Model SV40-transformed fibroblast lines for metabolic studies of human prosaposin and acid ceramidase deficiencies
Identifieur interne : 00CD82 ( Main/Exploration ); précédent : 00CD81; suivant : 00CD83Model SV40-transformed fibroblast lines for metabolic studies of human prosaposin and acid ceramidase deficiencies
Auteurs : Martine Chatelut [France] ; Klaus Harzer [Allemagne] ; Helen Christomanou [Grèce] ; Jean Feunteun [France] ; Marie-Thérèse Pieraggi [France] ; Barbara C. Paton [Australie] ; Yasuo Kishimoto [États-Unis] ; John S. O'Brien [États-Unis] ; Jean-Pierre Basile [France] ; Jean-Claude Thiers [France] ; Robert Salvayre [France] ; Thierry Levade [France]Source :
- Clinica Chimica Acta [ 0009-8981 ] ; 1997.
Descripteurs français
- Pascal (Inist)
- Wicri :
- topic : Homme.
English descriptors
- KwdEn :
- Acid ceramidase, Acid ceramidase activity, Acid sphingomyelinase, Acta, Activator, Assay, Biochem, Biol, Biol chem, Biological model, Cell immortalization, Cell lines, Ceramidase, Ceramide, Chatelut, Chem, Chimica, Clinica, Clinica chimica acta, Control cells, Degradation, Established cell line, Farber, Farber disease, Fetal, Fetal sibling, Fibroblast, Gaucher, Gaucher spleen, Harzer, Human, Human prosaposin deficiency, Initiation codon, Kishimoto, Lipid, Lipids, Liquid scintillation, Loading test, Lysosomal, Lysosomal degradation, Lysosomal storage disease, Prosaposin, Prosaposin deficiency, Prosaposin gene, Pure saposin, SV40 virus, 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
Affiliations:
- Allemagne, Australie, France, Grèce, États-Unis
- Attique (région), Bade-Wurtemberg, Californie, District de Tübingen, Midi-Pyrénées, Occitanie (région administrative)
- Athènes, Toulouse, Tübingen
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Le document en format XML
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Paton</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Chemical Pathology, Women's and Children's Hospital, North Adelaide</wicri:regionArea><wicri:noRegion>North Adelaide</wicri:noRegion></affiliation></author><author><name sortKey="Kishimoto, Yasuo" sort="Kishimoto, Yasuo" uniqKey="Kishimoto Y" first="Yasuo" last="Kishimoto">Yasuo Kishimoto</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Neurosciences, University of California-San Diego, Center for Molecular Genetics, La Jolla, CA</wicri:regionArea><placeName><region type="state">Californie</region></placeName></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. 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Rangueil, F-31403 Toulouse</wicri:regionArea><wicri:noRegion>31403 Toulouse</wicri:noRegion><wicri:noRegion>F-31403 Toulouse</wicri:noRegion></affiliation></author><author><name sortKey="Levade, Thierry" sort="Levade, Thierry" uniqKey="Levade T" first="Thierry" last="Levade">Thierry Levade</name><affiliation></affiliation><affiliation wicri:level="1"><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Biochimie, “Maladies Métaboliques”, INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil, F-31403 Toulouse</wicri:regionArea><wicri:noRegion>31403 Toulouse</wicri:noRegion><wicri:noRegion>F-31403 Toulouse</wicri:noRegion></affiliation><affiliation wicri:level="1"><country wicri:rule="url">France</country></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>Biological model</term><term>Cell immortalization</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>Established cell line</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</term><term>Human prosaposin deficiency</term><term>Initiation codon</term><term>Kishimoto</term><term>Lipid</term><term>Lipids</term><term>Liquid scintillation</term><term>Loading test</term><term>Lysosomal</term><term>Lysosomal degradation</term><term>Lysosomal storage disease</term><term>Prosaposin</term><term>Prosaposin deficiency</term><term>Prosaposin gene</term><term>Pure saposin</term><term>SV40 virus</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="Pascal" xml:lang="fr"><term>Fibroblaste</term><term>Homme</term><term>Immortalisation cellulaire</term><term>Lignée cellulaire établie</term><term>Lipide</term><term>Lysosome pathologie</term><term>Modèle biologique</term><term>Saposine</term><term>Sphingolipidose héréditaire Farber</term><term>Virus SV40</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><keywords scheme="Wicri" type="topic" xml:lang="fr"><term>Homme</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><affiliations><list><country><li>Allemagne</li><li>Australie</li><li>France</li><li>Grèce</li><li>États-Unis</li></country><region><li>Attique (région)</li><li>Bade-Wurtemberg</li><li>Californie</li><li>District de Tübingen</li><li>Midi-Pyrénées</li><li>Occitanie (région administrative)</li></region><settlement><li>Athènes</li><li>Toulouse</li><li>Tübingen</li></settlement></list><tree><country name="France"><region name="Occitanie (région administrative)"><name sortKey="Chatelut, Martine" sort="Chatelut, Martine" uniqKey="Chatelut M" first="Martine" last="Chatelut">Martine Chatelut</name></region><name sortKey="Basile, Jean Pierre" sort="Basile, Jean Pierre" uniqKey="Basile J" first="Jean-Pierre" last="Basile">Jean-Pierre Basile</name><name sortKey="Feunteun, Jean" sort="Feunteun, Jean" uniqKey="Feunteun J" first="Jean" last="Feunteun">Jean Feunteun</name><name sortKey="Levade, Thierry" sort="Levade, Thierry" uniqKey="Levade T" first="Thierry" last="Levade">Thierry Levade</name><name sortKey="Levade, Thierry" sort="Levade, Thierry" uniqKey="Levade T" first="Thierry" last="Levade">Thierry Levade</name><name sortKey="Pieraggi, Marie Therese" sort="Pieraggi, Marie Therese" uniqKey="Pieraggi M" first="Marie-Thérèse" last="Pieraggi">Marie-Thérèse Pieraggi</name><name sortKey="Salvayre, Robert" sort="Salvayre, Robert" uniqKey="Salvayre R" first="Robert" last="Salvayre">Robert Salvayre</name><name sortKey="Thiers, Jean Claude" sort="Thiers, Jean Claude" uniqKey="Thiers J" first="Jean-Claude" last="Thiers">Jean-Claude Thiers</name></country><country name="Allemagne"><region name="Bade-Wurtemberg"><name sortKey="Harzer, Klaus" sort="Harzer, Klaus" uniqKey="Harzer K" first="Klaus" last="Harzer">Klaus Harzer</name></region></country><country name="Grèce"><region name="Attique (région)"><name sortKey="Christomanou, Helen" sort="Christomanou, Helen" uniqKey="Christomanou H" first="Helen" last="Christomanou">Helen Christomanou</name></region></country><country name="Australie"><noRegion><name sortKey="Paton, Barbara C" sort="Paton, Barbara C" uniqKey="Paton B" first="Barbara C." last="Paton">Barbara C. Paton</name></noRegion></country><country name="États-Unis"><region name="Californie"><name sortKey="Kishimoto, Yasuo" sort="Kishimoto, Yasuo" uniqKey="Kishimoto Y" first="Yasuo" last="Kishimoto">Yasuo Kishimoto</name></region><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></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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