term><term>Clinica chimica acta</term><term>Control cells</term><term>Degradation</term><term>Farber</term><term>Farber disease</term><term>Fetal</term><term>Fetal sibling</term><term>Fibroblast</term><term>Gaucher</term><term>Gaucher spleen</term><term>Harzer</term><term>Human prosaposin deficiency</term><term>Initiation codon</term><term>Kishimoto</term><term>Lipid</term><term>Liquid scintillation</term><term>Loading test</term><term>Lysosomal</term><term>Lysosomal degradation</term><term>Prosaposin</term><term>Prosaposin deficiency</term><term>Prosaposin gene</term><term>Pure saposin</term><term>Sandhoff</term><term>Saposin</term><term>Saposins</term><term>Sibling</term><term>Skin fibroblasts</term><term>Sphingolipid</term><term>Sphingolipid activator protein</term><term>Sphingomyelin</term><term>Sphingomyelinase</term><term>Untransformed</term><term>Untransformed cells</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Acid ceramidase</term><term>Acid ceramidase activity</term><term>Acid sphingomyelinase</term><term>Acta</term><term>Activator</term><term>Assay</term><term>Biochem</term><term>Biol</term><term>Biol chem</term><term>Cell lines</term><term>Ceramidase</term><term>Ceramide</term><term>Chatelut</term><term>Chem</term><term>Chimica</term><term>Clinica</term><term>Clinica chimica acta</term><term>Control cells</term><term>Degradation</term><term>Farber</term><term>Farber disease</term><term>Fetal</term><term>Fetal sibling</term><term>Fibroblast</term><term>Gaucher</term><term>Gaucher spleen</term><term>Harzer</term><term>Human prosaposin deficiency</term><term>Initiation codon</term><term>Kishimoto</term><term>Lipid</term><term>Liquid scintillation</term><term>Loading test</term><term>Lysosomal</term><term>Lysosomal degradation</term><term>Prosaposin</term><term>Prosaposin deficiency</term><term>Prosaposin gene</term><term>Pure saposin</term><term>Sandhoff</term><term>Saposin</term><term>Saposins</term><term>Sibling</term><term>Skin fibroblasts</term><term>Sphingolipid</term><term>Sphingolipid activator protein</term><term>Sphingomyelin</term><term>Sphingomyelinase</term><term>Untransformed</term><term>Untransformed cells</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Skin fibroblasts from patients with Farber disease (acid ceramidase deficiency) and from two siblings of the only known family affected with prosaposin deficiency were transformed by transfection with a plasmid carrying the SV40 large T antigen. The prosaposin-deficient transformed cell lines conserved their original metabolic defects, and in particular they were free of detectable immunoreactivity when using anti-saposin B and anti-saposin C antisera. Ultrastructurally, the cells contained heterogeneous lysosomal storage products. As found for their parental cell lines, the SV40-transformed fibroblasts exhibited deficient in vitro activities of lysosomal ceramidase and β-galactosylceramidase, but a normal activity of acid sphingomyelinase. As observed for SV40-transformed fibroblasts from Farber disease, degradation of radioactive glucosylceramide or low density lipoprotein-associated radiolabelled sphingomyelin by the prosaposin-deficient cells in situ showed a clear impairment in the turnover of lysosomal ceramide. Ceramide storage in prosaposin-deficient cells was also demonstrated by ceramide mass determination. In contrast to acid ceramidase deficient cells, both the accumulation of ceramide and the reduced in vitro activity of acid ceramidase in cells from prosaposin deficiency could be corrected by addition of purified saposin D. The data confirm that prosaposin is required for lysosomal ceramide degradation, but not for sphingomyelin turnover. The SV40-transformed fibroblasts will be useful for pathophysiological studies on human prosaposin deficiency.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>fibroblast</json:string><json:string>ceramide</json:string><json:string>prosaposin</json:string><json:string>lysosomal</json:string><json:string>ceramidase</json:string><json:string>saposin</json:string><json:string>farber</json:string><json:string>acta</json:string><json:string>saposins</json:string><json:string>untransformed</json:string><json:string>chatelut</json:string><json:string>lipid</json:string><json:string>clinica</json:string><json:string>activator</json:string><json:string>chimica</json:string><json:string>sphingomyelinase</json:string><json:string>clinica chimica acta</json:string><json:string>farber disease</json:string><json:string>sphingomyelin</json:string><json:string>sphingolipid</json:string><json:string>harzer</json:string><json:string>biol</json:string><json:string>sandhoff</json:string><json:string>fetal</json:string><json:string>prosaposin deficiency</json:string><json:string>kishimoto</json:string><json:string>chem</json:string><json:string>biochem</json:string><json:string>gaucher</json:string><json:string>fetal sibling</json:string><json:string>biol chem</json:string><json:string>skin fibroblasts</json:string><json:string>acid sphingomyelinase</json:string><json:string>acid ceramidase</json:string><json:string>degradation</json:string><json:string>sibling</json:string><json:string>acid ceramidase activity</json:string><json:string>prosaposin gene</json:string><json:string>control cells</json:string><json:string>cell lines</json:string><json:string>pure saposin</json:string><json:string>assay</json:string><json:string>human prosaposin deficiency</json:string><json:string>untransformed cells</json:string><json:string>lysosomal degradation</json:string><json:string>loading test</json:string><json:string>sphingolipid activator protein</json:string><json:string>initiation codon</json:string><json:string>liquid scintillation</json:string><json:string>gaucher spleen</json:string></teeft></keywords><author><json:item><name>Martine Chatelut</name><affiliations><json:string>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</json:string></affiliations></json:item><json:item><name>Klaus Harzer</name><affiliations><json:string>Neurochemical Laboratory, Institut für Hirnforschung, University of Tübingen, Tübingen, Germany</json:string></affiliations></json:item><json:item><name>Helen Christomanou</name><affiliations><json:string>Laboratory of Neurochemistry and Molecular Biology, Athens, Greece</json:string></affiliations></json:item><json:item><name>Jean Feunteun</name><affiliations><json:string>Laboratoire de Génétique Oncologique, U.R.A. 1967 CNRS, Institut Gustave Roussy, Villejuif, France</json:string></affiliations></json:item><json:item><name>Marie-Thérèse Pieraggi</name><affiliations><json:string>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</json:string></affiliations></json:item><json:item><name>Barbara C. Paton</name><affiliations><json:string>Department of Chemical Pathology, Women's and Children's Hospital, North Adelaide, Australia</json:string></affiliations></json:item><json:item><name>Yasuo Kishimoto</name><affiliations><json:string>Department of Neurosciences, University of California-San Diego, Center for Molecular Genetics, La Jolla, CA, USA</json:string></affiliations></json:item><json:item><name>John S. O'Brien</name><affiliations><json:string>Department of Neurosciences, University of California-San Diego, Center for Molecular Genetics, La Jolla, CA, USA</json:string></affiliations></json:item><json:item><name>Jean-Pierre Basile</name><affiliations><json:string>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</json:string></affiliations></json:item><json:item><name>Jean-Claude Thiers</name><affiliations><json:string>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</json:string></affiliations></json:item><json:item><name>Robert Salvayre</name><affiliations><json:string>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</json:string></affiliations></json:item><json:item><name>Thierry Levade</name><affiliations><json:string>Corresponding author: Tel.: (33) 05.61.32.20.60. Fax: (33) 05.61.32.29.53.</json:string><json:string>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</json:string><json:string>E-mail: levade@rangueil.inserm.fr</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Prosaposin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Saposin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Ceramide</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Ceramidase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Sphingomyelin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Lysosomes</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Lysosomal storage disease</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Fibroblasts (SV40-transformed)</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>SPM, sphingomyelin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>LDL, low density lipoprotein</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>TLC, thin-layer chromatography</value></json:item></subject><arkIstex>ark:/67375/6H6-HJCFQNH3-2</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: Skin fibroblasts from patients with Farber disease (acid ceramidase deficiency) and from two siblings of the only known family affected with prosaposin deficiency were transformed by transfection with a plasmid carrying the SV40 large T antigen. The prosaposin-deficient transformed cell lines conserved their original metabolic defects, and in particular they were free of detectable immunoreactivity when using anti-saposin B and anti-saposin C antisera. Ultrastructurally, the cells contained heterogeneous lysosomal storage products. As found for their parental cell lines, the SV40-transformed fibroblasts exhibited deficient in vitro activities of lysosomal ceramidase and β-galactosylceramidase, but a normal activity of acid sphingomyelinase. As observed for SV40-transformed fibroblasts from Farber disease, degradation of radioactive glucosylceramide or low density lipoprotein-associated radiolabelled sphingomyelin by the prosaposin-deficient cells in situ showed a clear impairment in the turnover of lysosomal ceramide. Ceramide storage in prosaposin-deficient cells was also demonstrated by ceramide mass determination. In contrast to acid ceramidase deficient cells, both the accumulation of ceramide and the reduced in vitro activity of acid ceramidase in cells from prosaposin deficiency could be corrected by addition of purified saposin D. The data confirm that prosaposin is required for lysosomal ceramide degradation, but not for sphingomyelin turnover. The SV40-transformed fibroblasts will be useful for pathophysiological studies on human prosaposin deficiency.</abstract><qualityIndicators><refBibsNative>true</refBibsNative><abstractWordCount>209</abstractWordCount><abstractCharCount>1597</abstractCharCount><keywordCount>11</keywordCount><score>9.508</score><pdfWordCount>5183</pdfWordCount><pdfCharCount>32055</pdfCharCount><pdfVersion>1.2</pdfVersion><pdfPageCount>16</pdfPageCount><pdfPageSize>533 x 742 pts</pdfPageSize></qualityIndicators><title>Model SV40-transformed fibroblast lines for metabolic studies of human prosaposin and acid ceramidase deficiencies</title><pmid><json:string>9204210</json:string></pmid><pii><json:string>S0009-8981(97)06527-3</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>Clinica Chimica Acta</title><language><json:string>unknown</json:string></language><publicationDate>1997</publicationDate><issn><json:string>0009-8981</json:string></issn><pii><json:string>S0009-8981(00)X0049-6</json:string></pii><volume>262</volume><issue>1–2</issue><pages><first>61</first><last>76</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1997</json:string></date><geogName></geogName><orgName><json:string>University of California-San Diego</json:string><json:string>Laboratory of Neurochemistry and Molecular Biology</json:string><json:string>Children's Hospital, North Adelaide, Australia</json:string><json:string>France, JE DRED</json:string><json:string>CJF</json:string><json:string>INSERM</json:string></orgName><orgName_funder><json:string>CJF</json:string><json:string>INSERM</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Thierry Levade</json:string><json:string>B.V. Keywords</json:string><json:string>Sandhoff</json:string><json:string>C.H.U. Rangueil</json:string><json:string>M.A. Berges</json:string><json:string>Louis Bugnard</json:string><json:string>La Jolla</json:string><json:string>Kolter</json:string><json:string>Gustave Roussy</json:string><json:string>Fetus</json:string></persName><placeName><json:string>Bristol</json:string><json:string>Germany</json:string><json:string>Greece</json:string><json:string>UK</json:string><json:string>Darmstadt</json:string><json:string>VA</json:string><json:string>USA</json:string><json:string>Athens</json:string><json:string>Toulouse</json:string><json:string>Gif-sur-Yvette</json:string><json:string>France</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>[4]</json:string><json:string>[4,27]</json:string><json:string>Christomanou et al. [23]</json:string><json:string>[29-32]</json:string><json:string>[18]</json:string><json:string>[6]</json:string><json:string>[8,26]</json:string><json:string>[1-3,7]</json:string><json:string>[4,27,28,33,34]</json:string><json:string>[22]</json:string><json:string>[8]</json:string><json:string>[17]</json:string><json:string>[5,6]</json:string><json:string>[21]</json:string><json:string>Soeda et al. [16]</json:string><json:string>[8,18]</json:string><json:string>[13,17]</json:string><json:string>[20]</json:string><json:string>[2,3,28]</json:string><json:string>[5]</json:string><json:string>[8,13]</json:string><json:string>[8,25,26]</json:string><json:string>M. Chatelut et al.</json:string><json:string>[36]</json:string><json:string>[1-3]</json:string><json:string>[9]</json:string><json:string>[35]</json:string><json:string>Klein et al. [6]</json:string><json:string>[19]</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-HJCFQNH3-2</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - medical laboratory technology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - clinical medicine</json:string><json:string>3 - general clinical medicine</json:string></scienceMetrix><scopus><json:string>1 - Health Sciences</json:string><json:string>2 - Medicine</json:string><json:string>3 - Biochemistry, medical</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 - Biochemistry</json:string><json:string>1 - Health Sciences</json:string><json:string>2 - Medicine</json:string><json:string>3 - General Medicine</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 medicales</json:string><json:string>4 - maladies metaboliques</json:string></inist></categories><publicationDate>1997</publicationDate><copyrightDate>1997</copyrightDate><doi><json:string>10.1016/S0009-8981(97)06527-3</json:string></doi><id>DCFFFFDE3F417DC08D4E382405F19004B4C73D91</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/DCFFFFDE3F417DC08D4E382405F19004B4C73D91/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/DCFFFFDE3F417DC08D4E382405F19004B4C73D91/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/DCFFFFDE3F417DC08D4E382405F19004B4C73D91/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a">Model SV40-transformed fibroblast lines for metabolic studies of human prosaposin and acid ceramidase deficiencies</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>ELSEVIER</publisher><availability><p>ELSEVIER</p></availability><date>1997</date></publicationStmt><notesStmt><note type="content">Section title: Research article</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Model SV40-transformed fibroblast lines for metabolic studies of human prosaposin and acid ceramidase deficiencies</title><author xml:id="author-0000"><persName><forename type="first">Martine</forename><surname>Chatelut</surname></persName><affiliation>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Klaus</forename><surname>Harzer</surname></persName><affiliation>Neurochemical Laboratory, Institut für Hirnforschung, University of Tübingen, Tübingen, Germany</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Helen</forename><surname>Christomanou</surname></persName><affiliation>Laboratory of Neurochemistry and Molecular Biology, Athens, Greece</affiliation></author><author xml:id="author-0003"><persName><forename type="first">Jean</forename><surname>Feunteun</surname></persName><affiliation>Laboratoire de Génétique Oncologique, U.R.A. 1967 CNRS, Institut Gustave Roussy, Villejuif, France</affiliation></author><author xml:id="author-0004"><persName><forename type="first">Marie-Thérèse</forename><surname>Pieraggi</surname></persName><affiliation>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</affiliation></author><author xml:id="author-0005"><persName><forename type="first">Barbara C.</forename><surname>Paton</surname></persName><affiliation>Department of Chemical Pathology, Women's and Children's Hospital, North Adelaide, Australia</affiliation></author><author xml:id="author-0006"><persName><forename type="first">Yasuo</forename><surname>Kishimoto</surname></persName><affiliation>Department of Neurosciences, University of California-San Diego, Center for Molecular Genetics, La Jolla, CA, USA</affiliation></author><author xml:id="author-0007"><persName><forename type="first">John S.</forename><surname>O'Brien</surname></persName><affiliation>Department of Neurosciences, University of California-San Diego, Center for Molecular Genetics, La Jolla, CA, USA</affiliation></author><author xml:id="author-0008"><persName><forename type="first">Jean-Pierre</forename><surname>Basile</surname></persName><affiliation>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</affiliation></author><author xml:id="author-0009"><persName><forename type="first">Jean-Claude</forename><surname>Thiers</surname></persName><affiliation>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</affiliation></author><author xml:id="author-0010"><persName><forename type="first">Robert</forename><surname>Salvayre</surname></persName><affiliation>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</affiliation></author><author xml:id="author-0011"><persName><forename type="first">Thierry</forename><surname>Levade</surname></persName><email>levade@rangueil.inserm.fr</email><affiliation>Corresponding author: Tel.: (33) 05.61.32.20.60. Fax: (33) 05.61.32.29.53.</affiliation><affiliation>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</affiliation></author><idno type="istex">DCFFFFDE3F417DC08D4E382405F19004B4C73D91</idno><idno type="DOI">10.1016/S0009-8981(97)06527-3</idno><idno type="PII">S0009-8981(97)06527-3</idno></analytic><monogr><title level="j">Clinica Chimica Acta</title><title level="j" type="abbrev">CCA</title><idno type="pISSN">0009-8981</idno><idno type="PII">S0009-8981(00)X0049-6</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1997"></date><biblScope unit="volume">262</biblScope><biblScope unit="issue">1–2</biblScope><biblScope unit="page" from="61">61</biblScope><biblScope unit="page" to="76">76</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1997</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Skin fibroblasts from patients with Farber disease (acid ceramidase deficiency) and from two siblings of the only known family affected with prosaposin deficiency were transformed by transfection with a plasmid carrying the SV40 large T antigen. The prosaposin-deficient transformed cell lines conserved their original metabolic defects, and in particular they were free of detectable immunoreactivity when using anti-saposin B and anti-saposin C antisera. Ultrastructurally, the cells contained heterogeneous lysosomal storage products. As found for their parental cell lines, the SV40-transformed fibroblasts exhibited deficient in vitro activities of lysosomal ceramidase and β-galactosylceramidase, but a normal activity of acid sphingomyelinase. As observed for SV40-transformed fibroblasts from Farber disease, degradation of radioactive glucosylceramide or low density lipoprotein-associated radiolabelled sphingomyelin by the prosaposin-deficient cells in situ showed a clear impairment in the turnover of lysosomal ceramide. Ceramide storage in prosaposin-deficient cells was also demonstrated by ceramide mass determination. In contrast to acid ceramidase deficient cells, both the accumulation of ceramide and the reduced in vitro activity of acid ceramidase in cells from prosaposin deficiency could be corrected by addition of purified saposin D. The data confirm that prosaposin is required for lysosomal ceramide degradation, but not for sphingomyelin turnover. The SV40-transformed fibroblasts will be useful for pathophysiological studies on human prosaposin deficiency.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>Prosaposin</term></item><item><term>Saposin</term></item><item><term>Ceramide</term></item><item><term>Ceramidase</term></item><item><term>Sphingomyelin</term></item><item><term>Lysosomes</term></item><item><term>Lysosomal storage disease</term></item><item><term>Fibroblasts (SV40-transformed)</term></item></list></keywords></textClass><textClass><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>SPM, sphingomyelin</term></item><item><term>LDL, low density lipoprotein</term></item><item><term>TLC, thin-layer chromatography</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1997-01-08">Modified</change><change when="1997">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/DCFFFFDE3F417DC08D4E382405F19004B4C73D91/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>CCA</jid><aid>97065273</aid><ce:pii>S0009-8981(97)06527-3</ce:pii><ce:doi>10.1016/S0009-8981(97)06527-3</ce:doi><ce:copyright type="unknown" year="1997"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Research article</ce:textfn></ce:dochead><ce:title>Model SV40-transformed fibroblast lines for metabolic studies of human prosaposin and acid ceramidase deficiencies</ce:title><ce:author-group><ce:author><ce:given-name>Martine</ce:given-name><ce:surname>Chatelut</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Klaus</ce:given-name><ce:surname>Harzer</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Helen</ce:given-name><ce:surname>Christomanou</ce:surname><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>Feunteun</ce:surname><ce:cross-ref refid="AFF4"><ce:sup>d</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Marie-Thérèse</ce:given-name><ce:surname>Pieraggi</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Barbara C.</ce:given-name><ce:surname>Paton</ce:surname><ce:cross-ref refid="AFF5"><ce:sup>e</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Yasuo</ce:given-name><ce:surname>Kishimoto</ce:surname><ce:cross-ref refid="AFF6"><ce:sup>f</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>John S.</ce:given-name><ce:surname>O'Brien</ce:surname><ce:cross-ref refid="AFF6"><ce:sup>f</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Jean-Pierre</ce:given-name><ce:surname>Basile</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Jean-Claude</ce:given-name><ce:surname>Thiers</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Robert</ce:given-name><ce:surname>Salvayre</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Thierry</ce:given-name><ce:surname>Levade</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:e-address>levade@rangueil.inserm.fr</ce:e-address></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Neurochemical Laboratory, Institut für Hirnforschung, University of Tübingen, Tübingen, Germany</ce:textfn></ce:affiliation><ce:affiliation id="AFF3"><ce:label>c</ce:label><ce:textfn>Laboratory of Neurochemistry and Molecular Biology, Athens, Greece</ce:textfn></ce:affiliation><ce:affiliation id="AFF4"><ce:label>d</ce:label><ce:textfn>Laboratoire de Génétique Oncologique, U.R.A. 1967 CNRS, Institut Gustave Roussy, Villejuif, France</ce:textfn></ce:affiliation><ce:affiliation id="AFF5"><ce:label>e</ce:label><ce:textfn>Department of Chemical Pathology, Women's and Children's Hospital, North Adelaide, Australia</ce:textfn></ce:affiliation><ce:affiliation id="AFF6"><ce:label>f</ce:label><ce:textfn>Department of Neurosciences, University of California-San Diego, Center for Molecular Genetics, La Jolla, CA, USA</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>∗</ce:label><ce:text>Corresponding author: Tel.: (33) 05.61.32.20.60. Fax: (33) 05.61.32.29.53.</ce:text></ce:correspondence></ce:author-group><ce:date-received day="18" month="10" year="1996"></ce:date-received><ce:date-revised day="8" month="1" year="1997"></ce:date-revised><ce:date-accepted day="9" month="1" year="1997"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Skin fibroblasts from patients with Farber disease (acid ceramidase deficiency) and from two siblings of the only known family affected with prosaposin deficiency were transformed by transfection with a plasmid carrying the SV40 large T antigen. The prosaposin-deficient transformed cell lines conserved their original metabolic defects, and in particular they were free of detectable immunoreactivity when using anti-saposin B and anti-saposin C antisera. Ultrastructurally, the cells contained heterogeneous lysosomal storage products. As found for their parental cell lines, the SV40-transformed fibroblasts exhibited deficient in vitro activities of lysosomal ceramidase and β-galactosylceramidase, but a normal activity of acid sphingomyelinase. As observed for SV40-transformed fibroblasts from Farber disease, degradation of radioactive glucosylceramide or low density lipoprotein-associated radiolabelled sphingomyelin by the prosaposin-deficient cells in situ showed a clear impairment in the turnover of lysosomal ceramide. Ceramide storage in prosaposin-deficient cells was also demonstrated by ceramide mass determination. In contrast to acid ceramidase deficient cells, both the accumulation of ceramide and the reduced in vitro activity of acid ceramidase in cells from prosaposin deficiency could be corrected by addition of purified saposin D. The data confirm that prosaposin is required for lysosomal ceramide degradation, but not for sphingomyelin turnover. The SV40-transformed fibroblasts will be useful for pathophysiological studies on human prosaposin deficiency.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Prosaposin</ce:text></ce:keyword><ce:keyword><ce:text>Saposin</ce:text></ce:keyword><ce:keyword><ce:text>Ceramide</ce:text></ce:keyword><ce:keyword><ce:text>Ceramidase</ce:text></ce:keyword><ce:keyword><ce:text>Sphingomyelin</ce:text></ce:keyword><ce:keyword><ce:text>Lysosomes</ce:text></ce:keyword><ce:keyword><ce:text>Lysosomal storage disease</ce:text></ce:keyword><ce:keyword><ce:text>Fibroblasts (SV40-transformed)</ce:text></ce:keyword></ce:keywords><ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title><ce:keyword><ce:text>SPM, sphingomyelin</ce:text></ce:keyword><ce:keyword><ce:text>LDL, low density lipoprotein</ce:text></ce:keyword><ce:keyword><ce:text>TLC, thin-layer chromatography</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Model SV40-transformed fibroblast lines for metabolic studies of human prosaposin and acid ceramidase deficiencies</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Model SV40-transformed fibroblast lines for metabolic studies of human prosaposin and acid ceramidase deficiencies</title></titleInfo><name type="personal"><namePart type="given">Martine</namePart><namePart type="family">Chatelut</namePart><affiliation>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Klaus</namePart><namePart type="family">Harzer</namePart><affiliation>Neurochemical Laboratory, Institut für Hirnforschung, University of Tübingen, Tübingen, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Helen</namePart><namePart type="family">Christomanou</namePart><affiliation>Laboratory of Neurochemistry and Molecular Biology, Athens, Greece</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jean</namePart><namePart type="family">Feunteun</namePart><affiliation>Laboratoire de Génétique Oncologique, U.R.A. 1967 CNRS, Institut Gustave Roussy, Villejuif, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Marie-Thérèse</namePart><namePart type="family">Pieraggi</namePart><affiliation>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Barbara C.</namePart><namePart type="family">Paton</namePart><affiliation>Department of Chemical Pathology, Women's and Children's Hospital, North Adelaide, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Yasuo</namePart><namePart type="family">Kishimoto</namePart><affiliation>Department of Neurosciences, University of California-San Diego, Center for Molecular Genetics, La Jolla, CA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">John S.</namePart><namePart type="family">O'Brien</namePart><affiliation>Department of Neurosciences, University of California-San Diego, Center for Molecular Genetics, La Jolla, CA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jean-Pierre</namePart><namePart type="family">Basile</namePart><affiliation>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jean-Claude</namePart><namePart type="family">Thiers</namePart><affiliation>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Robert</namePart><namePart type="family">Salvayre</namePart><affiliation>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Thierry</namePart><namePart type="family">Levade</namePart><affiliation>Corresponding author: Tel.: (33) 05.61.32.20.60. Fax: (33) 05.61.32.29.53.</affiliation><affiliation>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse, France</affiliation><affiliation>E-mail: levade@rangueil.inserm.fr</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">1997</dateIssued><dateModified encoding="w3cdtf">1997-01-08</dateModified><copyrightDate encoding="w3cdtf">1997</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: Skin fibroblasts from patients with Farber disease (acid ceramidase deficiency) and from two siblings of the only known family affected with prosaposin deficiency were transformed by transfection with a plasmid carrying the SV40 large T antigen. The prosaposin-deficient transformed cell lines conserved their original metabolic defects, and in particular they were free of detectable immunoreactivity when using anti-saposin B and anti-saposin C antisera. Ultrastructurally, the cells contained heterogeneous lysosomal storage products. As found for their parental cell lines, the SV40-transformed fibroblasts exhibited deficient in vitro activities of lysosomal ceramidase and β-galactosylceramidase, but a normal activity of acid sphingomyelinase. As observed for SV40-transformed fibroblasts from Farber disease, degradation of radioactive glucosylceramide or low density lipoprotein-associated radiolabelled sphingomyelin by the prosaposin-deficient cells in situ showed a clear impairment in the turnover of lysosomal ceramide. Ceramide storage in prosaposin-deficient cells was also demonstrated by ceramide mass determination. In contrast to acid ceramidase deficient cells, both the accumulation of ceramide and the reduced in vitro activity of acid ceramidase in cells from prosaposin deficiency could be corrected by addition of purified saposin D. The data confirm that prosaposin is required for lysosomal ceramide degradation, but not for sphingomyelin turnover. The SV40-transformed fibroblasts will be useful for pathophysiological studies on human prosaposin deficiency.</abstract><note type="content">Section title: Research article</note><subject><genre>Keywords</genre><topic>Prosaposin</topic><topic>Saposin</topic><topic>Ceramide</topic><topic>Ceramidase</topic><topic>Sphingomyelin</topic><topic>Lysosomes</topic><topic>Lysosomal storage disease</topic><topic>Fibroblasts (SV40-transformed)</topic></subject><subject><genre>Abbreviations</genre><topic>SPM, sphingomyelin</topic><topic>LDL, low density lipoprotein</topic><topic>TLC, thin-layer chromatography</topic></subject><relatedItem type="host"><titleInfo><title>Clinica Chimica Acta</title></titleInfo><titleInfo type="abbreviated"><title>CCA</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">19970627</dateIssued></originInfo><identifier type="ISSN">0009-8981</identifier><identifier type="PII">S0009-8981(00)X0049-6</identifier><part><date>19970627</date><detail type="volume"><number>262</number><caption>vol.</caption></detail><detail type="issue"><number>1–2</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>165</end></extent><extent unit="pages"><start>61</start><end>76</end></extent></part></relatedItem><identifier type="istex">DCFFFFDE3F417DC08D4E382405F19004B4C73D91</identifier><identifier type="ark">ark:/67375/6H6-HJCFQNH3-2</identifier><identifier type="DOI">10.1016/S0009-8981(97)06527-3</identifier><identifier type="PII">S0009-8981(97)06527-3</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/document/DCFFFFDE3F417DC08D4E382405F19004B4C73D91/metadata/json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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