GSM-900MHz at low dose temperature-dependently downregulates α-synuclein in cultured cerebral cells independently of chaperone-mediated-autophagy.
Identifieur interne : 000805 ( PubMed/Checkpoint ); précédent : 000804; suivant : 000806GSM-900MHz at low dose temperature-dependently downregulates α-synuclein in cultured cerebral cells independently of chaperone-mediated-autophagy.
Auteurs : Faraj Terro [France] ; Amandine Magnaudeix ; Marion Crochetet ; Ludovic Martin ; Sylvie Bourthoumieu ; Cornelia-M Wilson ; Catherine Yardin ; Philippe LevequeSource :
- Toxicology [ 1879-3185 ] ; 2012.
English descriptors
- KwdEn :
- Autophagy (drug effects), Blotting, Western, Cell Line, Cerebral Cortex (cytology), Cerebral Cortex (drug effects), Cerebral Cortex (metabolism), Down-Regulation (drug effects), Electromagnetic Fields (adverse effects), Fluorescent Antibody Technique, Direct, HSC70 Heat-Shock Proteins (metabolism), HSP90 Heat-Shock Proteins (metabolism), Humans, Lysosomal-Associated Membrane Protein 2, Lysosome-Associated Membrane Glycoproteins (metabolism), Molecular Chaperones (physiology), alpha-Synuclein (biosynthesis), alpha-Synuclein (genetics).
- MESH :
- chemical , biosynthesis : alpha-Synuclein.
- chemical , genetics : alpha-Synuclein.
- chemical , metabolism : HSC70 Heat-Shock Proteins, HSP90 Heat-Shock Proteins, Lysosome-Associated Membrane Glycoproteins.
- adverse effects : Electromagnetic Fields.
- cytology : Cerebral Cortex.
- drug effects : Autophagy, Cerebral Cortex, Down-Regulation.
- metabolism : Cerebral Cortex.
- chemical , physiology : Molecular Chaperones.
- Blotting, Western, Cell Line, Fluorescent Antibody Technique, Direct, Humans, Lysosomal-Associated Membrane Protein 2.
Abstract
The expanding use of GSM devices has resulted in public concern. Chaperone-mediated autophagy (CMA) is a way for protein degradation in the lysosomes and increases under stress conditions as a cell defense response. α-synuclein, a CMA substrate, is a component of Parkinson disease. Since GSM might constitute a stress signal, we raised the possibility that GSM could alter the CMA process. Here, we analyzed the effects of chronic exposure to a low GSM-900MHz dose on apoptosis and CMA. Cultured cerebral cortical cells were sham-exposed or exposed to GSM-900MHz at specific absorption rate (SAR): 0.25W/kg for 24 h using a wire-patch cell. Apoptosis was analyzed by DAPI stain of the nuclei and western blot of cleaved caspase-3. The expression of proteins involved in CMA (HSC70, HSP40, HSP90 and LAMP-2A) and α-synuclein were analyzed by western blot. CMA was also quantified in situ by analyzing the cell localization of active lysosomes. 24 h exposure to GSM-900MHz resulted in ∼0.5°C temperature rise. It did not induce apoptosis but increased HSC70 by 26% and slightly decreased HSP90 (<10%). It also decreased α-synuclein by 24% independently of CMA, since the localization of active lysosomes was not altered. Comparable effects were observed in cells incubated at 37.5°C, a condition that mimics the GSM-generated temperature rise. The GSM-induced changes in HSC70, HSP90 and α-synuclein are most likely linked to temperature rise. We did not observe any immediate effect on cell viability. However, the delayed and long term consequences (protective or deleterious) of these changes on cell fate should be examined.
DOI: 10.1016/j.tox.2011.12.003
PubMed: 22185909
Affiliations:
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EA3842 Homéostasie cellulaire et pathologies, Faculté de Médecine, 2 rue du Dr Raymond Marcland, 87025 Limoges Cedex, France. faraj.terro@unilim.fr</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Groupe de Neurobiologie Cellulaire - EA3842 Homéostasie cellulaire et pathologies, Faculté de Médecine, 2 rue du Dr Raymond Marcland, 87025 Limoges Cedex</wicri:regionArea><placeName><region type="region" nuts="2">Nouvelle-Aquitaine</region><region type="old region" nuts="2">Limousin</region><settlement type="city">Limoges</settlement></placeName></affiliation></author><author><name sortKey="Magnaudeix, Amandine" sort="Magnaudeix, Amandine" uniqKey="Magnaudeix A" first="Amandine" last="Magnaudeix">Amandine Magnaudeix</name></author><author><name sortKey="Crochetet, Marion" sort="Crochetet, Marion" uniqKey="Crochetet M" first="Marion" last="Crochetet">Marion Crochetet</name></author><author><name sortKey="Martin, Ludovic" sort="Martin, Ludovic" uniqKey="Martin L" first="Ludovic" last="Martin">Ludovic Martin</name></author><author><name sortKey="Bourthoumieu, Sylvie" sort="Bourthoumieu, Sylvie" uniqKey="Bourthoumieu S" first="Sylvie" last="Bourthoumieu">Sylvie Bourthoumieu</name></author><author><name sortKey="Wilson, Cornelia M" sort="Wilson, Cornelia M" uniqKey="Wilson C" first="Cornelia-M" last="Wilson">Cornelia-M Wilson</name></author><author><name sortKey="Yardin, Catherine" sort="Yardin, Catherine" uniqKey="Yardin C" first="Catherine" last="Yardin">Catherine Yardin</name></author><author><name sortKey="Leveque, Philippe" sort="Leveque, Philippe" uniqKey="Leveque P" first="Philippe" last="Leveque">Philippe Leveque</name></author></analytic><series><title level="j">Toxicology</title><idno type="eISSN">1879-3185</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Autophagy (drug effects)</term><term>Blotting, Western</term><term>Cell Line</term><term>Cerebral Cortex (cytology)</term><term>Cerebral Cortex (drug effects)</term><term>Cerebral Cortex (metabolism)</term><term>Down-Regulation (drug effects)</term><term>Electromagnetic Fields (adverse effects)</term><term>Fluorescent Antibody Technique, Direct</term><term>HSC70 Heat-Shock Proteins (metabolism)</term><term>HSP90 Heat-Shock Proteins (metabolism)</term><term>Humans</term><term>Lysosomal-Associated Membrane Protein 2</term><term>Lysosome-Associated Membrane Glycoproteins (metabolism)</term><term>Molecular Chaperones (physiology)</term><term>alpha-Synuclein (biosynthesis)</term><term>alpha-Synuclein (genetics)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>HSC70 Heat-Shock Proteins</term><term>HSP90 Heat-Shock Proteins</term><term>Lysosome-Associated Membrane Glycoproteins</term></keywords><keywords scheme="MESH" qualifier="adverse effects" xml:lang="en"><term>Electromagnetic Fields</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Cerebral Cortex</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Autophagy</term><term>Cerebral Cortex</term><term>Down-Regulation</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cerebral Cortex</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Molecular Chaperones</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Blotting, Western</term><term>Cell Line</term><term>Fluorescent Antibody Technique, Direct</term><term>Humans</term><term>Lysosomal-Associated Membrane Protein 2</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The expanding use of GSM devices has resulted in public concern. Chaperone-mediated autophagy (CMA) is a way for protein degradation in the lysosomes and increases under stress conditions as a cell defense response. α-synuclein, a CMA substrate, is a component of Parkinson disease. Since GSM might constitute a stress signal, we raised the possibility that GSM could alter the CMA process. Here, we analyzed the effects of chronic exposure to a low GSM-900MHz dose on apoptosis and CMA. Cultured cerebral cortical cells were sham-exposed or exposed to GSM-900MHz at specific absorption rate (SAR): 0.25W/kg for 24 h using a wire-patch cell. Apoptosis was analyzed by DAPI stain of the nuclei and western blot of cleaved caspase-3. The expression of proteins involved in CMA (HSC70, HSP40, HSP90 and LAMP-2A) and α-synuclein were analyzed by western blot. CMA was also quantified in situ by analyzing the cell localization of active lysosomes. 24 h exposure to GSM-900MHz resulted in ∼0.5°C temperature rise. It did not induce apoptosis but increased HSC70 by 26% and slightly decreased HSP90 (<10%). It also decreased α-synuclein by 24% independently of CMA, since the localization of active lysosomes was not altered. Comparable effects were observed in cells incubated at 37.5°C, a condition that mimics the GSM-generated temperature rise. The GSM-induced changes in HSC70, HSP90 and α-synuclein are most likely linked to temperature rise. We did not observe any immediate effect on cell viability. However, the delayed and long term consequences (protective or deleterious) of these changes on cell fate should be examined.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22185909</PMID><DateCreated><Year>2012</Year><Month>01</Month><Day>23</Day></DateCreated><DateCompleted><Year>2012</Year><Month>03</Month><Day>21</Day></DateCompleted><DateRevised><Year>2014</Year><Month>11</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-3185</ISSN><JournalIssue CitedMedium="Internet"><Volume>292</Volume><Issue>2-3</Issue><PubDate><Year>2012</Year><Month>Feb</Month><Day>26</Day></PubDate></JournalIssue><Title>Toxicology</Title><ISOAbbreviation>Toxicology</ISOAbbreviation></Journal><ArticleTitle>GSM-900MHz at low dose temperature-dependently downregulates α-synuclein in cultured cerebral cells independently of chaperone-mediated-autophagy.</ArticleTitle><Pagination><MedlinePgn>136-44</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.tox.2011.12.003</ELocationID><Abstract><AbstractText>The expanding use of GSM devices has resulted in public concern. Chaperone-mediated autophagy (CMA) is a way for protein degradation in the lysosomes and increases under stress conditions as a cell defense response. α-synuclein, a CMA substrate, is a component of Parkinson disease. Since GSM might constitute a stress signal, we raised the possibility that GSM could alter the CMA process. Here, we analyzed the effects of chronic exposure to a low GSM-900MHz dose on apoptosis and CMA. Cultured cerebral cortical cells were sham-exposed or exposed to GSM-900MHz at specific absorption rate (SAR): 0.25W/kg for 24 h using a wire-patch cell. Apoptosis was analyzed by DAPI stain of the nuclei and western blot of cleaved caspase-3. The expression of proteins involved in CMA (HSC70, HSP40, HSP90 and LAMP-2A) and α-synuclein were analyzed by western blot. CMA was also quantified in situ by analyzing the cell localization of active lysosomes. 24 h exposure to GSM-900MHz resulted in ∼0.5°C temperature rise. It did not induce apoptosis but increased HSC70 by 26% and slightly decreased HSP90 (<10%). It also decreased α-synuclein by 24% independently of CMA, since the localization of active lysosomes was not altered. Comparable effects were observed in cells incubated at 37.5°C, a condition that mimics the GSM-generated temperature rise. The GSM-induced changes in HSC70, HSP90 and α-synuclein are most likely linked to temperature rise. We did not observe any immediate effect on cell viability. However, the delayed and long term consequences (protective or deleterious) of these changes on cell fate should be examined.</AbstractText><CopyrightInformation>Copyright © 2011 Elsevier Ireland Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Terro</LastName><ForeName>Faraj</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Groupe de Neurobiologie Cellulaire - EA3842 Homéostasie cellulaire et pathologies, Faculté de Médecine, 2 rue du Dr Raymond Marcland, 87025 Limoges Cedex, France. faraj.terro@unilim.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Magnaudeix</LastName><ForeName>Amandine</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Crochetet</LastName><ForeName>Marion</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Martin</LastName><ForeName>Ludovic</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Bourthoumieu</LastName><ForeName>Sylvie</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Wilson</LastName><ForeName>Cornelia-M</ForeName><Initials>CM</Initials></Author><Author ValidYN="Y"><LastName>Yardin</LastName><ForeName>Catherine</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Leveque</LastName><ForeName>Philippe</ForeName><Initials>P</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>12</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>Ireland</Country><MedlineTA>Toxicology</MedlineTA><NlmUniqueID>0361055</NlmUniqueID><ISSNLinking>0300-483X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050883">HSC70 Heat-Shock Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018841">HSP90 Heat-Shock Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C497811">LAMP2 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D052119">Lysosomal-Associated Membrane Protein 2</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051907">Lysosome-Associated Membrane Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018832">Molecular Chaperones</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051844">alpha-Synuclein</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001343" MajorTopicYN="N">Autophagy</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015153" MajorTopicYN="N">Blotting, Western</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002540" MajorTopicYN="N">Cerebral Cortex</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015536" MajorTopicYN="N">Down-Regulation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004574" MajorTopicYN="N">Electromagnetic Fields</DescriptorName><QualifierName UI="Q000009" MajorTopicYN="Y">adverse effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019085" MajorTopicYN="N">Fluorescent Antibody Technique, Direct</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D050883" MajorTopicYN="N">HSC70 Heat-Shock Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018841" MajorTopicYN="N">HSP90 Heat-Shock Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D052119" MajorTopicYN="N">Lysosomal-Associated Membrane Protein 2</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051907" MajorTopicYN="N">Lysosome-Associated Membrane Glycoproteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018832" MajorTopicYN="N">Molecular Chaperones</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051844" MajorTopicYN="N">alpha-Synuclein</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2011</Year><Month>09</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2011</Year><Month>11</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2011</Year><Month>12</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>12</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>12</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2012</Year><Month>3</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">22185909</ArticleId><ArticleId IdType="pii">S0300-483X(11)00508-7</ArticleId><ArticleId IdType="doi">10.1016/j.tox.2011.12.003</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Limousin</li><li>Nouvelle-Aquitaine</li></region><settlement><li>Limoges</li></settlement></list><tree><noCountry><name sortKey="Bourthoumieu, Sylvie" sort="Bourthoumieu, Sylvie" uniqKey="Bourthoumieu S" first="Sylvie" last="Bourthoumieu">Sylvie Bourthoumieu</name><name sortKey="Crochetet, Marion" sort="Crochetet, Marion" uniqKey="Crochetet M" first="Marion" last="Crochetet">Marion Crochetet</name><name sortKey="Leveque, Philippe" sort="Leveque, Philippe" uniqKey="Leveque P" first="Philippe" last="Leveque">Philippe Leveque</name><name sortKey="Magnaudeix, Amandine" sort="Magnaudeix, Amandine" uniqKey="Magnaudeix A" first="Amandine" last="Magnaudeix">Amandine Magnaudeix</name><name sortKey="Martin, Ludovic" sort="Martin, Ludovic" uniqKey="Martin L" first="Ludovic" last="Martin">Ludovic Martin</name><name sortKey="Wilson, Cornelia M" sort="Wilson, Cornelia M" uniqKey="Wilson C" first="Cornelia-M" last="Wilson">Cornelia-M Wilson</name><name sortKey="Yardin, Catherine" sort="Yardin, Catherine" uniqKey="Yardin C" first="Catherine" last="Yardin">Catherine Yardin</name></noCountry><country name="France"><region name="Nouvelle-Aquitaine"><name sortKey="Terro, Faraj" sort="Terro, Faraj" uniqKey="Terro F" first="Faraj" last="Terro">Faraj Terro</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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