Amyloid-β peptide binds to cytochrome C oxidase subunit 1
Extracellular and intraneuronal accumulation of amyloid-beta aggregates has been demonstrated to be involved in the pathogenesis of Alzheimer's disease (AD). However, the precise mechanism of amyloid-beta neurotoxicity is not completely understood. Previous studies suggest that binding of amylo...
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| Veröffentlicht in: | PloS one 2012-08, Vol.7 (8), p.e42344 |
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| description | Extracellular and intraneuronal accumulation of amyloid-beta aggregates has been demonstrated to be involved in the pathogenesis of Alzheimer's disease (AD). However, the precise mechanism of amyloid-beta neurotoxicity is not completely understood. Previous studies suggest that binding of amyloid-beta to a number of macromolecules has deleterious effects on cellular functions. Mitochondria were found to be the target for amyloid-beta, and mitochondrial dysfunction is well documented in AD. In the present study we have shown for the first time that Aβ 1-42 bound to a peptide comprising the amino-terminal region of cytochrome c oxidase subunit 1. Phage clone, selected after screening of a human brain cDNA library expressed on M13 phage and bearing a 61 amino acid fragment of cytochrome c oxidase subunit 1, bound to Aβ 1-42 in ELISA as well as to Aβ aggregates present in AD brain. Aβ 1-42 and cytochrome c oxidase subunit 1 co-immunoprecipitated from mitochondrial fraction of differentiated human neuroblastoma cells. Likewise, molecular dynamics simulation of the cytochrome c oxidase subunit 1 and the Aβ 1-42 peptide complex resulted in a reliable helix-helix interaction, supporting the experimental results. The interaction between Aβ 1-42 and cytochrome c oxidase subunit 1 may explain, in part, the diminished enzymatic activity of respiratory chain complex IV and subsequent neuronal metabolic dysfunction observed in AD. |
| doi_str_mv | 10.1371/journal.pone.0042344 |
| format | Article |
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However, the precise mechanism of amyloid-beta neurotoxicity is not completely understood. Previous studies suggest that binding of amyloid-beta to a number of macromolecules has deleterious effects on cellular functions. Mitochondria were found to be the target for amyloid-beta, and mitochondrial dysfunction is well documented in AD. In the present study we have shown for the first time that Aβ 1-42 bound to a peptide comprising the amino-terminal region of cytochrome c oxidase subunit 1. Phage clone, selected after screening of a human brain cDNA library expressed on M13 phage and bearing a 61 amino acid fragment of cytochrome c oxidase subunit 1, bound to Aβ 1-42 in ELISA as well as to Aβ aggregates present in AD brain. Aβ 1-42 and cytochrome c oxidase subunit 1 co-immunoprecipitated from mitochondrial fraction of differentiated human neuroblastoma cells. Likewise, molecular dynamics simulation of the cytochrome c oxidase subunit 1 and the Aβ 1-42 peptide complex resulted in a reliable helix-helix interaction, supporting the experimental results. The interaction between Aβ 1-42 and cytochrome c oxidase subunit 1 may explain, in part, the diminished enzymatic activity of respiratory chain complex IV and subsequent neuronal metabolic dysfunction observed in AD.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0042344</identifier><identifier>PMID: 22927926</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Aggregates ; Alzheimer's disease ; Amino Acid Sequence ; Amino acids ; Amyloid beta-Peptides - chemistry ; Amyloid beta-Peptides - metabolism ; Animals ; Biology ; Brain ; Cattle ; Chemistry ; Cloning ; Computer simulation ; Cytochrome ; Cytochrome-c oxidase ; Deoxyribonucleic acid ; DNA ; Electron transport ; Electron Transport Complex IV - chemistry ; Electron Transport Complex IV - metabolism ; Enzymatic activity ; Enzyme-linked immunosorbent assay ; Enzymes ; Humans ; Macromolecules ; Medicine ; Metabolism ; Mitochondria ; Mitochondrial DNA ; Molecular dynamics ; Molecular Dynamics Simulation ; Molecular Sequence Data ; Neuroblastoma ; Neuroblastoma cells ; Neurodegenerative diseases ; Neurosciences ; Neurotoxicity ; Oxidase ; Pathogenesis ; Peptide Fragments - chemistry ; Peptide Fragments - metabolism ; Peptides ; Phages ; Protein Binding ; Protein Multimerization ; Protein Structure, Secondary ; Proteins ; Respiration ; Rodents ; Signal transduction ; Transgenic animals ; β-Amyloid</subject><ispartof>PloS one, 2012-08, Vol.7 (8), p.e42344</ispartof><rights>Hernandez-Zimbron et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2012 Hernandez-Zimbron et al 2012 Hernandez-Zimbron et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c526t-8ad48094cc995f426a82c9e93219edc56542519d8bd048bfaa275eb3fbb083173</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3424232/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3424232/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793,79600,79601</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22927926$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Götz, Jürgen</contributor><creatorcontrib>Hernandez-Zimbron, Luis Fernando</creatorcontrib><creatorcontrib>Luna-Muñoz, Jose</creatorcontrib><creatorcontrib>Mena, Raul</creatorcontrib><creatorcontrib>Vazquez-Ramirez, Ricardo</creatorcontrib><creatorcontrib>Kubli-Garfias, Carlos</creatorcontrib><creatorcontrib>Cribbs, David H</creatorcontrib><creatorcontrib>Manoutcharian, Karen</creatorcontrib><creatorcontrib>Gevorkian, Goar</creatorcontrib><title>Amyloid-β peptide binds to cytochrome C oxidase subunit 1</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Extracellular and intraneuronal accumulation of amyloid-beta aggregates has been demonstrated to be involved in the pathogenesis of Alzheimer's disease (AD). However, the precise mechanism of amyloid-beta neurotoxicity is not completely understood. Previous studies suggest that binding of amyloid-beta to a number of macromolecules has deleterious effects on cellular functions. Mitochondria were found to be the target for amyloid-beta, and mitochondrial dysfunction is well documented in AD. In the present study we have shown for the first time that Aβ 1-42 bound to a peptide comprising the amino-terminal region of cytochrome c oxidase subunit 1. Phage clone, selected after screening of a human brain cDNA library expressed on M13 phage and bearing a 61 amino acid fragment of cytochrome c oxidase subunit 1, bound to Aβ 1-42 in ELISA as well as to Aβ aggregates present in AD brain. Aβ 1-42 and cytochrome c oxidase subunit 1 co-immunoprecipitated from mitochondrial fraction of differentiated human neuroblastoma cells. Likewise, molecular dynamics simulation of the cytochrome c oxidase subunit 1 and the Aβ 1-42 peptide complex resulted in a reliable helix-helix interaction, supporting the experimental results. The interaction between Aβ 1-42 and cytochrome c oxidase subunit 1 may explain, in part, the diminished enzymatic activity of respiratory chain complex IV and subsequent neuronal metabolic dysfunction observed in AD.</description><subject>Aggregates</subject><subject>Alzheimer's disease</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Amyloid beta-Peptides - chemistry</subject><subject>Amyloid beta-Peptides - metabolism</subject><subject>Animals</subject><subject>Biology</subject><subject>Brain</subject><subject>Cattle</subject><subject>Chemistry</subject><subject>Cloning</subject><subject>Computer simulation</subject><subject>Cytochrome</subject><subject>Cytochrome-c oxidase</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>Electron transport</subject><subject>Electron Transport Complex IV - chemistry</subject><subject>Electron Transport Complex IV - metabolism</subject><subject>Enzymatic activity</subject><subject>Enzyme-linked immunosorbent assay</subject><subject>Enzymes</subject><subject>Humans</subject><subject>Macromolecules</subject><subject>Medicine</subject><subject>Metabolism</subject><subject>Mitochondria</subject><subject>Mitochondrial DNA</subject><subject>Molecular dynamics</subject><subject>Molecular Dynamics Simulation</subject><subject>Molecular Sequence Data</subject><subject>Neuroblastoma</subject><subject>Neuroblastoma cells</subject><subject>Neurodegenerative diseases</subject><subject>Neurosciences</subject><subject>Neurotoxicity</subject><subject>Oxidase</subject><subject>Pathogenesis</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - metabolism</subject><subject>Peptides</subject><subject>Phages</subject><subject>Protein Binding</subject><subject>Protein Multimerization</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Respiration</subject><subject>Rodents</subject><subject>Signal transduction</subject><subject>Transgenic animals</subject><subject>β-Amyloid</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNp1kc1u1DAUhS0EoqXwBggidZ3Bf_HYLJCqET-VKnVT1pZ_rluPMnGwk4p5LR6kz4TLpFW7YGXLPue75-og9J7gFWFr8mmb5jyYfjWmAVYYc8o4f4GOiWK0FRSzl0_uR-hNKVuMOyaFeI2OKFV0rag4Rp_Pdvs-Rd_e_WlGGKfoobFx8KWZUuP2U3I3Oe2g2TTpd_SmQFNmOw9xashb9CqYvsC75TxBP799vdr8aC8uv59vzi5a11ExtdJ4LrHizinVBU6FkdQpqNGIAu860XHaEeWl9ZhLG4yh6w4sC9ZiycianaCPB-7Yp6KXtYsmjIq6BBa8Ks4PCp_MVo857kze62Si_veQ8rU2eYquBx1CoJIBr2TggVILnSMSaozgvbVQWV-WabPd1XwwTNn0z6DPf4Z4o6_TrWac1g5oBZwugJx-zVCm_0TmB5XLqZQM4XECwfq-3weXvu9XL_1W24en6R5ND4Wyv4Q_pGU</recordid><startdate>20120821</startdate><enddate>20120821</enddate><creator>Hernandez-Zimbron, Luis Fernando</creator><creator>Luna-Muñoz, Jose</creator><creator>Mena, Raul</creator><creator>Vazquez-Ramirez, Ricardo</creator><creator>Kubli-Garfias, Carlos</creator><creator>Cribbs, David H</creator><creator>Manoutcharian, Karen</creator><creator>Gevorkian, Goar</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><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>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20120821</creationdate><title>Amyloid-β peptide binds to cytochrome C oxidase subunit 1</title><author>Hernandez-Zimbron, Luis Fernando ; Luna-Muñoz, Jose ; Mena, Raul ; Vazquez-Ramirez, Ricardo ; Kubli-Garfias, Carlos ; Cribbs, David H ; Manoutcharian, Karen ; Gevorkian, Goar</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c526t-8ad48094cc995f426a82c9e93219edc56542519d8bd048bfaa275eb3fbb083173</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Aggregates</topic><topic>Alzheimer's disease</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Amyloid beta-Peptides - 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However, the precise mechanism of amyloid-beta neurotoxicity is not completely understood. Previous studies suggest that binding of amyloid-beta to a number of macromolecules has deleterious effects on cellular functions. Mitochondria were found to be the target for amyloid-beta, and mitochondrial dysfunction is well documented in AD. In the present study we have shown for the first time that Aβ 1-42 bound to a peptide comprising the amino-terminal region of cytochrome c oxidase subunit 1. Phage clone, selected after screening of a human brain cDNA library expressed on M13 phage and bearing a 61 amino acid fragment of cytochrome c oxidase subunit 1, bound to Aβ 1-42 in ELISA as well as to Aβ aggregates present in AD brain. Aβ 1-42 and cytochrome c oxidase subunit 1 co-immunoprecipitated from mitochondrial fraction of differentiated human neuroblastoma cells. Likewise, molecular dynamics simulation of the cytochrome c oxidase subunit 1 and the Aβ 1-42 peptide complex resulted in a reliable helix-helix interaction, supporting the experimental results. The interaction between Aβ 1-42 and cytochrome c oxidase subunit 1 may explain, in part, the diminished enzymatic activity of respiratory chain complex IV and subsequent neuronal metabolic dysfunction observed in AD.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>22927926</pmid><doi>10.1371/journal.pone.0042344</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Aggregates Alzheimer's disease Amino Acid Sequence Amino acids Amyloid beta-Peptides - chemistry Amyloid beta-Peptides - metabolism Animals Biology Brain Cattle Chemistry Cloning Computer simulation Cytochrome Cytochrome-c oxidase Deoxyribonucleic acid DNA Electron transport Electron Transport Complex IV - chemistry Electron Transport Complex IV - metabolism Enzymatic activity Enzyme-linked immunosorbent assay Enzymes Humans Macromolecules Medicine Metabolism Mitochondria Mitochondrial DNA Molecular dynamics Molecular Dynamics Simulation Molecular Sequence Data Neuroblastoma Neuroblastoma cells Neurodegenerative diseases Neurosciences Neurotoxicity Oxidase Pathogenesis Peptide Fragments - chemistry Peptide Fragments - metabolism Peptides Phages Protein Binding Protein Multimerization Protein Structure, Secondary Proteins Respiration Rodents Signal transduction Transgenic animals β-Amyloid |
| title | Amyloid-β peptide binds to cytochrome C oxidase subunit 1 |
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