Amyloid β cytotoxicity is enhanced or reduced depending on formation of amyloid β oligomeric forms
Objectives We explored the underlying mechanisms that facilitate reducing and enhancing effects of exogenous proteins on cytotoxicity of amyloid β (Aβ), a main pathogen of Alzheimer’s disease, by using an Escherichia coli chaperonin DnaK. Results DnaK was chosen as a tool, because it, easily availab...
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| Veröffentlicht in: | Biotechnology letters 2021, Vol.43 (1), p.165-175 |
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| creator | Shahnawaz, Md Bilkis, Tahmina Park, Il-Seon |
| description | Objectives
We explored the underlying mechanisms that facilitate reducing and enhancing effects of exogenous proteins on cytotoxicity of amyloid β (Aβ), a main pathogen of Alzheimer’s disease, by using an
Escherichia coli
chaperonin DnaK.
Results
DnaK was chosen as a tool, because it, easily available and functionally stable, reduced or enhanced Aβ cytotoxicity depending on its concentration. Cytotoxicity was enhanced when the molar ratio of DnaK to Aβ42, at 20 μM Aβ42, was 0.01–0.5, while reduced cytotoxicity was observed at higher ratios (> 1) at 1 μM Aβ42. Significant amounts of oligomeric Aβ42 species accumulated concomitantly with enhanced cytotoxicity, whereas the oligomers appeared to form complexes with DnaK in conditions of reduced cytotoxicity.
Conclusions
The difference in cytotoxicity was due to variations in the toxic oligomeric Aβ species and DnaK is a useful tool for the study of the Aβ ultrastructure formation and toxicity of Aβ peptide. |
| doi_str_mv | 10.1007/s10529-020-03015-8 |
| format | Article |
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We explored the underlying mechanisms that facilitate reducing and enhancing effects of exogenous proteins on cytotoxicity of amyloid β (Aβ), a main pathogen of Alzheimer’s disease, by using an
Escherichia coli
chaperonin DnaK.
Results
DnaK was chosen as a tool, because it, easily available and functionally stable, reduced or enhanced Aβ cytotoxicity depending on its concentration. Cytotoxicity was enhanced when the molar ratio of DnaK to Aβ42, at 20 μM Aβ42, was 0.01–0.5, while reduced cytotoxicity was observed at higher ratios (> 1) at 1 μM Aβ42. Significant amounts of oligomeric Aβ42 species accumulated concomitantly with enhanced cytotoxicity, whereas the oligomers appeared to form complexes with DnaK in conditions of reduced cytotoxicity.
Conclusions
The difference in cytotoxicity was due to variations in the toxic oligomeric Aβ species and DnaK is a useful tool for the study of the Aβ ultrastructure formation and toxicity of Aβ peptide.</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1007/s10529-020-03015-8</identifier><identifier>PMID: 33025333</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Alzheimer's disease ; Amyloid ; Applied Microbiology ; Biochemistry ; Biomedical and Life Sciences ; Biotechnology ; Cytotoxicity ; DnaK protein ; E coli ; Life Sciences ; Microbiology ; Neurodegenerative diseases ; Oligomers ; Original Research Paper ; Toxicity ; Ultrastructure</subject><ispartof>Biotechnology letters, 2021, Vol.43 (1), p.165-175</ispartof><rights>Springer Nature B.V. 2020</rights><rights>Springer Nature B.V. 2020.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-d0d7ef670c96ea517a6e19c77cd48ebe2e3fdf45c5c77862858dec6b9dcf83483</citedby><cites>FETCH-LOGICAL-c375t-d0d7ef670c96ea517a6e19c77cd48ebe2e3fdf45c5c77862858dec6b9dcf83483</cites><orcidid>0000-0003-4754-6142</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10529-020-03015-8$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10529-020-03015-8$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,27905,27906,41469,42538,51300</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33025333$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shahnawaz, Md</creatorcontrib><creatorcontrib>Bilkis, Tahmina</creatorcontrib><creatorcontrib>Park, Il-Seon</creatorcontrib><title>Amyloid β cytotoxicity is enhanced or reduced depending on formation of amyloid β oligomeric forms</title><title>Biotechnology letters</title><addtitle>Biotechnol Lett</addtitle><addtitle>Biotechnol Lett</addtitle><description>Objectives
We explored the underlying mechanisms that facilitate reducing and enhancing effects of exogenous proteins on cytotoxicity of amyloid β (Aβ), a main pathogen of Alzheimer’s disease, by using an
Escherichia coli
chaperonin DnaK.
Results
DnaK was chosen as a tool, because it, easily available and functionally stable, reduced or enhanced Aβ cytotoxicity depending on its concentration. Cytotoxicity was enhanced when the molar ratio of DnaK to Aβ42, at 20 μM Aβ42, was 0.01–0.5, while reduced cytotoxicity was observed at higher ratios (> 1) at 1 μM Aβ42. Significant amounts of oligomeric Aβ42 species accumulated concomitantly with enhanced cytotoxicity, whereas the oligomers appeared to form complexes with DnaK in conditions of reduced cytotoxicity.
Conclusions
The difference in cytotoxicity was due to variations in the toxic oligomeric Aβ species and DnaK is a useful tool for the study of the Aβ ultrastructure formation and toxicity of Aβ peptide.</description><subject>Alzheimer's disease</subject><subject>Amyloid</subject><subject>Applied Microbiology</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Cytotoxicity</subject><subject>DnaK protein</subject><subject>E coli</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>Neurodegenerative diseases</subject><subject>Oligomers</subject><subject>Original Research Paper</subject><subject>Toxicity</subject><subject>Ultrastructure</subject><issn>0141-5492</issn><issn>1573-6776</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kEtOwzAQQC0EoqVwARbIEuvA2I7jZFlV_CQkNrC2UntSXDVxsVOJXIuDcCbSptAdK4_s5zfSI-SSwQ0DULeRgeRFAhwSEMBkkh-RMZNKJJlS2TEZA0tZItOCj8hZjEsAKBSoUzISArgUQoyJndbdyjtLv7-o6Vrf-k9nXNtRFyk272Vj0FIfaEC72Y4W19hY1yyob2jlQ122rp98RcuDyK_cwtcYnNkh8ZycVOUq4sX-nJC3-7vX2WPy_PLwNJs-J0Yo2SYWrMIqU2CKDEvJVJkhK4xSxqY5zpGjqGyVSiP7uzzjucwtmmxeWFPlIs3FhFwP3nXwHxuMrV76TWj6lZqnKhOKi1z1FB8oE3yMASu9Dq4uQ6cZ6G1YPYTVfVi9C6u36qu9ejOv0f59-S3ZA2IAYv_ULDAcdv-j_QEau4Zf</recordid><startdate>2021</startdate><enddate>2021</enddate><creator>Shahnawaz, Md</creator><creator>Bilkis, Tahmina</creator><creator>Park, Il-Seon</creator><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QR</scope><scope>7T7</scope><scope>7TB</scope><scope>7U5</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</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>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope><orcidid>https://orcid.org/0000-0003-4754-6142</orcidid></search><sort><creationdate>2021</creationdate><title>Amyloid β cytotoxicity is enhanced or reduced depending on formation of amyloid β oligomeric forms</title><author>Shahnawaz, Md ; Bilkis, Tahmina ; Park, Il-Seon</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-d0d7ef670c96ea517a6e19c77cd48ebe2e3fdf45c5c77862858dec6b9dcf83483</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Alzheimer's disease</topic><topic>Amyloid</topic><topic>Applied Microbiology</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Cytotoxicity</topic><topic>DnaK protein</topic><topic>E coli</topic><topic>Life Sciences</topic><topic>Microbiology</topic><topic>Neurodegenerative diseases</topic><topic>Oligomers</topic><topic>Original Research Paper</topic><topic>Toxicity</topic><topic>Ultrastructure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shahnawaz, Md</creatorcontrib><creatorcontrib>Bilkis, Tahmina</creatorcontrib><creatorcontrib>Park, Il-Seon</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology 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>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</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 Engineering Collection</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Engineering Collection</collection><collection>ProQuest Central Basic</collection><jtitle>Biotechnology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shahnawaz, Md</au><au>Bilkis, Tahmina</au><au>Park, Il-Seon</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Amyloid β cytotoxicity is enhanced or reduced depending on formation of amyloid β oligomeric forms</atitle><jtitle>Biotechnology letters</jtitle><stitle>Biotechnol Lett</stitle><addtitle>Biotechnol Lett</addtitle><date>2021</date><risdate>2021</risdate><volume>43</volume><issue>1</issue><spage>165</spage><epage>175</epage><pages>165-175</pages><issn>0141-5492</issn><eissn>1573-6776</eissn><abstract>Objectives
We explored the underlying mechanisms that facilitate reducing and enhancing effects of exogenous proteins on cytotoxicity of amyloid β (Aβ), a main pathogen of Alzheimer’s disease, by using an
Escherichia coli
chaperonin DnaK.
Results
DnaK was chosen as a tool, because it, easily available and functionally stable, reduced or enhanced Aβ cytotoxicity depending on its concentration. Cytotoxicity was enhanced when the molar ratio of DnaK to Aβ42, at 20 μM Aβ42, was 0.01–0.5, while reduced cytotoxicity was observed at higher ratios (> 1) at 1 μM Aβ42. Significant amounts of oligomeric Aβ42 species accumulated concomitantly with enhanced cytotoxicity, whereas the oligomers appeared to form complexes with DnaK in conditions of reduced cytotoxicity.
Conclusions
The difference in cytotoxicity was due to variations in the toxic oligomeric Aβ species and DnaK is a useful tool for the study of the Aβ ultrastructure formation and toxicity of Aβ peptide.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>33025333</pmid><doi>10.1007/s10529-020-03015-8</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0003-4754-6142</orcidid></addata></record> |
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| subjects | Alzheimer's disease Amyloid Applied Microbiology Biochemistry Biomedical and Life Sciences Biotechnology Cytotoxicity DnaK protein E coli Life Sciences Microbiology Neurodegenerative diseases Oligomers Original Research Paper Toxicity Ultrastructure |
| title | Amyloid β cytotoxicity is enhanced or reduced depending on formation of amyloid β oligomeric forms |
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