Model SV40-transformed fibroblast lines for metabolic studies of human prosaposin and acid ceramidase deficiencies
Identifieur interne : 00E120 ( Main/Merge ); précédent : 00E119; suivant : 00E121Model SV40-transformed fibroblast lines for metabolic studies of human prosaposin and acid ceramidase deficiencies
Auteurs : M. Chatelut [France] ; K. Harzer [Allemagne] ; H. Christomanou [Grèce] ; J. Feunteun [France] ; M. T. Pieraggi [France] ; B. C. Paton [Australie] ; Y. Kishimoto [États-Unis] ; J. S. Obrien [États-Unis] ; J. P. Basile [France] ; J. C. Thiers [France] ; R. Salvayre [France] ; T. Levade [France]Source :
- Clinica chimica acta [ 0009-8981 ] ; 1997.
Descripteurs français
- Pascal (Inist)
- Wicri :
- topic : Homme.
English descriptors
- KwdEn :
Abstract
Copyright (c) 1997 Elsevier Science B.V. All rights reserved. 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.
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Chatelut</name><affiliation wicri:level="3"><inist:fA14 i1="01"><s1>Laboratoire de Biochimie, Maladies Métaboliques , INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil</s1><s2>F-31403Toulouse</s2><s3>FRA</s3><sZ>1 aut.</sZ><sZ>5 aut.</sZ><sZ>9 aut.</sZ><sZ>10 aut.</sZ><sZ>11 aut.</sZ><sZ>12 aut.</sZ></inist:fA14><country>France</country><placeName><region type="region" nuts="2">Occitanie (région administrative)</region><region type="old region" nuts="2">Midi-Pyrénées</region></placeName></affiliation></author><author><name sortKey="Harzer, K" sort="Harzer, K" uniqKey="Harzer K" first="K." last="Harzer">K. Harzer</name><affiliation wicri:level="3"><inist:fA14 i1="02"><s1>Neurochemical Laboratory, Institut für Hirnforschung, University of Tübingen</s1><s2>Tübingen</s2><s3>DEU</s3><sZ>2 aut.</sZ></inist:fA14><country>Allemagne</country><placeName><region type="land" nuts="1">Bade-Wurtemberg</region><region type="district" nuts="2">District de Tübingen</region><settlement type="city">Tübingen</settlement></placeName></affiliation></author><author><name sortKey="Christomanou, H" sort="Christomanou, H" uniqKey="Christomanou H" first="H." last="Christomanou">H. Christomanou</name><affiliation wicri:level="3"><inist:fA14 i1="03"><s1>Laboratory of Neurochemistry and Molecular Biology</s1><s2>Athens</s2><s3>GRC</s3><sZ>3 aut.</sZ></inist:fA14><country>Grèce</country><placeName><settlement type="city">Athènes</settlement><region nuts="2" type="region">Attique (région)</region></placeName></affiliation></author><author><name sortKey="Feunteun, J" sort="Feunteun, J" uniqKey="Feunteun J" first="J." last="Feunteun">J. Feunteun</name><affiliation wicri:level="1"><inist:fA14 i1="04"><s1>Laboratoire de Génétique Oncologique, U.R.A. 1967 CNRS, Institut Gustave Roussy</s1><s2>Villejuif</s2><s3>FRA</s3><sZ>4 aut.</sZ></inist:fA14><country>France</country><wicri:noRegion>Villejuif</wicri:noRegion><wicri:noRegion>Institut Gustave Roussy</wicri:noRegion><wicri:noRegion>Villejuif</wicri:noRegion></affiliation></author><author><name sortKey="Pieraggi, M T" sort="Pieraggi, M T" uniqKey="Pieraggi M" first="M. T." last="Pieraggi">M. T. Pieraggi</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Laboratoire de Biochimie, Maladies Métaboliques , INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil</s1><s2>F-31403Toulouse</s2><s3>FRA</s3><sZ>1 aut.</sZ><sZ>5 aut.</sZ><sZ>9 aut.</sZ><sZ>10 aut.</sZ><sZ>11 aut.</sZ><sZ>12 aut.</sZ></inist:fA14><country>France</country><wicri:noRegion>31403Toulouse</wicri:noRegion><wicri:noRegion>C.H.U. Rangueil</wicri:noRegion><wicri:noRegion>F-31403Toulouse</wicri:noRegion></affiliation></author><author><name sortKey="Paton, B C" sort="Paton, B C" uniqKey="Paton B" first="B. C." last="Paton">B. C. Paton</name><affiliation wicri:level="1"><inist:fA14 i1="05"><s1>Department of Chemical Pathology, Women's and Children's Hospital</s1><s2>North Adelaide</s2><s3>AUS</s3><sZ>6 aut.</sZ></inist:fA14><country>Australie</country><wicri:noRegion>North Adelaide</wicri:noRegion></affiliation></author><author><name sortKey="Kishimoto, Y" sort="Kishimoto, Y" uniqKey="Kishimoto Y" first="Y." last="Kishimoto">Y. Kishimoto</name><affiliation wicri:level="1"><inist:fA14 i1="06"><s1>Department of Neurosciences, University of California-San Diego, Center for Molecular Genetics</s1><s2>La Jolla, CA</s2><s3>USA</s3><sZ>7 aut.</sZ><sZ>8 aut.</sZ></inist:fA14><country>États-Unis</country><wicri:noRegion>La Jolla, CA</wicri:noRegion></affiliation></author><author><name sortKey="Obrien, J S" sort="Obrien, J S" uniqKey="Obrien J" first="J. S." last="Obrien">J. S. Obrien</name><affiliation wicri:level="1"><inist:fA14 i1="06"><s1>Department of Neurosciences, University of California-San Diego, Center for Molecular Genetics</s1><s2>La Jolla, CA</s2><s3>USA</s3><sZ>7 aut.</sZ><sZ>8 aut.</sZ></inist:fA14><country>États-Unis</country><wicri:noRegion>La Jolla, CA</wicri:noRegion></affiliation></author><author><name sortKey="Basile, J P" sort="Basile, J P" uniqKey="Basile J" first="J. P." last="Basile">J. P. Basile</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Laboratoire de Biochimie, Maladies Métaboliques , INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil</s1><s2>F-31403Toulouse</s2><s3>FRA</s3><sZ>1 aut.</sZ><sZ>5 aut.</sZ><sZ>9 aut.</sZ><sZ>10 aut.</sZ><sZ>11 aut.</sZ><sZ>12 aut.</sZ></inist:fA14><country>France</country><wicri:noRegion>31403Toulouse</wicri:noRegion><wicri:noRegion>C.H.U. Rangueil</wicri:noRegion><wicri:noRegion>F-31403Toulouse</wicri:noRegion></affiliation></author><author><name sortKey="Thiers, J C" sort="Thiers, J C" uniqKey="Thiers J" first="J. C." last="Thiers">J. C. Thiers</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Laboratoire de Biochimie, Maladies Métaboliques , INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil</s1><s2>F-31403Toulouse</s2><s3>FRA</s3><sZ>1 aut.</sZ><sZ>5 aut.</sZ><sZ>9 aut.</sZ><sZ>10 aut.</sZ><sZ>11 aut.</sZ><sZ>12 aut.</sZ></inist:fA14><country>France</country><wicri:noRegion>31403Toulouse</wicri:noRegion><wicri:noRegion>C.H.U. Rangueil</wicri:noRegion><wicri:noRegion>F-31403Toulouse</wicri:noRegion></affiliation></author><author><name sortKey="Salvayre, R" sort="Salvayre, R" uniqKey="Salvayre R" first="R." last="Salvayre">R. Salvayre</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Laboratoire de Biochimie, Maladies Métaboliques , INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil</s1><s2>F-31403Toulouse</s2><s3>FRA</s3><sZ>1 aut.</sZ><sZ>5 aut.</sZ><sZ>9 aut.</sZ><sZ>10 aut.</sZ><sZ>11 aut.</sZ><sZ>12 aut.</sZ></inist:fA14><country>France</country><wicri:noRegion>31403Toulouse</wicri:noRegion><wicri:noRegion>C.H.U. Rangueil</wicri:noRegion><wicri:noRegion>F-31403Toulouse</wicri:noRegion></affiliation></author><author><name sortKey="Levade, T" sort="Levade, T" uniqKey="Levade T" first="T." last="Levade">T. Levade</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Laboratoire de Biochimie, Maladies Métaboliques , INSERM U. 466, Institut Louis Bugnard, C.H.U. Rangueil</s1><s2>F-31403Toulouse</s2><s3>FRA</s3><sZ>1 aut.</sZ><sZ>5 aut.</sZ><sZ>9 aut.</sZ><sZ>10 aut.</sZ><sZ>11 aut.</sZ><sZ>12 aut.</sZ></inist:fA14><country>France</country><wicri:noRegion>31403Toulouse</wicri:noRegion><wicri:noRegion>C.H.U. Rangueil</wicri:noRegion><wicri:noRegion>F-31403Toulouse</wicri:noRegion></affiliation></author></analytic><series><title level="j" type="main">Clinica chimica acta</title><title level="j" type="abbreviated">Clin. chim. acta</title><idno type="ISSN">0009-8981</idno><imprint><date when="1997">1997</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Clinica chimica acta</title><title level="j" type="abbreviated">Clin. chim. acta</title><idno type="ISSN">0009-8981</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biological model</term><term>Cell immortalization</term><term>Established cell line</term><term>Farber disease</term><term>Fibroblast</term><term>Human</term><term>Lipids</term><term>Lysosomal storage disease</term><term>SV40 virus</term><term>Saposin</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Homme</term><term>Fibroblaste</term><term>Lignée cellulaire établie</term><term>Immortalisation cellulaire</term><term>Virus SV40</term><term>Modèle biologique</term><term>Lysosome pathologie</term><term>Sphingolipidose héréditaire Farber</term><term>Lipide</term><term>Saposine</term></keywords><keywords scheme="Wicri" type="topic" xml:lang="fr"><term>Homme</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Copyright (c) 1997 Elsevier Science B.V. All rights reserved. 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>District de Tübingen</li><li>Midi-Pyrénées</li><li>Occitanie (région administrative)</li></region><settlement><li>Athènes</li><li>Tübingen</li></settlement></list><tree><country name="France"><region name="Occitanie (région administrative)"><name sortKey="Chatelut, M" sort="Chatelut, M" uniqKey="Chatelut M" first="M." last="Chatelut">M. Chatelut</name></region><name sortKey="Basile, J P" sort="Basile, J P" uniqKey="Basile J" first="J. P." last="Basile">J. P. Basile</name><name sortKey="Feunteun, J" sort="Feunteun, J" uniqKey="Feunteun J" first="J." last="Feunteun">J. Feunteun</name><name sortKey="Levade, T" sort="Levade, T" uniqKey="Levade T" first="T." last="Levade">T. Levade</name><name sortKey="Pieraggi, M T" sort="Pieraggi, M T" uniqKey="Pieraggi M" first="M. T." last="Pieraggi">M. T. Pieraggi</name><name sortKey="Salvayre, R" sort="Salvayre, R" uniqKey="Salvayre R" first="R." last="Salvayre">R. Salvayre</name><name sortKey="Thiers, J C" sort="Thiers, J C" uniqKey="Thiers J" first="J. C." last="Thiers">J. C. Thiers</name></country><country name="Allemagne"><region name="Bade-Wurtemberg"><name sortKey="Harzer, K" sort="Harzer, K" uniqKey="Harzer K" first="K." last="Harzer">K. Harzer</name></region></country><country name="Grèce"><region name="Attique (région)"><name sortKey="Christomanou, H" sort="Christomanou, H" uniqKey="Christomanou H" first="H." last="Christomanou">H. Christomanou</name></region></country><country name="Australie"><noRegion><name sortKey="Paton, B C" sort="Paton, B C" uniqKey="Paton B" first="B. C." last="Paton">B. C. Paton</name></noRegion></country><country name="États-Unis"><noRegion><name sortKey="Kishimoto, Y" sort="Kishimoto, Y" uniqKey="Kishimoto Y" first="Y." last="Kishimoto">Y. Kishimoto</name></noRegion><name sortKey="Obrien, J S" sort="Obrien, J S" uniqKey="Obrien J" first="J. S." last="Obrien">J. S. Obrien</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|étape= Merge
|type= RBID
|clé= Pascal:97-0493913
|texte= Model SV40-transformed fibroblast lines for metabolic studies of human prosaposin and acid ceramidase deficiencies
}}
| This area was generated with Dilib version V0.6.33. |  |