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3. Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates.

Author

Walsh, DM, Hartley, DM, Kusumoto, Y, Fezoui, Y, Condron, MM, Lomakin, A, Benedek, GB, Selkoe, DJ, and Teplow, DB

Subjects
Humans, Alzheimer Disease, Protein Structure, Secondary, Protein Folding, Dimerization, Amyloid beta-Peptides, Biochemistry & Molecular Biology, Biological Sciences, Medical and Health Sciences, Chemical Sciences
Abstract

Alzheimer's disease is characterized by extensive cerebral amyloid deposition. Amyloid deposits associated with damaged neuropil and blood vessels contain abundant fibrils formed by the amyloid beta-protein (Abeta). Fibrils, both in vitro and in vivo, are neurotoxic. For this reason, substantial effort has been expended to develop therapeutic approaches to control Abeta production and amyloidogenesis. Achievement of the latter goal is facilitated by a rigorous mechanistic understanding of the fibrillogenesis process. Recently, we discovered a novel intermediate in the pathway of Abeta fibril formation, the amyloid protofibril (Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., and Teplow, D. B. (1997) J. Biol. Chem. 272, 22364-22372). We report here results of studies of the assembly, structure, and biological activity of these polymers. We find that protofibrils: 1) are in equilibrium with low molecular weight Abeta (monomeric or dimeric); 2) have a secondary structure characteristic of amyloid fibrils; 3) appear as beaded chains in rotary shadowed preparations examined electron microscopically; 4) give rise to mature amyloid-like fibrils; and 5) affect the normal metabolism of cultured neurons. The implications of these results for the development of therapies for Alzheimer's disease and for our understanding of fibril assembly are discussed.

Published
1999

4. Temperature dependence of amyloid beta-protein fibrillization.

Author

Kusumoto, Y, Lomakin, A, Teplow, DB, and Benedek, GB

Subjects
Temperature, Kinetics, Light, Scattering, Radiation, Amyloid beta-Peptides
Abstract

Fibrillogenesis of the amyloid beta-protein (Abeta) is believed to play a central role in the pathogenesis of Alzheimer's disease. Previous studies of the kinetics of Abeta fibrillogenesis showed that the rate of fibril elongation is proportional to the concentration of monomers. We report here the study of the temperature dependence of the Abeta fibril elongation rate constant, ke, in 0.1 M HCl. The rate of fibril elongation was measured at Abeta monomer concentrations ranging from 50 to 400 microM and at temperatures from 4 degreesC to 40 degreesC. Over this temperature range, ke increases by two orders of magnitude. The temperature dependence of ke follows the Arrhenius law, ke = A exp (-EA/kT). The preexponential factor A and the activation energy EA are approximately 6 x 10(18) liter/(mol.sec) and 23 kcal/mol, respectively. Such a high value of EA suggests that significant conformational changes are associated with the binding of Abeta monomers to fibril ends.

Published
1998

9. Trends in Outcomes for Neonates Born Very Preterm and Very Low Birth Weight in 11 High-Income Countries

Author

Lui K, Lee S, Kusuda S, Adams M, Vento M, Reichman B, Darlow B, Lehtonen L, Modi N, Norman M, Hakansson S, Bassler D, Rusconi F, Lodha A, Yang J, Shah P, Marshall P, Schmidt P, Dhawan A, Craven P, de Waal K, Simmer K, Gill A, Pillow J, Stack J, Birch P, Cooke L, Casalaz D, Holberton J, Stewart A, Downe L, Stewart M, Bajuk B, Berry A, Hunt R, Kilburn C, De Paoli T, Bolisetty S, Paradisis M, Rieger I, Koorts P, Kuschel C, Doyle L, Numa A, Carlisle H, Badawi N, Loughran-Fowlds A, Koh G, Davis J, Luig M, Andersen C, Chambers G, Austin N, Lynn A, Edmonds L, Mildenhall L, Buksh M, Battin M, van den Boom J, Bourchier D, Richardson V, Dineen F, Rajadurai V, Lam S, Fung G, Harrison A, Synnes A, Cieslak Z, Sherlock R, Yee W, Aziz K, Fajardo C, Kalapesi Z, Sankaran K, Daspal S, Seshia M, Alvaro R, Mukerji A, Da Silva O, Nwaesei C, Lee K, Dunn M, Lemyre B, Dow K, Pelausa E, Barrington K, Drolet C, Piedboeuf B, Claveau M, Beltempo M, Bertelle V, Masse E, Canning R, Makary H, Ojah C, Monterrosa L, Deshpandey A, Afifi J, Kajetanowicz A, Andersson S, Tammela O, Sankilampi U, Saarela T, Prazad P, Noguchi A, McWan K, Button B, Stratton W, Hamvus A, Raghaven A, Derrick M, Hadley R, Covert R, Lablanc O, Weiss M, Bell A, Shareef M, Silvestri J, Heymann E, Zangen S, Smolkin T, Mimouni F, Bader D, Rothschild A, Strauss Z, Felszer C, Omari H, Tov-Friedman S, Bar-Oz B, Feldman M, Saad N, Flidel-Rimon O, Weisbrod M, Lubin D, Litmanovitz I, Kugelman A, Shinwell E, Klinger G, Nijim Y, Bin-Nun A, Golan A, Mandel D, Fleisher-Sheffer V, Kohelet D, Bakhrakh L, Hattori S, Shirai M, Ishioka T, Mori T, Amizuka T, Huchimukai T, Yoshida H, Sasaki A, Shimizu J, Nakamura T, Maruyama M, Matsumoto H, Hosokawa S, Taki A, Nakagawa M, Ko K, Uozumi A, Nakata S, Shimazaki A, Yoda T, Numata O, Imamura H, Kobayashi A, Tokuriki S, Uchida Y, Arai T, Ito M, Ieda K, Ono T, Hayashi M, Maki K, Yamakawa M, Kawai M, Fujii N, Shiomi K, Nozaki K, Wada H, Kim T, Tokunaga Y, Takatera A, Oshima T, Sumida H, Michinomae Y, Kusumoto Y, Yoshimoto S, Morisawa T, Ohashi T, Takahashi Y, Sugimoto M, Ono N, Miyagawa S, Saijo T, Yamagami T, Koyano K, Kobayashi S, Kanda T, Sakemi Y, Aoki M, Iida K, Goshi M, Maruyama Y, Avila-Alvarez A, Ting J, Toye J, Fernandez-Trisac J, Pico M, Seara M, Gutierrez A, Vizcaino C, Iglesias M, Zaplana H, Colomer B, Lopez J, Mozo R, Martinez M, Sebastian M, Carbonell M, Barnusell J, Puiggros M, Aloy J, Mussons F, Sanz I, Galiana G, Coroleu W, Iriondo M, Vilella L, Porta R, Demestre X, Nadal S, Martinez C, Cuesta M, Mora D, Tardio J, Benavente I, Alonso A, Olmos R, Cabezas M, Jimenez M, Caballero P, Diaz M, Fagundo A, Canals L, Rodrigo F, Marti L, Galdo M, Suazo J, Lopez E, Fernandez J, Altuna M, Muga O, Navarro D, Dominguez M, del Prado M, Diez I, Benavides M, Lapena S, Prada T, Mir E, Sanchez A, Vega E, del Prado N, Fernandez C, Vilaplana L, Perez I, Gomez L, Comeche L, Martin I, Armengod C, Labian C, Munoz M, Bravo D, Perez V, Fernandez M, Gonzalez C, Segura S, Azorin M, Jimenez A, Sanchez-Tamayo T, Moreno E, Gonzalez M, Martinez J, Garcia J, Orayen C, Gonzalez J, Albo M, Colmenero E, Gonzalez E, del Arco B, Gordillo L, Asensio M, Diaz C, Albujar R, Jorge P, Romero S, Falero M, Izquierdo A, Capell J, Vicente M, Caballero R, Euba A, Serna A, Goya J, Legorburu A, Amoros A, Isabel V, Gonzalez N, Gracia S, Faci P, Villagrasa M, Macian M, Kofron J, Brodd K, Odlind A, Alberg L, Arwehed S, Hafstrom O, Kasemo A, Nederman K, Ahman L, Ingemarsson F, Petersson H, Thurn P, Albinsson E, Selander B, Abrahamsson T, Heimdahl I, Sveinsdottir K, Wejryd E, Hedlund A, Soderberg M, Hallberg B, Brune T, Backstrom J, Robinson J, Farooqi A, Normann E, Fredriksson M, Palm A, Rosenqvist U, Walde B, Hagman C, Ohlin A, Florell R, Smedsaas-Lofvenberg A, Meyer P, Anderegg C, Schulzke S, Nelle M, Wagner B, Riedel T, Kaczala G, Pfister R, Tolsa J, Roth M, Stocker M, Laubscher B, Malzacher A, Micallef J, Hegi L, Arlettaz R, Bernet V, Fiorini P, Boldrini A, Tomasini B, Kefas J, Kamalanathan A, Jayachandran, Yoxall B, McBride T, Webb D, Garr R, Hassan A, Ambadkar P, Dyke M, McDevitt K, Rewitzky G, D'Amore A, Panasa N, Settle P, Maddock N, Edi-Osagie N, Zipitis C, Heal C, Birch J, Hasib A, Soe A, Kumar N, Kisat H, Vasu V, Lama M, Gupta R, Rawlingson C, Wickham T, Theron M, Kendall G, Gupta A, Aladangady N, Ali I, Alsford L, Lopez W, Murthy V, Sullivan C, Thomas M, Bate T, Godambe S, Watts T, Kuna J, Chang J, Pai V, Huddy C, Yasin S, Nicholl R, Pandey P, Cusack J, Kairamkonda V, Muogbo D, Harry L, Simmons P, Nycyk J, Gallagher A, Pillay T, Deshpande S, Mahadevan, Moore A, Clark S, Garbash M, Lal M, Abu-Harb M, Dani C, Mittal A, Allwood A, Selter M, Munyard P, Bartle D, Paul S, Whincup G, Mallik A, Amess P, Godden C, Reynolds P, Misra I, De Halpert P, Salgia S, Sanghavi R, Wigfield R, Deketelaere A, Khashu M, Hall M, Groves C, Brown N, Brennan N, Vamvakiti K, McIntyre J, Pirie S, Jones S, Mannix P, Cairns P, Eaton M, Schwarz K, Gibson D, Miall L, Krishnamurthy, and Int Network Evaluation Outcomes iN

Abstract

Objective To evaluate outcome trends of neonates born very preterm in 11 high-income countries participating in the International Network for Evaluating Outcomes of neonates. Study design In a retrospective cohort study, we included 154 233 neonates admitted to 529 neonatal units between January 1, 2007, and December 31, 2015, at 24(0/7) to 31(6/7) weeks of gestational age and birth weight

Published
2019

12. Thermal stability of Pt/Co multilayered films

Author

Sumi, S., Kusumoto, Y., Teragaki, Y., Torazawa, K., Tsunashima, S., and Uchiyama, S.

Subjects
Annealing -- Research, Thin films, Multilayered -- Research, Stability -- Research, Physics
Abstract

The thermal stability of PtCo multilayered thin films subjected to 400 degree celsius annealing treatments was investigated using vibrating sample magnetometry and x-ray diffraction. The results showed that annealing at temperatures greater than 300 degrees celsius caused the coercivity and hysteresis loops of films with glass or AlN substrates to deteriorate. On the other hand, samples with ZnO or Pt underlayers exhibited perfectly squared hysteresis loops even after being annealed at temperatures greater than 400 degrees celsius.

Published
1993

15. Amyloid β-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates

Author

Walsh, DM, Hartley, DM, Kusumoto, Y, Fezoui, Y, Condron, MM, Lomakin, A, Benedek, GB, Selkoe, DJ, and Teplow, DB

Subjects
macromolecular substances
Abstract

Alzheimer's disease is characterized by extensive cerebral amyloid deposition. Amyloid deposits associated with damaged neuropil and blood vessels contain abundant fibrils formed by the amyloid β-protein (Aβ). Fibrils, both in vitro and in vivo, are neurotoxic. For this reason, substantial effort has been expended to develop therapeutic approaches to control Aβ production and amyloidogenesis. Achievement of the latter goal is facilitated by a rigorous mechanistic understanding of the fibrillogenesis process. Recently, we discovered a novel intermediate in the pathway of Aβ fibril formation, the amyloid protofibril (Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., and Teplow, D. B. (1997) J. Biol Chem. 272, 22364-22372). We report here results of studies of the assembly, structure, and biological activity of these polymers. We find that protofibrils: 1) are in equilibrium with low molecular weight Aβ (monomeric or dimeric); 2) have a secondary structure characteristic of amyloid fibrils; 3) appear as beaded chains in rotary shadowed preparations examined electron microscopically; 4) give rise to mature amyloid-like fibrils; and 5) affect the normal metabolism of cultured neurons. The implications of these results for the development of therapies for Alzheimer's disease and for our understanding of fibril assembly are discussed.

Published
1999

36. A Comparative Performance Study of Plasmon-induced Charge Separation of Au@TiO2, Au@Fe2O3, and Au@ZnO Photocell Thin-films.

Author

Abdulla-Al-Mamun, M., Kusumoto, Y., and Islam, G. J.

Subjects
*GOLD nanoparticles, *CITRATES, *PLASMONS (Physics), *THIN films, *ELECTRODES
Abstract

The gold colloidal nanoparticles was prepared by citrate reduction from chloroauric acid (HAuCl4•4H2O). An ITO glass was coated with nanoporous TiO2, Fe2O3 and ZnO by squeegee method. The squeezing coated films were loaded with Au-nanoparticles by depositing technique. The film was characterized by UV-visible transmittance absorption spectroscopy, SEM, XRD, XPS, and EDX techniques. The Pt counter electrode was prepared by a magnetron sputter method on an ITO glass. The semiconductor with Auloaded film was used as a working electrode whereas Pt film was used as a counter electrode in a solar cell. The charge was separated by short circuit current and an open circuit voltage and the cell efficiency was measured by IPCE analyzer. The comparative photocurrent-performance of different semiconductors loaded with Au-nanoparticles was analysed. Au@TiO2, Au@Fe2O3, Au@ZnO were found to be suitable films for photo-current production having a good efficiency with Au@TiO2 as the best of the three. [ABSTRACT FROM AUTHOR]

Published
2013
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41. Hydrothermal Novel Synthesis of Neck-structured Hyperthermia-suitable Magnetic (Fe3O4, γ-Fe2O3 and α-Fe2O3) Nanoparticles.

Author

Islam, M. S., Kurawaki, J., Kusumoto, Y., Abdulla-Al-Mamun, M., and Mukhlish, M. Z. Bin

Subjects
MAGNETIC materials, FEVER, NANOPARTICLES, NANOSTRUCTURED materials, X-ray diffraction, FIELD emission, IRON oxides
Abstract

Novel neck-structured Fe3O4, γ-Fe2O3 and α-Fe2O3 magnetic nanoparticles were successfully prepared by a modified hydrothermal method. Ferrous chloride tetrahydrate was solely used as a precursor for the novel nanomaterials. The X-ray diffractometric study revealed the purity of the nanomaterials thus synthesized. All of the products were characterized using a field-emission scanning electron microscope (FE-SEM) and a transmission electron microscope (TEM) for the particle size and morphology. Neck-structured particle morphology was observed for the first time in all of iron oxides with magnetic properties. The particle size observed was 50--60 nm. The synthesized nanomaterials showed excellent magnetization values when magnetic hysteresis loops were measured using a superconducting quantum interference device (SQUID). Moreover, the as-prepared magnetic nanoparticles suspensions showed significant temperature increments under an AC (alternating current) magnetic-field induction condition at room temperature which indicates the hyperthermia feasibility. [ABSTRACT FROM AUTHOR]

Published
2012
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