Trace amounts of pyroglutaminated Aβ-(3-42) enhance aggregation of Aβ-(1-42) on neuronal membranes at physiological concentrations: FCS analysis of cell surface.
Identifieur interne : 000A01 ( PubMed/Corpus ); précédent : 000A00; suivant : 000A02Trace amounts of pyroglutaminated Aβ-(3-42) enhance aggregation of Aβ-(1-42) on neuronal membranes at physiological concentrations: FCS analysis of cell surface.
Auteurs : Yoshiaki Yano ; An Takeno ; Katsumi MatsuzakiSource :
- Biochimica et biophysica acta. Biomembranes [ 0005-2736 ] ; 2018.
Abstract
Minor species of amyloid β-peptide (Aβ), such as Aβ-(1-43) and pyroglutaminated Aβ-(3-42) (Aβ-(3pE-42)), have been suggested to be involved in the initiation of the Aβ aggregation process, which is closely associated with the etiology of Alzheimer's disease. They can play important roles in aggregation not only in the aqueous phase but also on neuroral membranes; however, the latter behaviors remain mostly unexplored. Here, initial aggregation processes of Aβ on living cells were monitored at physiological nanomolar concentrations by fluorescence correlation spectroscopy. Membrane-bound Aβ-(1-42) and Aβ-(1-40) formed oligomers composed of ~4 Aβ molecules during 48-h incubation, whereas the peptides remained monomeric in the culture medium, indicating that the membranes facilitated Aβ aggregation. The presence of 5 mol% Aβ-(3pE-42), but not Aβ-(1-43), significantly enhanced the aggregation of Aβ-(1-42) up to ~10-mers. On the other hand, neither trace amounts of Aβ-(1-42) nor Aβ-(3pE-42) enhanced the aggregation of Aβ-(1-40). The observed small Aβ oligomers are expected to act as pathogenic seeds for amyloid fibrils responsible for neurotoxicity. This article is part of a Special Issue entitled: Protein Aggregation and Misfolding at the Cell Membrane Interface edited by Ayyalusamy Ramamoorthy.
DOI: 10.1016/j.bbamem.2018.01.023
PubMed: 29410161
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Electronic address: mkatsumi@pharm.kyoto-u.ac.jp.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2018">2018</date><idno type="RBID">pubmed:29410161</idno><idno type="pmid">29410161</idno><idno type="doi">10.1016/j.bbamem.2018.01.023</idno><idno type="wicri:Area/PubMed/Corpus">000A01</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000A01</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Trace amounts of pyroglutaminated Aβ-(3-42) enhance aggregation of Aβ-(1-42) on neuronal membranes at physiological concentrations: FCS analysis of cell surface.</title><author><name sortKey="Yano, Yoshiaki" sort="Yano, Yoshiaki" uniqKey="Yano Y" first="Yoshiaki" last="Yano">Yoshiaki Yano</name><affiliation><nlm:affiliation>Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Takeno, An" sort="Takeno, An" uniqKey="Takeno A" first="An" last="Takeno">An Takeno</name><affiliation><nlm:affiliation>Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Matsuzaki, Katsumi" sort="Matsuzaki, Katsumi" uniqKey="Matsuzaki K" first="Katsumi" last="Matsuzaki">Katsumi Matsuzaki</name><affiliation><nlm:affiliation>Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan. Electronic address: mkatsumi@pharm.kyoto-u.ac.jp.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Biochimica et biophysica acta. Biomembranes</title><idno type="ISSN">0005-2736</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Minor species of amyloid β-peptide (Aβ), such as Aβ-(1-43) and pyroglutaminated Aβ-(3-42) (Aβ-(3pE-42)), have been suggested to be involved in the initiation of the Aβ aggregation process, which is closely associated with the etiology of Alzheimer's disease. They can play important roles in aggregation not only in the aqueous phase but also on neuroral membranes; however, the latter behaviors remain mostly unexplored. Here, initial aggregation processes of Aβ on living cells were monitored at physiological nanomolar concentrations by fluorescence correlation spectroscopy. Membrane-bound Aβ-(1-42) and Aβ-(1-40) formed oligomers composed of ~4 Aβ molecules during 48-h incubation, whereas the peptides remained monomeric in the culture medium, indicating that the membranes facilitated Aβ aggregation. The presence of 5 mol% Aβ-(3pE-42), but not Aβ-(1-43), significantly enhanced the aggregation of Aβ-(1-42) up to ~10-mers. On the other hand, neither trace amounts of Aβ-(1-42) nor Aβ-(3pE-42) enhanced the aggregation of Aβ-(1-40). The observed small Aβ oligomers are expected to act as pathogenic seeds for amyloid fibrils responsible for neurotoxicity. This article is part of a Special Issue entitled: Protein Aggregation and Misfolding at the Cell Membrane Interface edited by Ayyalusamy Ramamoorthy.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">29410161</PMID><DateRevised><Year>2019</Year><Month>11</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0005-2736</ISSN><JournalIssue CitedMedium="Print"><PubDate><Year>2018</Year><Month>Feb</Month><Day>02</Day></PubDate></JournalIssue><Title>Biochimica et biophysica acta. Biomembranes</Title><ISOAbbreviation>Biochim Biophys Acta Biomembr</ISOAbbreviation></Journal><ArticleTitle>Trace amounts of pyroglutaminated Aβ-(3-42) enhance aggregation of Aβ-(1-42) on neuronal membranes at physiological concentrations: FCS analysis of cell surface.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">S0005-2736(18)30038-5</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbamem.2018.01.023</ELocationID><Abstract><AbstractText>Minor species of amyloid β-peptide (Aβ), such as Aβ-(1-43) and pyroglutaminated Aβ-(3-42) (Aβ-(3pE-42)), have been suggested to be involved in the initiation of the Aβ aggregation process, which is closely associated with the etiology of Alzheimer's disease. They can play important roles in aggregation not only in the aqueous phase but also on neuroral membranes; however, the latter behaviors remain mostly unexplored. Here, initial aggregation processes of Aβ on living cells were monitored at physiological nanomolar concentrations by fluorescence correlation spectroscopy. Membrane-bound Aβ-(1-42) and Aβ-(1-40) formed oligomers composed of ~4 Aβ molecules during 48-h incubation, whereas the peptides remained monomeric in the culture medium, indicating that the membranes facilitated Aβ aggregation. The presence of 5 mol% Aβ-(3pE-42), but not Aβ-(1-43), significantly enhanced the aggregation of Aβ-(1-42) up to ~10-mers. On the other hand, neither trace amounts of Aβ-(1-42) nor Aβ-(3pE-42) enhanced the aggregation of Aβ-(1-40). The observed small Aβ oligomers are expected to act as pathogenic seeds for amyloid fibrils responsible for neurotoxicity. This article is part of a Special Issue entitled: Protein Aggregation and Misfolding at the Cell Membrane Interface edited by Ayyalusamy Ramamoorthy.</AbstractText><CopyrightInformation>Copyright © 2018 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yano</LastName><ForeName>Yoshiaki</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Takeno</LastName><ForeName>An</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Matsuzaki</LastName><ForeName>Katsumi</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan. 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