Two distinct amyloid beta-protein (Abeta) assembly pathways leading to oligomers and fibrils identified by combined fluorescence correlation spectroscopy, morphology, and toxicity analyses.
Identifieur interne : 002417 ( Main/Exploration ); précédent : 002416; suivant : 002418Two distinct amyloid beta-protein (Abeta) assembly pathways leading to oligomers and fibrils identified by combined fluorescence correlation spectroscopy, morphology, and toxicity analyses.
Auteurs : Satoko Matsumura [Japon] ; Keiko Shinoda ; Mayumi Yamada ; Satoshi Yokojima ; Masafumi Inoue ; Takayuki Ohnishi ; Tetsuya Shimada ; Kazuya Kikuchi ; Dai Masui ; Shigeki Hashimoto ; Michio Sato ; Akane Ito ; Manami Akioka ; Shinsuke Takagi ; Yoshihiro Nakamura ; Kiyokazu Nemoto ; Yutaka Hasegawa ; Hisayoshi Takamoto ; Haruo Inoue ; Shinichiro Nakamura ; Yo-Ichi Nabeshima ; David B. Teplow ; Masataka Kinjo ; Minako HoshiSource :
- The Journal of biological chemistry [ 1083-351X ] ; 2011.
Descripteurs français
- KwdFr :
- Amyloïde (), Amyloïde (métabolisme), Amyloïde (pharmacologie), Amyloïde (ultrastructure), Animaux, Cellules cultivées, Humains, Maladie d'Alzheimer (métabolisme), Multimérisation de protéines, Peptides (), Peptides (métabolisme), Peptides (pharmacologie), Peptides bêta-amyloïdes (), Peptides bêta-amyloïdes (métabolisme), Peptides bêta-amyloïdes (pharmacologie), Rats.
- MESH :
- métabolisme : Amyloïde, Maladie d'Alzheimer, Peptides, Peptides bêta-amyloïdes.
- pharmacologie : Amyloïde, Peptides, Peptides bêta-amyloïdes.
- Amyloïde, Animaux, Cellules cultivées, Humains, Multimérisation de protéines, Peptides, Peptides bêta-amyloïdes, Rats.
English descriptors
- KwdEn :
- Alzheimer Disease (metabolism), Amyloid (chemistry), Amyloid (metabolism), Amyloid (pharmacology), Amyloid (ultrastructure), Amyloid beta-Peptides (chemistry), Amyloid beta-Peptides (metabolism), Amyloid beta-Peptides (pharmacology), Animals, Cells, Cultured, Humans, Peptides (chemistry), Peptides (metabolism), Peptides (pharmacology), Protein Multimerization, Rats.
- MESH :
- chemical , chemistry : Amyloid, Amyloid beta-Peptides, Peptides.
- metabolism : Alzheimer Disease, Amyloid, Amyloid beta-Peptides, Peptides.
- chemical , pharmacology : Amyloid, Amyloid beta-Peptides, Peptides.
- chemical , ultrastructure : Amyloid.
- Animals, Cells, Cultured, Humans, Protein Multimerization, Rats.
Abstract
Nonfibrillar assemblies of amyloid β-protein (Aβ) are considered to play primary roles in Alzheimer disease (AD). Elucidating the assembly pathways of these specific aggregates is essential for understanding disease pathogenesis and developing knowledge-based therapies. However, these assemblies cannot be monitored in vivo, and there has been no reliable in vitro monitoring method at low protein concentration. We have developed a highly sensitive in vitro monitoring method using fluorescence correlation spectroscopy (FCS) combined with transmission electron microscopy (TEM) and toxicity assays. Using Aβ labeled at the N terminus or Lys(16), we uncovered two distinct assembly pathways. One leads to highly toxic 10-15-nm spherical Aβ assemblies, termed amylospheroids (ASPDs). The other leads to fibrils. The first step in ASPD formation is trimerization. ASPDs of ∼330 kDa in mass form from these trimers after 5 h of slow rotation. Up to at least 24 h, ASPDs remain the dominant structures in assembly reactions. Neurotoxicity studies reveal that the most toxic ASPDs are ∼128 kDa (∼32-mers). In contrast, fibrillogenesis begins with dimer formation and then proceeds to formation of 15-40-nm spherical intermediates, from which fibrils originate after 15 h. Unlike ASPD formation, the Lys(16)-labeled peptide disturbed fibril formation because the Aβ(16-20) region is critical for this final step. These differences in the assembly pathways clearly indicated that ASPDs are not fibril precursors. The method we have developed should facilitate identifying Aβ assembly steps at which inhibition may be beneficial.
DOI: 10.1074/jbc.M110.181313
PubMed: 21292768
Affiliations:
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type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Shinoda, Keiko" sort="Shinoda, Keiko" uniqKey="Shinoda K" first="Keiko" last="Shinoda">Keiko Shinoda</name></author><author><name sortKey="Yamada, Mayumi" sort="Yamada, Mayumi" uniqKey="Yamada M" first="Mayumi" last="Yamada">Mayumi Yamada</name></author><author><name sortKey="Yokojima, Satoshi" sort="Yokojima, Satoshi" uniqKey="Yokojima S" first="Satoshi" last="Yokojima">Satoshi Yokojima</name></author><author><name sortKey="Inoue, Masafumi" sort="Inoue, Masafumi" uniqKey="Inoue M" first="Masafumi" last="Inoue">Masafumi Inoue</name></author><author><name sortKey="Ohnishi, Takayuki" sort="Ohnishi, Takayuki" uniqKey="Ohnishi T" first="Takayuki" last="Ohnishi">Takayuki Ohnishi</name></author><author><name sortKey="Shimada, Tetsuya" sort="Shimada, Tetsuya" uniqKey="Shimada T" first="Tetsuya" last="Shimada">Tetsuya Shimada</name></author><author><name sortKey="Kikuchi, Kazuya" sort="Kikuchi, Kazuya" uniqKey="Kikuchi K" first="Kazuya" last="Kikuchi">Kazuya Kikuchi</name></author><author><name sortKey="Masui, Dai" sort="Masui, Dai" uniqKey="Masui D" first="Dai" last="Masui">Dai Masui</name></author><author><name sortKey="Hashimoto, Shigeki" sort="Hashimoto, Shigeki" uniqKey="Hashimoto S" first="Shigeki" last="Hashimoto">Shigeki Hashimoto</name></author><author><name sortKey="Sato, Michio" sort="Sato, Michio" uniqKey="Sato M" first="Michio" last="Sato">Michio Sato</name></author><author><name sortKey="Ito, Akane" sort="Ito, Akane" uniqKey="Ito A" first="Akane" last="Ito">Akane Ito</name></author><author><name sortKey="Akioka, Manami" sort="Akioka, Manami" uniqKey="Akioka M" first="Manami" last="Akioka">Manami Akioka</name></author><author><name sortKey="Takagi, Shinsuke" sort="Takagi, Shinsuke" uniqKey="Takagi S" first="Shinsuke" last="Takagi">Shinsuke Takagi</name></author><author><name sortKey="Nakamura, Yoshihiro" sort="Nakamura, Yoshihiro" uniqKey="Nakamura Y" first="Yoshihiro" last="Nakamura">Yoshihiro Nakamura</name></author><author><name sortKey="Nemoto, Kiyokazu" sort="Nemoto, Kiyokazu" uniqKey="Nemoto K" first="Kiyokazu" last="Nemoto">Kiyokazu Nemoto</name></author><author><name sortKey="Hasegawa, Yutaka" sort="Hasegawa, Yutaka" uniqKey="Hasegawa Y" first="Yutaka" last="Hasegawa">Yutaka Hasegawa</name></author><author><name sortKey="Takamoto, Hisayoshi" sort="Takamoto, Hisayoshi" uniqKey="Takamoto H" first="Hisayoshi" last="Takamoto">Hisayoshi Takamoto</name></author><author><name sortKey="Inoue, Haruo" sort="Inoue, Haruo" uniqKey="Inoue H" first="Haruo" last="Inoue">Haruo Inoue</name></author><author><name sortKey="Nakamura, Shinichiro" sort="Nakamura, Shinichiro" uniqKey="Nakamura S" first="Shinichiro" last="Nakamura">Shinichiro Nakamura</name></author><author><name sortKey="Nabeshima, Yo Ichi" sort="Nabeshima, Yo Ichi" uniqKey="Nabeshima Y" first="Yo-Ichi" last="Nabeshima">Yo-Ichi Nabeshima</name></author><author><name sortKey="Teplow, David B" sort="Teplow, David B" uniqKey="Teplow D" first="David B" last="Teplow">David B. Teplow</name></author><author><name sortKey="Kinjo, Masataka" sort="Kinjo, Masataka" uniqKey="Kinjo M" first="Masataka" last="Kinjo">Masataka Kinjo</name></author><author><name sortKey="Hoshi, Minako" sort="Hoshi, Minako" uniqKey="Hoshi M" first="Minako" last="Hoshi">Minako Hoshi</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="eISSN">1083-351X</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alzheimer Disease (metabolism)</term><term>Amyloid (chemistry)</term><term>Amyloid (metabolism)</term><term>Amyloid (pharmacology)</term><term>Amyloid (ultrastructure)</term><term>Amyloid beta-Peptides (chemistry)</term><term>Amyloid beta-Peptides (metabolism)</term><term>Amyloid beta-Peptides (pharmacology)</term><term>Animals</term><term>Cells, Cultured</term><term>Humans</term><term>Peptides (chemistry)</term><term>Peptides (metabolism)</term><term>Peptides (pharmacology)</term><term>Protein Multimerization</term><term>Rats</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Amyloïde ()</term><term>Amyloïde (métabolisme)</term><term>Amyloïde (pharmacologie)</term><term>Amyloïde (ultrastructure)</term><term>Animaux</term><term>Cellules cultivées</term><term>Humains</term><term>Maladie d'Alzheimer (métabolisme)</term><term>Multimérisation de protéines</term><term>Peptides ()</term><term>Peptides (métabolisme)</term><term>Peptides (pharmacologie)</term><term>Peptides bêta-amyloïdes ()</term><term>Peptides bêta-amyloïdes (métabolisme)</term><term>Peptides bêta-amyloïdes (pharmacologie)</term><term>Rats</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amyloid</term><term>Amyloid beta-Peptides</term><term>Peptides</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Alzheimer Disease</term><term>Amyloid</term><term>Amyloid beta-Peptides</term><term>Peptides</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Amyloïde</term><term>Maladie d'Alzheimer</term><term>Peptides</term><term>Peptides bêta-amyloïdes</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Amyloïde</term><term>Peptides</term><term>Peptides bêta-amyloïdes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Amyloid</term><term>Amyloid beta-Peptides</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Amyloid</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cells, Cultured</term><term>Humans</term><term>Protein Multimerization</term><term>Rats</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Amyloïde</term><term>Animaux</term><term>Cellules cultivées</term><term>Humains</term><term>Multimérisation de protéines</term><term>Peptides</term><term>Peptides bêta-amyloïdes</term><term>Rats</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Nonfibrillar assemblies of amyloid β-protein (Aβ) are considered to play primary roles in Alzheimer disease (AD). Elucidating the assembly pathways of these specific aggregates is essential for understanding disease pathogenesis and developing knowledge-based therapies. However, these assemblies cannot be monitored in vivo, and there has been no reliable in vitro monitoring method at low protein concentration. We have developed a highly sensitive in vitro monitoring method using fluorescence correlation spectroscopy (FCS) combined with transmission electron microscopy (TEM) and toxicity assays. Using Aβ labeled at the N terminus or Lys(16), we uncovered two distinct assembly pathways. One leads to highly toxic 10-15-nm spherical Aβ assemblies, termed amylospheroids (ASPDs). The other leads to fibrils. The first step in ASPD formation is trimerization. ASPDs of ∼330 kDa in mass form from these trimers after 5 h of slow rotation. Up to at least 24 h, ASPDs remain the dominant structures in assembly reactions. Neurotoxicity studies reveal that the most toxic ASPDs are ∼128 kDa (∼32-mers). In contrast, fibrillogenesis begins with dimer formation and then proceeds to formation of 15-40-nm spherical intermediates, from which fibrils originate after 15 h. Unlike ASPD formation, the Lys(16)-labeled peptide disturbed fibril formation because the Aβ(16-20) region is critical for this final step. These differences in the assembly pathways clearly indicated that ASPDs are not fibril precursors. The method we have developed should facilitate identifying Aβ assembly steps at which inhibition may be beneficial.</div></front></TEI><affiliations><list><country><li>Japon</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement></list><tree><noCountry><name sortKey="Akioka, Manami" sort="Akioka, Manami" uniqKey="Akioka M" first="Manami" last="Akioka">Manami Akioka</name><name sortKey="Hasegawa, Yutaka" sort="Hasegawa, Yutaka" uniqKey="Hasegawa Y" first="Yutaka" last="Hasegawa">Yutaka Hasegawa</name><name sortKey="Hashimoto, Shigeki" sort="Hashimoto, Shigeki" uniqKey="Hashimoto S" first="Shigeki" last="Hashimoto">Shigeki Hashimoto</name><name sortKey="Hoshi, Minako" sort="Hoshi, Minako" uniqKey="Hoshi M" first="Minako" last="Hoshi">Minako Hoshi</name><name sortKey="Inoue, Haruo" sort="Inoue, Haruo" uniqKey="Inoue H" first="Haruo" last="Inoue">Haruo Inoue</name><name sortKey="Inoue, Masafumi" sort="Inoue, Masafumi" uniqKey="Inoue M" first="Masafumi" last="Inoue">Masafumi Inoue</name><name sortKey="Ito, Akane" sort="Ito, Akane" uniqKey="Ito A" first="Akane" last="Ito">Akane Ito</name><name sortKey="Kikuchi, Kazuya" sort="Kikuchi, Kazuya" uniqKey="Kikuchi K" first="Kazuya" last="Kikuchi">Kazuya Kikuchi</name><name sortKey="Kinjo, Masataka" sort="Kinjo, Masataka" uniqKey="Kinjo M" first="Masataka" last="Kinjo">Masataka Kinjo</name><name sortKey="Masui, Dai" sort="Masui, Dai" uniqKey="Masui D" first="Dai" last="Masui">Dai Masui</name><name sortKey="Nabeshima, Yo Ichi" sort="Nabeshima, Yo Ichi" uniqKey="Nabeshima Y" first="Yo-Ichi" last="Nabeshima">Yo-Ichi Nabeshima</name><name sortKey="Nakamura, Shinichiro" sort="Nakamura, Shinichiro" uniqKey="Nakamura S" first="Shinichiro" last="Nakamura">Shinichiro Nakamura</name><name sortKey="Nakamura, Yoshihiro" sort="Nakamura, Yoshihiro" uniqKey="Nakamura Y" first="Yoshihiro" last="Nakamura">Yoshihiro Nakamura</name><name sortKey="Nemoto, Kiyokazu" sort="Nemoto, Kiyokazu" uniqKey="Nemoto K" first="Kiyokazu" last="Nemoto">Kiyokazu Nemoto</name><name sortKey="Ohnishi, Takayuki" sort="Ohnishi, Takayuki" uniqKey="Ohnishi T" first="Takayuki" last="Ohnishi">Takayuki Ohnishi</name><name sortKey="Sato, Michio" sort="Sato, Michio" uniqKey="Sato M" first="Michio" last="Sato">Michio Sato</name><name sortKey="Shimada, Tetsuya" sort="Shimada, Tetsuya" uniqKey="Shimada T" first="Tetsuya" last="Shimada">Tetsuya Shimada</name><name sortKey="Shinoda, Keiko" sort="Shinoda, Keiko" uniqKey="Shinoda K" first="Keiko" last="Shinoda">Keiko Shinoda</name><name sortKey="Takagi, Shinsuke" sort="Takagi, Shinsuke" uniqKey="Takagi S" first="Shinsuke" last="Takagi">Shinsuke Takagi</name><name sortKey="Takamoto, Hisayoshi" sort="Takamoto, Hisayoshi" uniqKey="Takamoto H" first="Hisayoshi" last="Takamoto">Hisayoshi Takamoto</name><name sortKey="Teplow, David B" sort="Teplow, David B" uniqKey="Teplow D" first="David B" last="Teplow">David B. Teplow</name><name sortKey="Yamada, Mayumi" sort="Yamada, Mayumi" uniqKey="Yamada M" first="Mayumi" last="Yamada">Mayumi Yamada</name><name sortKey="Yokojima, Satoshi" sort="Yokojima, Satoshi" uniqKey="Yokojima S" first="Satoshi" last="Yokojima">Satoshi Yokojima</name></noCountry><country name="Japon"><region name="Région de Kantō"><name sortKey="Matsumura, Satoko" sort="Matsumura, Satoko" uniqKey="Matsumura S" first="Satoko" last="Matsumura">Satoko Matsumura</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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