Aggregates from mutant and wild-type α-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of β-sheet and amyloid-like filaments
α-Synuclein (α-syn) protein and a fragment of it, called NAC, have been found in association with the pathological lesions of a number of neurodegenerative diseases. Recently, mutations in the α-syn gene have been reported in families susceptible to an inherited form of Parkinson's disease. We...
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| Veröffentlicht in: | FEBS letters 1998-11, Vol.440 (1), p.71-75 |
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| creator | El-Agnaf, Omar M.A Jakes, Ross Curran, Martin D Middleton, Derek Ingenito, Raffaele Bianchi, Elisabetta Pessi, Antonello Neill, David Wallace, Andrew |
| description | α-Synuclein (α-syn) protein and a fragment of it, called NAC, have been found in association with the pathological lesions of a number of neurodegenerative diseases. Recently, mutations in the α-syn gene have been reported in families susceptible to an inherited form of Parkinson's disease. We have shown that human wild-type α-syn, mutant α-syn(Ala30Pro) and mutant α-syn(Ala53Thr) proteins can self-aggregate and form amyloid-like filaments. Here we report that aggregates of NAC and α-syn proteins induced apoptotic cell death in human neuroblastoma SH-SY5Y cells. These findings indicate that accumulation of α-syn and its degradation products may play a major role in the development of the pathogenesis of these neurodegenerative diseases. |
| doi_str_mv | 10.1016/S0014-5793(98)01418-5 |
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Recently, mutations in the α-syn gene have been reported in families susceptible to an inherited form of Parkinson's disease. We have shown that human wild-type α-syn, mutant α-syn(Ala30Pro) and mutant α-syn(Ala53Thr) proteins can self-aggregate and form amyloid-like filaments. Here we report that aggregates of NAC and α-syn proteins induced apoptotic cell death in human neuroblastoma SH-SY5Y cells. These findings indicate that accumulation of α-syn and its degradation products may play a major role in the development of the pathogenesis of these neurodegenerative diseases.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(98)01418-5</identifier><identifier>PMID: 9862428</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>AD, Alzheimer's disease ; alpha-Synuclein ; ALS, amyotrophic lateral sclerosis ; Amyloid ; Amyloid - chemistry ; Amyloid - metabolism ; Amyloid - physiology ; Apoptosis ; Aβ, β-amyloid protein ; Biopolymers - metabolism ; Biopolymers - physiology ; Cell Nucleus - metabolism ; Cell Survival ; Circular Dichroism ; DLB, dementia with Lewy bodies ; GCI, glial cytoplasmic inclusion ; HD, Huntington's disease ; Humans ; LB, Lewy body ; Lewy body ; LN, Lewy neurite ; Microscopy, Electron ; MSA, multiple system atrophy ; Mutation ; NAC, non-Aβ component of AD amyloid ; Nerve Tissue Proteins - chemistry ; Nerve Tissue Proteins - genetics ; Nerve Tissue Proteins - metabolism ; Nerve Tissue Proteins - physiology ; Neuroblastoma ; Neurodegenerative disease ; Neurodegenerative Diseases - etiology ; Neurons - cytology ; Parkinson Disease - etiology ; Parkinson Disease - genetics ; Parkinson's disease ; PD, Parkinson's disease ; Peptides - metabolism ; Peptides - physiology ; Protein Structure, Secondary ; Synucleins ; Thiazoles ; Toxicity ; Tumor Cells, Cultured ; α-Synuclein</subject><ispartof>FEBS letters, 1998-11, Vol.440 (1), p.71-75</ispartof><rights>1998 Federation of European Biochemical Societies</rights><rights>FEBS Letters 440 (1998) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4255-7ceb8f0946c472648f9ba179008040b5749de549c4526897c628657cfa5d3a513</citedby><cites>FETCH-LOGICAL-c4255-7ceb8f0946c472648f9ba179008040b5749de549c4526897c628657cfa5d3a513</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2898%2901418-5$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579398014185$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9862428$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>El-Agnaf, Omar M.A</creatorcontrib><creatorcontrib>Jakes, Ross</creatorcontrib><creatorcontrib>Curran, Martin D</creatorcontrib><creatorcontrib>Middleton, Derek</creatorcontrib><creatorcontrib>Ingenito, Raffaele</creatorcontrib><creatorcontrib>Bianchi, Elisabetta</creatorcontrib><creatorcontrib>Pessi, Antonello</creatorcontrib><creatorcontrib>Neill, David</creatorcontrib><creatorcontrib>Wallace, Andrew</creatorcontrib><title>Aggregates from mutant and wild-type α-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of β-sheet and amyloid-like filaments</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>α-Synuclein (α-syn) protein and a fragment of it, called NAC, have been found in association with the pathological lesions of a number of neurodegenerative diseases. Recently, mutations in the α-syn gene have been reported in families susceptible to an inherited form of Parkinson's disease. We have shown that human wild-type α-syn, mutant α-syn(Ala30Pro) and mutant α-syn(Ala53Thr) proteins can self-aggregate and form amyloid-like filaments. Here we report that aggregates of NAC and α-syn proteins induced apoptotic cell death in human neuroblastoma SH-SY5Y cells. These findings indicate that accumulation of α-syn and its degradation products may play a major role in the development of the pathogenesis of these neurodegenerative diseases.</description><subject>AD, Alzheimer's disease</subject><subject>alpha-Synuclein</subject><subject>ALS, amyotrophic lateral sclerosis</subject><subject>Amyloid</subject><subject>Amyloid - chemistry</subject><subject>Amyloid - metabolism</subject><subject>Amyloid - physiology</subject><subject>Apoptosis</subject><subject>Aβ, β-amyloid protein</subject><subject>Biopolymers - metabolism</subject><subject>Biopolymers - physiology</subject><subject>Cell Nucleus - metabolism</subject><subject>Cell Survival</subject><subject>Circular Dichroism</subject><subject>DLB, dementia with Lewy bodies</subject><subject>GCI, glial cytoplasmic inclusion</subject><subject>HD, Huntington's disease</subject><subject>Humans</subject><subject>LB, Lewy body</subject><subject>Lewy body</subject><subject>LN, Lewy neurite</subject><subject>Microscopy, Electron</subject><subject>MSA, multiple system atrophy</subject><subject>Mutation</subject><subject>NAC, non-Aβ component of AD amyloid</subject><subject>Nerve Tissue Proteins - chemistry</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Nerve Tissue Proteins - physiology</subject><subject>Neuroblastoma</subject><subject>Neurodegenerative disease</subject><subject>Neurodegenerative Diseases - etiology</subject><subject>Neurons - cytology</subject><subject>Parkinson Disease - etiology</subject><subject>Parkinson Disease - genetics</subject><subject>Parkinson's disease</subject><subject>PD, Parkinson's disease</subject><subject>Peptides - metabolism</subject><subject>Peptides - physiology</subject><subject>Protein Structure, Secondary</subject><subject>Synucleins</subject><subject>Thiazoles</subject><subject>Toxicity</subject><subject>Tumor Cells, Cultured</subject><subject>α-Synuclein</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUcFu1DAUjBColMInVPIJwSFgJ3Zin9CyailSBQfgbDn2y64hsYPtgPJZcOEv-k14s6te4fTsN_PmjT1FcUnwK4JJ8_oTxoSWrBX1C8Ff5jPhJXtQnBPe1mVNG_6wOL-nPC6exPgV5zsn4qw4E7ypaMXPiz-b3S7ATiWIqA9-ROOclEtIOYN-2sGUaZkA3f0q4-JmPYB1aAo-5RpXzofNFk0wJWsAWWdmDUhNfko-WY00DAMyoNI-Y2g_j8ohB3Pw3aBi8qNaGRF1C-p9GFWy3iHfo7vfZdwDHF2ocRm8NeVgvwHq7aBGcCk-LR71aojw7FQvii_XV5-3N-Xtx3fvt5vbUtOKsbLV0PEeC9po2lYN5b3oFGkFxhxT3LGWCgOMCk1Z1XDR6qbiDWt1r5ipFSP1RfH8qJtf_X2GmORo48G1cuDnKBtBspaoM5EdiTr4GAP0cgp2VGGRBMtDYHINTB7SkILLNTDJ8tzlacHcjWDup04JZfzmiOc0YPk_UXl99bZakQMg-No-rHpzlIL8YT8sBBm1BafB2AA6SePtP8z-BbTyvbU</recordid><startdate>19981127</startdate><enddate>19981127</enddate><creator>El-Agnaf, Omar M.A</creator><creator>Jakes, Ross</creator><creator>Curran, Martin D</creator><creator>Middleton, Derek</creator><creator>Ingenito, Raffaele</creator><creator>Bianchi, Elisabetta</creator><creator>Pessi, Antonello</creator><creator>Neill, David</creator><creator>Wallace, Andrew</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope></search><sort><creationdate>19981127</creationdate><title>Aggregates from mutant and wild-type α-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of β-sheet and amyloid-like filaments</title><author>El-Agnaf, Omar M.A ; Jakes, Ross ; Curran, Martin D ; Middleton, Derek ; Ingenito, Raffaele ; Bianchi, Elisabetta ; Pessi, Antonello ; Neill, David ; Wallace, Andrew</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4255-7ceb8f0946c472648f9ba179008040b5749de549c4526897c628657cfa5d3a513</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>AD, Alzheimer's disease</topic><topic>alpha-Synuclein</topic><topic>ALS, amyotrophic lateral sclerosis</topic><topic>Amyloid</topic><topic>Amyloid - chemistry</topic><topic>Amyloid - metabolism</topic><topic>Amyloid - physiology</topic><topic>Apoptosis</topic><topic>Aβ, β-amyloid protein</topic><topic>Biopolymers - metabolism</topic><topic>Biopolymers - physiology</topic><topic>Cell Nucleus - metabolism</topic><topic>Cell Survival</topic><topic>Circular Dichroism</topic><topic>DLB, dementia with Lewy bodies</topic><topic>GCI, glial cytoplasmic inclusion</topic><topic>HD, Huntington's disease</topic><topic>Humans</topic><topic>LB, Lewy body</topic><topic>Lewy body</topic><topic>LN, Lewy neurite</topic><topic>Microscopy, Electron</topic><topic>MSA, multiple system atrophy</topic><topic>Mutation</topic><topic>NAC, non-Aβ component of AD amyloid</topic><topic>Nerve Tissue Proteins - chemistry</topic><topic>Nerve Tissue Proteins - genetics</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Nerve Tissue Proteins - physiology</topic><topic>Neuroblastoma</topic><topic>Neurodegenerative disease</topic><topic>Neurodegenerative Diseases - etiology</topic><topic>Neurons - cytology</topic><topic>Parkinson Disease - etiology</topic><topic>Parkinson Disease - genetics</topic><topic>Parkinson's disease</topic><topic>PD, Parkinson's disease</topic><topic>Peptides - metabolism</topic><topic>Peptides - physiology</topic><topic>Protein Structure, Secondary</topic><topic>Synucleins</topic><topic>Thiazoles</topic><topic>Toxicity</topic><topic>Tumor Cells, Cultured</topic><topic>α-Synuclein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>El-Agnaf, Omar M.A</creatorcontrib><creatorcontrib>Jakes, Ross</creatorcontrib><creatorcontrib>Curran, Martin D</creatorcontrib><creatorcontrib>Middleton, Derek</creatorcontrib><creatorcontrib>Ingenito, Raffaele</creatorcontrib><creatorcontrib>Bianchi, Elisabetta</creatorcontrib><creatorcontrib>Pessi, Antonello</creatorcontrib><creatorcontrib>Neill, David</creatorcontrib><creatorcontrib>Wallace, Andrew</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>El-Agnaf, Omar M.A</au><au>Jakes, Ross</au><au>Curran, Martin D</au><au>Middleton, Derek</au><au>Ingenito, Raffaele</au><au>Bianchi, Elisabetta</au><au>Pessi, Antonello</au><au>Neill, David</au><au>Wallace, Andrew</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Aggregates from mutant and wild-type α-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of β-sheet and amyloid-like filaments</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1998-11-27</date><risdate>1998</risdate><volume>440</volume><issue>1</issue><spage>71</spage><epage>75</epage><pages>71-75</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>α-Synuclein (α-syn) protein and a fragment of it, called NAC, have been found in association with the pathological lesions of a number of neurodegenerative diseases. Recently, mutations in the α-syn gene have been reported in families susceptible to an inherited form of Parkinson's disease. We have shown that human wild-type α-syn, mutant α-syn(Ala30Pro) and mutant α-syn(Ala53Thr) proteins can self-aggregate and form amyloid-like filaments. Here we report that aggregates of NAC and α-syn proteins induced apoptotic cell death in human neuroblastoma SH-SY5Y cells. These findings indicate that accumulation of α-syn and its degradation products may play a major role in the development of the pathogenesis of these neurodegenerative diseases.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>9862428</pmid><doi>10.1016/S0014-5793(98)01418-5</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 1998-11, Vol.440 (1), p.71-75 |
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| source | Wiley Free Content; MEDLINE; Elsevier ScienceDirect Journals Complete; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | AD, Alzheimer's disease alpha-Synuclein ALS, amyotrophic lateral sclerosis Amyloid Amyloid - chemistry Amyloid - metabolism Amyloid - physiology Apoptosis Aβ, β-amyloid protein Biopolymers - metabolism Biopolymers - physiology Cell Nucleus - metabolism Cell Survival Circular Dichroism DLB, dementia with Lewy bodies GCI, glial cytoplasmic inclusion HD, Huntington's disease Humans LB, Lewy body Lewy body LN, Lewy neurite Microscopy, Electron MSA, multiple system atrophy Mutation NAC, non-Aβ component of AD amyloid Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Nerve Tissue Proteins - physiology Neuroblastoma Neurodegenerative disease Neurodegenerative Diseases - etiology Neurons - cytology Parkinson Disease - etiology Parkinson Disease - genetics Parkinson's disease PD, Parkinson's disease Peptides - metabolism Peptides - physiology Protein Structure, Secondary Synucleins Thiazoles Toxicity Tumor Cells, Cultured α-Synuclein |
| title | Aggregates from mutant and wild-type α-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of β-sheet and amyloid-like filaments |
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