Is trehalose an autophagic inducer? Unraveling the roles of non-reducing disaccharides on autophagic flux and alpha-synuclein aggregation
Autophagy is a pivotal intracellular process by which cellular macromolecules are degraded upon various stimuli. A failure in the degradation of autophagic substrates such as impaired organelles and protein aggregates leads to their accumulations, which are characteristics of many neurodegenerative...
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| creator | Yoon, Ye-Seul Cho, Eun-Duk Jung Ahn, Woo Won Lee, Kyung Lee, Seung-Jae Lee, He-Jin |
| description | Autophagy is a pivotal intracellular process by which cellular macromolecules are degraded upon various stimuli. A failure in the degradation of autophagic substrates such as impaired organelles and protein aggregates leads to their accumulations, which are characteristics of many neurodegenerative diseases. Pharmacological activation of autophagy has thus been considered a prospective therapeutic approach for treating neurodegenerative diseases. Among a number of autophagy-inducing agents, trehalose has received attention for its beneficial effects in different disease models of neurodegeneration. However, how trehalose promotes autophagy has not been fully revealed. We investigated the influence of trehalose and other disaccharides upon autophagic flux and aggregation of
α
-synuclein, a protein linked to Parkinson's disease. In differentiated human neuroblastoma and primary rat cortical neuron culture models, treatment with trehalose and other disaccharides resulted in accumulation of lipidated LC3 (LC3-II), p62, and autophagosomes, whereas it decreased autolysosomes. On the other hand, addition of Bafilomycin A1 to trehalose treatments had relatively marginal effect, an indicative of autophagic flux blockage. In concordance with these results, the cells treated with trehalose exhibited an incremental tendency in
α-
synuclein aggregation. Secretion of
α-
synuclein was also elevated in the culture medium upon trehalose treatment, thereby significantly increasing intercellular transmission of this protein. Despite the substantial increase in
α-
synuclein aggregation, which normally leads to cell death, cell viability was not affected upon treatment with trehalose, suggesting an autophagy-independent protective function of trehalose against protein aggregates. This study demonstrates that, although trehalose has been widely considered an autophagic inducer, it may be actually a potent blocker of the autophagic flux. |
| doi_str_mv | 10.1038/cddis.2017.501 |
| format | Article |
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α
-synuclein, a protein linked to Parkinson's disease. In differentiated human neuroblastoma and primary rat cortical neuron culture models, treatment with trehalose and other disaccharides resulted in accumulation of lipidated LC3 (LC3-II), p62, and autophagosomes, whereas it decreased autolysosomes. On the other hand, addition of Bafilomycin A1 to trehalose treatments had relatively marginal effect, an indicative of autophagic flux blockage. In concordance with these results, the cells treated with trehalose exhibited an incremental tendency in
α-
synuclein aggregation. Secretion of
α-
synuclein was also elevated in the culture medium upon trehalose treatment, thereby significantly increasing intercellular transmission of this protein. Despite the substantial increase in
α-
synuclein aggregation, which normally leads to cell death, cell viability was not affected upon treatment with trehalose, suggesting an autophagy-independent protective function of trehalose against protein aggregates. This study demonstrates that, although trehalose has been widely considered an autophagic inducer, it may be actually a potent blocker of the autophagic flux.</description><identifier>ISSN: 2041-4889</identifier><identifier>EISSN: 2041-4889</identifier><identifier>DOI: 10.1038/cddis.2017.501</identifier><identifier>PMID: 28981090</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/378/1689/364 ; 631/45/72/1205 ; 631/80/470/2284 ; 631/80/82/39 ; alpha-Synuclein - genetics ; Animal models ; Animals ; Antibodies ; Autophagosomes - drug effects ; Autophagy ; Autophagy - drug effects ; Biochemistry ; Cell Biology ; Cell Culture ; Cell death ; Cell Survival - drug effects ; Disaccharides ; Disaccharides - administration & dosage ; Humans ; Immunology ; Life Sciences ; Lysosomes ; Macromolecules ; Microtubule-Associated Proteins - chemistry ; Microtubule-Associated Proteins - genetics ; Movement disorders ; Neuroblastoma ; Neurodegeneration ; Neurodegenerative diseases ; Neurons - drug effects ; Organelles ; Original ; original-article ; Parkinson Disease - drug therapy ; Parkinson Disease - genetics ; Parkinson Disease - pathology ; Parkinson's disease ; Phagocytosis ; Phagosomes ; Primary Cell Culture ; Protein Aggregation, Pathological - drug therapy ; Protein Aggregation, Pathological - genetics ; Protein Aggregation, Pathological - pathology ; Proteins ; Rats ; RNA-Binding Proteins - chemistry ; RNA-Binding Proteins - genetics ; Secretion ; Synuclein ; Trehalose ; Trehalose - administration & dosage</subject><ispartof>Cell death & disease, 2017-10, Vol.8 (10), p.e3091-e3091</ispartof><rights>The Author(s) 2017</rights><rights>Copyright Nature Publishing Group Oct 2017</rights><rights>Copyright © 2017 The Author(s) 2017 The Author(s)</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c524t-f9820dafcb71c2c1c68daea49d216f2c9648f0d968d4c06074be09bbe9508c6c3</citedby><cites>FETCH-LOGICAL-c524t-f9820dafcb71c2c1c68daea49d216f2c9648f0d968d4c06074be09bbe9508c6c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5682667/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5682667/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,27901,27902,41096,42165,51551,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28981090$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yoon, Ye-Seul</creatorcontrib><creatorcontrib>Cho, Eun-Duk</creatorcontrib><creatorcontrib>Jung Ahn, Woo</creatorcontrib><creatorcontrib>Won Lee, Kyung</creatorcontrib><creatorcontrib>Lee, Seung-Jae</creatorcontrib><creatorcontrib>Lee, He-Jin</creatorcontrib><title>Is trehalose an autophagic inducer? Unraveling the roles of non-reducing disaccharides on autophagic flux and alpha-synuclein aggregation</title><title>Cell death & disease</title><addtitle>Cell Death Dis</addtitle><addtitle>Cell Death Dis</addtitle><description>Autophagy is a pivotal intracellular process by which cellular macromolecules are degraded upon various stimuli. A failure in the degradation of autophagic substrates such as impaired organelles and protein aggregates leads to their accumulations, which are characteristics of many neurodegenerative diseases. Pharmacological activation of autophagy has thus been considered a prospective therapeutic approach for treating neurodegenerative diseases. Among a number of autophagy-inducing agents, trehalose has received attention for its beneficial effects in different disease models of neurodegeneration. However, how trehalose promotes autophagy has not been fully revealed. We investigated the influence of trehalose and other disaccharides upon autophagic flux and aggregation of
α
-synuclein, a protein linked to Parkinson's disease. In differentiated human neuroblastoma and primary rat cortical neuron culture models, treatment with trehalose and other disaccharides resulted in accumulation of lipidated LC3 (LC3-II), p62, and autophagosomes, whereas it decreased autolysosomes. On the other hand, addition of Bafilomycin A1 to trehalose treatments had relatively marginal effect, an indicative of autophagic flux blockage. In concordance with these results, the cells treated with trehalose exhibited an incremental tendency in
α-
synuclein aggregation. Secretion of
α-
synuclein was also elevated in the culture medium upon trehalose treatment, thereby significantly increasing intercellular transmission of this protein. Despite the substantial increase in
α-
synuclein aggregation, which normally leads to cell death, cell viability was not affected upon treatment with trehalose, suggesting an autophagy-independent protective function of trehalose against protein aggregates. This study demonstrates that, although trehalose has been widely considered an autophagic inducer, it may be actually a potent blocker of the autophagic flux.</description><subject>631/378/1689/364</subject><subject>631/45/72/1205</subject><subject>631/80/470/2284</subject><subject>631/80/82/39</subject><subject>alpha-Synuclein - genetics</subject><subject>Animal models</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Autophagosomes - drug effects</subject><subject>Autophagy</subject><subject>Autophagy - drug effects</subject><subject>Biochemistry</subject><subject>Cell Biology</subject><subject>Cell Culture</subject><subject>Cell death</subject><subject>Cell Survival - drug effects</subject><subject>Disaccharides</subject><subject>Disaccharides - administration & dosage</subject><subject>Humans</subject><subject>Immunology</subject><subject>Life Sciences</subject><subject>Lysosomes</subject><subject>Macromolecules</subject><subject>Microtubule-Associated Proteins - chemistry</subject><subject>Microtubule-Associated Proteins - genetics</subject><subject>Movement disorders</subject><subject>Neuroblastoma</subject><subject>Neurodegeneration</subject><subject>Neurodegenerative diseases</subject><subject>Neurons - drug effects</subject><subject>Organelles</subject><subject>Original</subject><subject>original-article</subject><subject>Parkinson Disease - drug therapy</subject><subject>Parkinson Disease - genetics</subject><subject>Parkinson Disease - pathology</subject><subject>Parkinson's disease</subject><subject>Phagocytosis</subject><subject>Phagosomes</subject><subject>Primary Cell Culture</subject><subject>Protein Aggregation, Pathological - drug therapy</subject><subject>Protein Aggregation, Pathological - genetics</subject><subject>Protein Aggregation, Pathological - pathology</subject><subject>Proteins</subject><subject>Rats</subject><subject>RNA-Binding Proteins - chemistry</subject><subject>RNA-Binding Proteins - genetics</subject><subject>Secretion</subject><subject>Synuclein</subject><subject>Trehalose</subject><subject>Trehalose - administration & dosage</subject><issn>2041-4889</issn><issn>2041-4889</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNptkcFvFCEUxonR2Kb26tGQePEyW2AZBi4a06ht0sSLPRMG3szQsLDCTNP-Cf7Xst3abBu5QN734-M9PoTeU7KiZC3PrHO-rBih3aol9BU6ZoTThkupXh-cj9BpKTekrvWasFa8RUdMKkmJIsfoz2XBc4bJhFQAm4jNMqftZEZvsY9usZC_4OuYzS0EH0c8T4BzClBwGnBMsclQoZ1SWzHWTiZ7t1OfOQ1huavmDptQK025j4sN4CszjhlGM_sU36E3gwkFTh_3E3T9_duv84vm6uePy_OvV41tGZ-bQUlGnBls31HLLLVCOgOGK8eoGJhVgsuBOFXL3BJBOt4DUX0PqiXSCrs-QZ_3vtul34CzEOdsgt5mvzH5Xifj9XMl-kmP6Va3QjIhumrw6dEgp98LlFlvfLEQgomQlqKp4p1g9XtlRT--QG_SkmMd74EinLdKVGq1p2xOpWQYnpqhRO-C1g9B613QugZdL3w4HOEJ_xdrBc72QKlSHCEfvPt_y7-kdLgi</recordid><startdate>20171005</startdate><enddate>20171005</enddate><creator>Yoon, Ye-Seul</creator><creator>Cho, Eun-Duk</creator><creator>Jung Ahn, Woo</creator><creator>Won Lee, Kyung</creator><creator>Lee, Seung-Jae</creator><creator>Lee, He-Jin</creator><general>Nature Publishing Group UK</general><general>Springer Nature B.V</general><general>Nature Publishing Group</general><scope>C6C</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20171005</creationdate><title>Is trehalose an autophagic inducer? Unraveling the roles of non-reducing disaccharides on autophagic flux and alpha-synuclein aggregation</title><author>Yoon, Ye-Seul ; Cho, Eun-Duk ; Jung Ahn, Woo ; Won Lee, Kyung ; Lee, Seung-Jae ; Lee, He-Jin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c524t-f9820dafcb71c2c1c68daea49d216f2c9648f0d968d4c06074be09bbe9508c6c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>631/378/1689/364</topic><topic>631/45/72/1205</topic><topic>631/80/470/2284</topic><topic>631/80/82/39</topic><topic>alpha-Synuclein - genetics</topic><topic>Animal models</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Autophagosomes - drug effects</topic><topic>Autophagy</topic><topic>Autophagy - drug effects</topic><topic>Biochemistry</topic><topic>Cell Biology</topic><topic>Cell Culture</topic><topic>Cell death</topic><topic>Cell Survival - drug effects</topic><topic>Disaccharides</topic><topic>Disaccharides - administration & dosage</topic><topic>Humans</topic><topic>Immunology</topic><topic>Life Sciences</topic><topic>Lysosomes</topic><topic>Macromolecules</topic><topic>Microtubule-Associated Proteins - chemistry</topic><topic>Microtubule-Associated Proteins - genetics</topic><topic>Movement disorders</topic><topic>Neuroblastoma</topic><topic>Neurodegeneration</topic><topic>Neurodegenerative diseases</topic><topic>Neurons - drug effects</topic><topic>Organelles</topic><topic>Original</topic><topic>original-article</topic><topic>Parkinson Disease - drug therapy</topic><topic>Parkinson Disease - genetics</topic><topic>Parkinson Disease - pathology</topic><topic>Parkinson's disease</topic><topic>Phagocytosis</topic><topic>Phagosomes</topic><topic>Primary Cell Culture</topic><topic>Protein Aggregation, Pathological - drug therapy</topic><topic>Protein Aggregation, Pathological - genetics</topic><topic>Protein Aggregation, Pathological - pathology</topic><topic>Proteins</topic><topic>Rats</topic><topic>RNA-Binding Proteins - chemistry</topic><topic>RNA-Binding Proteins - genetics</topic><topic>Secretion</topic><topic>Synuclein</topic><topic>Trehalose</topic><topic>Trehalose - administration & dosage</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yoon, Ye-Seul</creatorcontrib><creatorcontrib>Cho, Eun-Duk</creatorcontrib><creatorcontrib>Jung Ahn, Woo</creatorcontrib><creatorcontrib>Won Lee, Kyung</creatorcontrib><creatorcontrib>Lee, Seung-Jae</creatorcontrib><creatorcontrib>Lee, He-Jin</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell death & disease</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yoon, Ye-Seul</au><au>Cho, Eun-Duk</au><au>Jung Ahn, Woo</au><au>Won Lee, Kyung</au><au>Lee, Seung-Jae</au><au>Lee, He-Jin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Is trehalose an autophagic inducer? Unraveling the roles of non-reducing disaccharides on autophagic flux and alpha-synuclein aggregation</atitle><jtitle>Cell death & disease</jtitle><stitle>Cell Death Dis</stitle><addtitle>Cell Death Dis</addtitle><date>2017-10-05</date><risdate>2017</risdate><volume>8</volume><issue>10</issue><spage>e3091</spage><epage>e3091</epage><pages>e3091-e3091</pages><issn>2041-4889</issn><eissn>2041-4889</eissn><abstract>Autophagy is a pivotal intracellular process by which cellular macromolecules are degraded upon various stimuli. A failure in the degradation of autophagic substrates such as impaired organelles and protein aggregates leads to their accumulations, which are characteristics of many neurodegenerative diseases. Pharmacological activation of autophagy has thus been considered a prospective therapeutic approach for treating neurodegenerative diseases. Among a number of autophagy-inducing agents, trehalose has received attention for its beneficial effects in different disease models of neurodegeneration. However, how trehalose promotes autophagy has not been fully revealed. We investigated the influence of trehalose and other disaccharides upon autophagic flux and aggregation of
α
-synuclein, a protein linked to Parkinson's disease. In differentiated human neuroblastoma and primary rat cortical neuron culture models, treatment with trehalose and other disaccharides resulted in accumulation of lipidated LC3 (LC3-II), p62, and autophagosomes, whereas it decreased autolysosomes. On the other hand, addition of Bafilomycin A1 to trehalose treatments had relatively marginal effect, an indicative of autophagic flux blockage. In concordance with these results, the cells treated with trehalose exhibited an incremental tendency in
α-
synuclein aggregation. Secretion of
α-
synuclein was also elevated in the culture medium upon trehalose treatment, thereby significantly increasing intercellular transmission of this protein. Despite the substantial increase in
α-
synuclein aggregation, which normally leads to cell death, cell viability was not affected upon treatment with trehalose, suggesting an autophagy-independent protective function of trehalose against protein aggregates. This study demonstrates that, although trehalose has been widely considered an autophagic inducer, it may be actually a potent blocker of the autophagic flux.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>28981090</pmid><doi>10.1038/cddis.2017.501</doi><oa>free_for_read</oa></addata></record> |
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| subjects | 631/378/1689/364 631/45/72/1205 631/80/470/2284 631/80/82/39 alpha-Synuclein - genetics Animal models Animals Antibodies Autophagosomes - drug effects Autophagy Autophagy - drug effects Biochemistry Cell Biology Cell Culture Cell death Cell Survival - drug effects Disaccharides Disaccharides - administration & dosage Humans Immunology Life Sciences Lysosomes Macromolecules Microtubule-Associated Proteins - chemistry Microtubule-Associated Proteins - genetics Movement disorders Neuroblastoma Neurodegeneration Neurodegenerative diseases Neurons - drug effects Organelles Original original-article Parkinson Disease - drug therapy Parkinson Disease - genetics Parkinson Disease - pathology Parkinson's disease Phagocytosis Phagosomes Primary Cell Culture Protein Aggregation, Pathological - drug therapy Protein Aggregation, Pathological - genetics Protein Aggregation, Pathological - pathology Proteins Rats RNA-Binding Proteins - chemistry RNA-Binding Proteins - genetics Secretion Synuclein Trehalose Trehalose - administration & dosage |
| title | Is trehalose an autophagic inducer? Unraveling the roles of non-reducing disaccharides on autophagic flux and alpha-synuclein aggregation |
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