Autophagy-dependent and -independent involvement of AMP-activated protein kinase in 6-hydroxydopamine toxicity to SH-SY5Y neuroblastoma cells.
Identifieur interne : 001214 ( Main/Exploration ); précédent : 001213; suivant : 001215Autophagy-dependent and -independent involvement of AMP-activated protein kinase in 6-hydroxydopamine toxicity to SH-SY5Y neuroblastoma cells.
Auteurs : Katarina Arsikin [Serbie] ; Tamara Kravic-Stevovic ; Maja Jovanovic ; Biljana Ristic ; Gordana Tovilovic ; Nevena Zogovic ; Vladimir Bumbasirevic ; Vladimir Trajkovic ; Ljubica Harhaji-TrajkovicSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2012.
Descripteurs français
- KwdFr :
- AMP-Activated Protein Kinases (génétique), AMP-Activated Protein Kinases (métabolisme), Acétylcystéine (pharmacologie), Apoptose (effets des médicaments et des substances chimiques), Autophagie (effets des médicaments et des substances chimiques), Autophagie (génétique), Humains (MeSH), Lignée cellulaire (MeSH), Microscopie électronique à transmission (MeSH), Neuroblastome (métabolisme), Oxidopamine (pharmacologie), Petit ARN interférent (MeSH), Phosphorylation (MeSH), Protéines adaptatrices de la transduction du signal (MeSH), Protéines associées aux microtubules (génétique), Protéines associées aux microtubules (métabolisme), Ribosomal Protein S6 Kinases, 70-kDa (métabolisme), Régulation de l'expression des gènes (effets des médicaments et des substances chimiques), Sirolimus (pharmacologie), Séquestosome-1 (MeSH), Sérine-thréonine kinases TOR (métabolisme), p38 Mitogen-Activated Protein Kinases (métabolisme).
- MESH :
- effets des médicaments et des substances chimiques : Apoptose, Autophagie, Régulation de l'expression des gènes.
- génétique : AMP-Activated Protein Kinases, Autophagie, Protéines associées aux microtubules.
- métabolisme : AMP-Activated Protein Kinases, Neuroblastome, Protéines associées aux microtubules, Ribosomal Protein S6 Kinases, 70-kDa, Sérine-thréonine kinases TOR, p38 Mitogen-Activated Protein Kinases.
- pharmacologie : Acétylcystéine, Oxidopamine, Sirolimus.
- Humains, Lignée cellulaire, Microscopie électronique à transmission, Petit ARN interférent, Phosphorylation, Protéines adaptatrices de la transduction du signal, Séquestosome-1.
English descriptors
- KwdEn :
- AMP-Activated Protein Kinases (genetics), AMP-Activated Protein Kinases (metabolism), Acetylcysteine (pharmacology), Adaptor Proteins, Signal Transducing (MeSH), Apoptosis (drug effects), Autophagy (drug effects), Autophagy (genetics), Cell Line (MeSH), Gene Expression Regulation (drug effects), Humans (MeSH), Microscopy, Electron, Transmission (MeSH), Microtubule-Associated Proteins (genetics), Microtubule-Associated Proteins (metabolism), Neuroblastoma (metabolism), Oxidopamine (pharmacology), Phosphorylation (MeSH), RNA, Small Interfering (MeSH), Ribosomal Protein S6 Kinases, 70-kDa (metabolism), Sequestosome-1 Protein (MeSH), Sirolimus (pharmacology), TOR Serine-Threonine Kinases (metabolism), p38 Mitogen-Activated Protein Kinases (metabolism).
- MESH :
- chemical , genetics : AMP-Activated Protein Kinases, Microtubule-Associated Proteins.
- chemical , metabolism : AMP-Activated Protein Kinases, Microtubule-Associated Proteins, Ribosomal Protein S6 Kinases, 70-kDa, TOR Serine-Threonine Kinases, p38 Mitogen-Activated Protein Kinases.
- chemical , pharmacology : Acetylcysteine, Oxidopamine, Sirolimus.
- chemical : Adaptor Proteins, Signal Transducing, RNA, Small Interfering, Sequestosome-1 Protein.
- drug effects : Apoptosis, Autophagy, Gene Expression Regulation.
- genetics : Autophagy.
- metabolism : Neuroblastoma.
- Cell Line, Humans, Microscopy, Electron, Transmission, Phosphorylation.
Abstract
The role of the main intracellular energy sensor adenosine monophosphate (AMP)-activated protein kinase (AMPK) in the induction of autophagic response and cell death was investigated in SH-SY5Y human neuroblastoma cells exposed to the dopaminergic neurotoxin 6-hydroxydopamine (6-OHDA). The induction of autophagy in SH-SY5Y cells was demonstrated by acridine orange staining of intracellular acidic vesicles, the presence of autophagosome- and autophagolysosome-like vesicles confirmed by transmission electron microscopy, as well as by microtubule-associated protein 1 light-chain 3 (LC3) conversion and p62 degradation detected by immunoblotting. 6-OHDA induced phosphorylation of AMPK and its target Raptor, followed by the dephosphorylation of the major autophagy inhibitor mammalian target of rapamycin (mTOR) and its substrate p70S6 kinase (S6K). 6-OHDA treatment failed to suppress mTOR/S6K phosphorylation and to increase LC3 conversion, p62 degradation and cytoplasmatic acidification in neuroblastoma cells in which AMPK expression was downregulated by RNA interference. Transfection of SH-SY5Y cells with AMPK or LC3β shRNA, as well as treatment with pharmacological autophagy inhibitors suppressed, while mTOR inhibitor rapamycin potentiated 6-OHDA-induced oxidative stress and apoptotic cell death. 6-OHDA induced phosphorylation of p38 mitogen-activated protein (MAP) kinase in an AMPK-dependent manner, and pharmacological inhibition of p38 MAP kinase reduced neurotoxicity, but not AMPK activation and autophagy triggered by 6-OHDA. Finally, the antioxidant N-acetyl cysteine antagonized 6-OHDA-induced activation of AMPK, p38 and autophagy. These data suggest that oxidative stress-mediated AMPK/mTOR-dependent autophagy and AMPK/p38-dependent apoptosis could be valid therapeutic targets for neuroprotection.
DOI: 10.1016/j.bbadis.2012.08.006
PubMed: 22917563
Affiliations:
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xml:lang="en"><term>Neuroblastoma</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>AMP-Activated Protein Kinases</term><term>Neuroblastome</term><term>Protéines associées aux microtubules</term><term>Ribosomal Protein S6 Kinases, 70-kDa</term><term>Sérine-thréonine kinases TOR</term><term>p38 Mitogen-Activated Protein Kinases</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Acétylcystéine</term><term>Oxidopamine</term><term>Sirolimus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Humans</term><term>Microscopy, Electron, Transmission</term><term>Phosphorylation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Lignée cellulaire</term><term>Microscopie électronique à transmission</term><term>Petit ARN interférent</term><term>Phosphorylation</term><term>Protéines adaptatrices de la transduction du signal</term><term>Séquestosome-1</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The role of the main intracellular energy sensor adenosine monophosphate (AMP)-activated protein kinase (AMPK) in the induction of autophagic response and cell death was investigated in SH-SY5Y human neuroblastoma cells exposed to the dopaminergic neurotoxin 6-hydroxydopamine (6-OHDA). The induction of autophagy in SH-SY5Y cells was demonstrated by acridine orange staining of intracellular acidic vesicles, the presence of autophagosome- and autophagolysosome-like vesicles confirmed by transmission electron microscopy, as well as by microtubule-associated protein 1 light-chain 3 (LC3) conversion and p62 degradation detected by immunoblotting. 6-OHDA induced phosphorylation of AMPK and its target Raptor, followed by the dephosphorylation of the major autophagy inhibitor mammalian target of rapamycin (mTOR) and its substrate p70S6 kinase (S6K). 6-OHDA treatment failed to suppress mTOR/S6K phosphorylation and to increase LC3 conversion, p62 degradation and cytoplasmatic acidification in neuroblastoma cells in which AMPK expression was downregulated by RNA interference. Transfection of SH-SY5Y cells with AMPK or LC3β shRNA, as well as treatment with pharmacological autophagy inhibitors suppressed, while mTOR inhibitor rapamycin potentiated 6-OHDA-induced oxidative stress and apoptotic cell death. 6-OHDA induced phosphorylation of p38 mitogen-activated protein (MAP) kinase in an AMPK-dependent manner, and pharmacological inhibition of p38 MAP kinase reduced neurotoxicity, but not AMPK activation and autophagy triggered by 6-OHDA. Finally, the antioxidant N-acetyl cysteine antagonized 6-OHDA-induced activation of AMPK, p38 and autophagy. These data suggest that oxidative stress-mediated AMPK/mTOR-dependent autophagy and AMPK/p38-dependent apoptosis could be valid therapeutic targets for neuroprotection.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22917563</PMID><DateCompleted><Year>2012</Year><Month>11</Month><Day>13</Day></DateCompleted><DateRevised><Year>2017</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1822</Volume><Issue>11</Issue><PubDate><Year>2012</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim Biophys Acta</ISOAbbreviation></Journal><ArticleTitle>Autophagy-dependent and -independent involvement of AMP-activated protein kinase in 6-hydroxydopamine toxicity to SH-SY5Y neuroblastoma cells.</ArticleTitle><Pagination><MedlinePgn>1826-36</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbadis.2012.08.006</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0925-4439(12)00192-5</ELocationID><Abstract><AbstractText>The role of the main intracellular energy sensor adenosine monophosphate (AMP)-activated protein kinase (AMPK) in the induction of autophagic response and cell death was investigated in SH-SY5Y human neuroblastoma cells exposed to the dopaminergic neurotoxin 6-hydroxydopamine (6-OHDA). The induction of autophagy in SH-SY5Y cells was demonstrated by acridine orange staining of intracellular acidic vesicles, the presence of autophagosome- and autophagolysosome-like vesicles confirmed by transmission electron microscopy, as well as by microtubule-associated protein 1 light-chain 3 (LC3) conversion and p62 degradation detected by immunoblotting. 6-OHDA induced phosphorylation of AMPK and its target Raptor, followed by the dephosphorylation of the major autophagy inhibitor mammalian target of rapamycin (mTOR) and its substrate p70S6 kinase (S6K). 6-OHDA treatment failed to suppress mTOR/S6K phosphorylation and to increase LC3 conversion, p62 degradation and cytoplasmatic acidification in neuroblastoma cells in which AMPK expression was downregulated by RNA interference. Transfection of SH-SY5Y cells with AMPK or LC3β shRNA, as well as treatment with pharmacological autophagy inhibitors suppressed, while mTOR inhibitor rapamycin potentiated 6-OHDA-induced oxidative stress and apoptotic cell death. 6-OHDA induced phosphorylation of p38 mitogen-activated protein (MAP) kinase in an AMPK-dependent manner, and pharmacological inhibition of p38 MAP kinase reduced neurotoxicity, but not AMPK activation and autophagy triggered by 6-OHDA. Finally, the antioxidant N-acetyl cysteine antagonized 6-OHDA-induced activation of AMPK, p38 and autophagy. These data suggest that oxidative stress-mediated AMPK/mTOR-dependent autophagy and AMPK/p38-dependent apoptosis could be valid therapeutic targets for neuroprotection.</AbstractText><CopyrightInformation>Copyright © 2012 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Arsikin</LastName><ForeName>Katarina</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Institute of Microbiology and Immunology, School of Medicine, University of Belgrade, Dr. Subotica 1, 11000 Belgrade, Serbia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kravic-Stevovic</LastName><ForeName>Tamara</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Jovanovic</LastName><ForeName>Maja</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Ristic</LastName><ForeName>Biljana</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Tovilovic</LastName><ForeName>Gordana</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Zogovic</LastName><ForeName>Nevena</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Bumbasirevic</LastName><ForeName>Vladimir</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Trajkovic</LastName><ForeName>Vladimir</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Harhaji-Trajkovic</LastName><ForeName>Ljubica</ForeName><Initials>L</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>2012</Year><Month>08</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D048868">Adaptor Proteins, Signal 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UI="D058570">TOR Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D038762">Ribosomal Protein S6 Kinases, 70-kDa</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.24</RegistryNumber><NameOfSubstance UI="D048051">p38 Mitogen-Activated Protein Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.31</RegistryNumber><NameOfSubstance UI="D055372">AMP-Activated Protein Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber><NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance></Chemical><Chemical><RegistryNumber>WYQ7N0BPYC</RegistryNumber><NameOfSubstance UI="D000111">Acetylcysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D055372" MajorTopicYN="N">AMP-Activated Protein Kinases</DescriptorName><QualifierName UI="Q000235" 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MajorTopicYN="N">Gene Expression Regulation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046529" MajorTopicYN="N">Microscopy, Electron, Transmission</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008869" MajorTopicYN="N">Microtubule-Associated Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009447" MajorTopicYN="N">Neuroblastoma</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016627" MajorTopicYN="N">Oxidopamine</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D034741" MajorTopicYN="N">RNA, Small Interfering</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D038762" MajorTopicYN="N">Ribosomal Protein S6 Kinases, 70-kDa</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000071456" MajorTopicYN="N">Sequestosome-1 Protein</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020123" MajorTopicYN="N">Sirolimus</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D058570" MajorTopicYN="N">TOR Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D048051" MajorTopicYN="N">p38 Mitogen-Activated Protein Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>05</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2012</Year><Month>08</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2012</Year><Month>08</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>8</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>8</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2012</Year><Month>11</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">22917563</ArticleId><ArticleId IdType="pii">S0925-4439(12)00192-5</ArticleId><ArticleId IdType="doi">10.1016/j.bbadis.2012.08.006</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Serbie</li></country></list><tree><noCountry><name sortKey="Bumbasirevic, Vladimir" sort="Bumbasirevic, Vladimir" uniqKey="Bumbasirevic V" first="Vladimir" last="Bumbasirevic">Vladimir Bumbasirevic</name><name sortKey="Harhaji Trajkovic, Ljubica" sort="Harhaji Trajkovic, Ljubica" uniqKey="Harhaji Trajkovic L" first="Ljubica" last="Harhaji-Trajkovic">Ljubica Harhaji-Trajkovic</name><name sortKey="Jovanovic, Maja" sort="Jovanovic, Maja" uniqKey="Jovanovic M" first="Maja" last="Jovanovic">Maja Jovanovic</name><name sortKey="Kravic Stevovic, Tamara" sort="Kravic Stevovic, Tamara" uniqKey="Kravic Stevovic T" first="Tamara" last="Kravic-Stevovic">Tamara Kravic-Stevovic</name><name sortKey="Ristic, Biljana" sort="Ristic, Biljana" uniqKey="Ristic B" first="Biljana" last="Ristic">Biljana Ristic</name><name sortKey="Tovilovic, Gordana" sort="Tovilovic, Gordana" uniqKey="Tovilovic G" first="Gordana" last="Tovilovic">Gordana Tovilovic</name><name sortKey="Trajkovic, Vladimir" sort="Trajkovic, Vladimir" uniqKey="Trajkovic V" first="Vladimir" last="Trajkovic">Vladimir Trajkovic</name><name sortKey="Zogovic, Nevena" sort="Zogovic, Nevena" uniqKey="Zogovic N" first="Nevena" last="Zogovic">Nevena Zogovic</name></noCountry><country name="Serbie"><noRegion><name sortKey="Arsikin, Katarina" sort="Arsikin, Katarina" uniqKey="Arsikin K" first="Katarina" last="Arsikin">Katarina Arsikin</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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