Oleate and linoleate stimulate degradation of β-casein in prolactin-treated HC11 mouse mammary epithelial cells
Identifieur interne : 000C14 ( Istex/Corpus ); précédent : 000C13; suivant : 000C15Oleate and linoleate stimulate degradation of β-casein in prolactin-treated HC11 mouse mammary epithelial cells
Auteurs : Alain Pauloin ; Sophie Chat ; Christine Péchoux ; Catherine Hue-Beauvais ; Stéphanie Droineau ; Laurent Galio ; Eve Devinoy ; Eric ChanatSource :
- Cell and Tissue Research [ 0302-766X ] ; 2010-04-01.
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Abstract
Abstract: Although virtually all cells store neutral lipids as cytoplasmic lipid droplets, mammary epithelial cells have developed a specialized function to secrete them as milk fat globules. We have used the mammary epithelial cell line HC11 to evaluate the potential connections between the lipid and protein synthetic pathways. We show that unsaturated fatty acids induce a pronounced proliferation of cytoplasmic lipid droplets and stimulate the synthesis of adipose differentiation-related protein. Unexpectedly, the cellular level of β-casein, accumulated under lactogenic hormone treatment, decreases following treatment of the cells with unsaturated fatty acids. In contrast, saturated fatty acids have no significant effect on either cytoplasmic lipid droplet proliferation or cellular β-casein levels. We demonstrate that the action of unsaturated fatty acids on the level of β-casein is post-translational and requires protein synthesis. We have also observed that proteasome inhibitors potentiate β-casein degradation, indicating that proteasomal activity can destroy some cytosolic protein(s) involved in the process that negatively controls β-casein levels. Finally, lysosome inhibitors block the effect of unsaturated fatty acids on the cellular level of β-casein. Our data thus suggest that the degradation of β-casein occurs via the microautophagic pathway.
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DOI: 10.1007/s00441-009-0926-3
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We have used the mammary epithelial cell line HC11 to evaluate the potential connections between the lipid and protein synthetic pathways. We show that unsaturated fatty acids induce a pronounced proliferation of cytoplasmic lipid droplets and stimulate the synthesis of adipose differentiation-related protein. Unexpectedly, the cellular level of β-casein, accumulated under lactogenic hormone treatment, decreases following treatment of the cells with unsaturated fatty acids. In contrast, saturated fatty acids have no significant effect on either cytoplasmic lipid droplet proliferation or cellular β-casein levels. We demonstrate that the action of unsaturated fatty acids on the level of β-casein is post-translational and requires protein synthesis. We have also observed that proteasome inhibitors potentiate β-casein degradation, indicating that proteasomal activity can destroy some cytosolic protein(s) involved in the process that negatively controls β-casein levels. Finally, lysosome inhibitors block the effect of unsaturated fatty acids on the cellular level of β-casein. Our data thus suggest that the degradation of β-casein occurs via the microautophagic pathway.</div></front></TEI><istex><corpusName>springer-journals</corpusName><author><json:item><name>Alain Pauloin</name><affiliations><json:string>INRA, UR1196 Génomique et Physiologie de la Lactation Domaine de Vilvert, 78352, Jouy-en-Josas, France</json:string><json:string>E-mail: alain.pauloin@jouy.inra.fr</json:string></affiliations></json:item><json:item><name>Sophie Chat</name><affiliations><json:string>INRA, UR1196 Génomique et Physiologie de la Lactation Domaine de Vilvert, 78352, Jouy-en-Josas, France</json:string></affiliations></json:item><json:item><name>Christine Péchoux</name><affiliations><json:string>INRA, UR1196 Génomique et Physiologie de la Lactation Domaine de Vilvert, 78352, Jouy-en-Josas, France</json:string></affiliations></json:item><json:item><name>Catherine Hue-Beauvais</name><affiliations><json:string>INRA, UR1196 Génomique et Physiologie de la Lactation Domaine de Vilvert, 78352, Jouy-en-Josas, France</json:string></affiliations></json:item><json:item><name>Stéphanie Droineau</name><affiliations><json:string>INRA, UR1196 Génomique et Physiologie de la Lactation Domaine de Vilvert, 78352, Jouy-en-Josas, France</json:string></affiliations></json:item><json:item><name>Laurent Galio</name><affiliations><json:string>INRA, UR1196 Génomique et Physiologie de la Lactation Domaine de Vilvert, 78352, Jouy-en-Josas, France</json:string></affiliations></json:item><json:item><name>Eve Devinoy</name><affiliations><json:string>INRA, UR1196 Génomique et Physiologie de la Lactation Domaine de Vilvert, 78352, Jouy-en-Josas, France</json:string></affiliations></json:item><json:item><name>Eric Chanat</name><affiliations><json:string>INRA, UR1196 Génomique et Physiologie de la Lactation Domaine de Vilvert, 78352, Jouy-en-Josas, France</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Mammary epithelial cell</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Casein</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Lipid droplet</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Endoplasmic reticulum</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Cell culture (Mouse, Line HC 11)</value></json:item></subject><articleId><json:string>926</json:string><json:string>s00441-009-0926-3</json:string></articleId><arkIstex>ark:/67375/VQC-4C1J0JGJ-M</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>OriginalPaper</json:string></originalGenre><abstract>Abstract: Although virtually all cells store neutral lipids as cytoplasmic lipid droplets, mammary epithelial cells have developed a specialized function to secrete them as milk fat globules. We have used the mammary epithelial cell line HC11 to evaluate the potential connections between the lipid and protein synthetic pathways. We show that unsaturated fatty acids induce a pronounced proliferation of cytoplasmic lipid droplets and stimulate the synthesis of adipose differentiation-related protein. Unexpectedly, the cellular level of β-casein, accumulated under lactogenic hormone treatment, decreases following treatment of the cells with unsaturated fatty acids. In contrast, saturated fatty acids have no significant effect on either cytoplasmic lipid droplet proliferation or cellular β-casein levels. We demonstrate that the action of unsaturated fatty acids on the level of β-casein is post-translational and requires protein synthesis. We have also observed that proteasome inhibitors potentiate β-casein degradation, indicating that proteasomal activity can destroy some cytosolic protein(s) involved in the process that negatively controls β-casein levels. Finally, lysosome inhibitors block the effect of unsaturated fatty acids on the cellular level of β-casein. 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We have used the mammary epithelial cell line HC11 to evaluate the potential connections between the lipid and protein synthetic pathways. We show that unsaturated fatty acids induce a pronounced proliferation of cytoplasmic lipid droplets and stimulate the synthesis of adipose differentiation-related protein. Unexpectedly, the cellular level of β-casein, accumulated under lactogenic hormone treatment, decreases following treatment of the cells with unsaturated fatty acids. In contrast, saturated fatty acids have no significant effect on either cytoplasmic lipid droplet proliferation or cellular β-casein levels. We demonstrate that the action of unsaturated fatty acids on the level of β-casein is post-translational and requires protein synthesis. We have also observed that proteasome inhibitors potentiate β-casein degradation, indicating that proteasomal activity can destroy some cytosolic protein(s) involved in the process that negatively controls β-casein levels. 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Article</ArticleCategory><ArticleFirstPage>91</ArticleFirstPage><ArticleLastPage>102</ArticleLastPage><ArticleHistory><RegistrationDate><Year>2009</Year><Month>12</Month><Day>19</Day></RegistrationDate><Received><Year>2009</Year><Month>9</Month><Day>25</Day></Received><Accepted><Year>2009</Year><Month>12</Month><Day>18</Day></Accepted><OnlineDate><Year>2010</Year><Month>2</Month><Day>25</Day></OnlineDate></ArticleHistory><ArticleCopyright><CopyrightHolderName>Springer-Verlag</CopyrightHolderName><CopyrightYear>2010</CopyrightYear></ArticleCopyright><ArticleGrants Type="Regular"><MetadataGrant Grant="OpenAccess"></MetadataGrant><AbstractGrant Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="Restricted"></BodyPDFGrant><BodyHTMLGrant Grant="Restricted"></BodyHTMLGrant><BibliographyGrant Grant="Restricted"></BibliographyGrant><ESMGrant Grant="Restricted"></ESMGrant></ArticleGrants></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1" CorrespondingAffiliationID="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Alain</GivenName><FamilyName>Pauloin</FamilyName></AuthorName><Contact><Phone>+33-1-34652548</Phone><Fax>+33-1-34652241</Fax><Email>alain.pauloin@jouy.inra.fr</Email></Contact></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Sophie</GivenName><FamilyName>Chat</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Christine</GivenName><FamilyName>Péchoux</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Catherine</GivenName><FamilyName>Hue-Beauvais</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Stéphanie</GivenName><FamilyName>Droineau</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Laurent</GivenName><FamilyName>Galio</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Eve</GivenName><FamilyName>Devinoy</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Eric</GivenName><FamilyName>Chanat</FamilyName></AuthorName></Author><Affiliation ID="Aff1"><OrgName>INRA, UR1196 Génomique et Physiologie de la Lactation Domaine de Vilvert</OrgName><OrgAddress><Postcode>78352</Postcode><City>Jouy-en-Josas</City><Country Code="FR">France</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En" OutputMedium="All"><Heading>Abstract</Heading><Para>Although virtually all cells store neutral lipids as cytoplasmic lipid droplets, mammary epithelial cells have developed a specialized function to secrete them as milk fat globules. We have used the mammary epithelial cell line HC11 to evaluate the potential connections between the lipid and protein synthetic pathways. We show that unsaturated fatty acids induce a pronounced proliferation of cytoplasmic lipid droplets and stimulate the synthesis of adipose differentiation-related protein. Unexpectedly, the cellular level of β-casein, accumulated under lactogenic hormone treatment, decreases following treatment of the cells with unsaturated fatty acids. In contrast, saturated fatty acids have no significant effect on either cytoplasmic lipid droplet proliferation or cellular β-casein levels. We demonstrate that the action of unsaturated fatty acids on the level of β-casein is post-translational and requires protein synthesis. We have also observed that proteasome inhibitors potentiate β-casein degradation, indicating that proteasomal activity can destroy some cytosolic protein(s) involved in the process that negatively controls β-casein levels. Finally, lysosome inhibitors block the effect of unsaturated fatty acids on the cellular level of β-casein. Our data thus suggest that the degradation of β-casein occurs via the microautophagic pathway.</Para></Abstract><KeywordGroup Language="En" OutputMedium="All"><Heading>Keywords</Heading><Keyword>Mammary epithelial cell</Keyword><Keyword>Casein</Keyword><Keyword>Lipid droplet</Keyword><Keyword>Endoplasmic reticulum</Keyword><Keyword>Cell culture (Mouse, Line HC 11)</Keyword></KeywordGroup><ArticleNote Type="Misc"><SimplePara> A.P. is supported by the Centre National de la Recherche Scientifique.</SimplePara></ArticleNote></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Oleate and linoleate stimulate degradation of β-casein in prolactin-treated HC11 mouse mammary epithelial cells</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Oleate and linoleate stimulate degradation of β-casein in prolactin-treated HC11 mouse mammary epithelial cells</title></titleInfo><name type="personal" displayLabel="corresp"><namePart type="given">Alain</namePart><namePart type="family">Pauloin</namePart><affiliation>INRA, UR1196 Génomique et Physiologie de la Lactation Domaine de Vilvert, 78352, Jouy-en-Josas, France</affiliation><affiliation>E-mail: alain.pauloin@jouy.inra.fr</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Sophie</namePart><namePart type="family">Chat</namePart><affiliation>INRA, UR1196 Génomique et Physiologie de la Lactation Domaine de Vilvert, 78352, Jouy-en-Josas, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Christine</namePart><namePart type="family">Péchoux</namePart><affiliation>INRA, UR1196 Génomique et Physiologie de la Lactation Domaine de Vilvert, 78352, Jouy-en-Josas, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Catherine</namePart><namePart type="family">Hue-Beauvais</namePart><affiliation>INRA, UR1196 Génomique et Physiologie de la Lactation Domaine de Vilvert, 78352, Jouy-en-Josas, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Stéphanie</namePart><namePart type="family">Droineau</namePart><affiliation>INRA, UR1196 Génomique et Physiologie de la Lactation Domaine de Vilvert, 78352, Jouy-en-Josas, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Laurent</namePart><namePart type="family">Galio</namePart><affiliation>INRA, UR1196 Génomique et Physiologie de la Lactation Domaine de Vilvert, 78352, Jouy-en-Josas, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Eve</namePart><namePart type="family">Devinoy</namePart><affiliation>INRA, UR1196 Génomique et Physiologie de la Lactation Domaine de Vilvert, 78352, Jouy-en-Josas, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Eric</namePart><namePart type="family">Chanat</namePart><affiliation>INRA, UR1196 Génomique et Physiologie de la Lactation Domaine de Vilvert, 78352, Jouy-en-Josas, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="OriginalPaper" 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>Springer-Verlag</publisher><place><placeTerm type="text">Berlin/Heidelberg</placeTerm></place><dateCreated encoding="w3cdtf">2009-09-25</dateCreated><dateIssued encoding="w3cdtf">2010-04-01</dateIssued><copyrightDate encoding="w3cdtf">2010</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Abstract: Although virtually all cells store neutral lipids as cytoplasmic lipid droplets, mammary epithelial cells have developed a specialized function to secrete them as milk fat globules. We have used the mammary epithelial cell line HC11 to evaluate the potential connections between the lipid and protein synthetic pathways. We show that unsaturated fatty acids induce a pronounced proliferation of cytoplasmic lipid droplets and stimulate the synthesis of adipose differentiation-related protein. Unexpectedly, the cellular level of β-casein, accumulated under lactogenic hormone treatment, decreases following treatment of the cells with unsaturated fatty acids. In contrast, saturated fatty acids have no significant effect on either cytoplasmic lipid droplet proliferation or cellular β-casein levels. We demonstrate that the action of unsaturated fatty acids on the level of β-casein is post-translational and requires protein synthesis. We have also observed that proteasome inhibitors potentiate β-casein degradation, indicating that proteasomal activity can destroy some cytosolic protein(s) involved in the process that negatively controls β-casein levels. Finally, lysosome inhibitors block the effect of unsaturated fatty acids on the cellular level of β-casein. Our data thus suggest that the degradation of β-casein occurs via the microautophagic pathway.</abstract><note>Regular Article</note><subject lang="en"><genre>Keywords</genre><topic>Mammary epithelial cell</topic><topic>Casein</topic><topic>Lipid droplet</topic><topic>Endoplasmic reticulum</topic><topic>Cell culture (Mouse, Line HC 11)</topic></subject><relatedItem type="host"><titleInfo><title>Cell and Tissue Research</title></titleInfo><titleInfo type="abbreviated"><title>Cell Tissue Res</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>Springer</publisher><dateIssued encoding="w3cdtf">2010-03-31</dateIssued><copyrightDate encoding="w3cdtf">2010</copyrightDate></originInfo><subject><genre>Biomedicine</genre><topic>Molecular Medicine</topic><topic>Proteomics</topic><topic>Human Genetics</topic></subject><identifier type="ISSN">0302-766X</identifier><identifier type="eISSN">1432-0878</identifier><identifier type="JournalID">441</identifier><identifier type="IssueArticleCount">19</identifier><identifier type="VolumeIssueCount">3</identifier><part><date>2010</date><detail type="volume"><number>340</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="pages"><start>91</start><end>102</end></extent></part><recordInfo><recordOrigin>Springer-Verlag, 2010</recordOrigin></recordInfo></relatedItem><identifier type="istex">63380DAC193B520812E08EE0A3D96239C46214FB</identifier><identifier type="ark">ark:/67375/VQC-4C1J0JGJ-M</identifier><identifier type="DOI">10.1007/s00441-009-0926-3</identifier><identifier type="ArticleID">926</identifier><identifier type="ArticleID">s00441-009-0926-3</identifier><accessCondition type="use and reproduction" contentType="copyright">Springer-Verlag, 2010</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</recordContentSource><recordOrigin>Springer-Verlag, 2010</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-4C1J0JGJ-M/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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