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J. Biol. Chem., Vol. 281, Issue 44, 33677-33683, November 3, 2006

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Real-time and Single Fibril Observation of the Formation of Amyloid Spherulitic Structures^*

Tadato Ban¹, Kenichi Morigaki, Hisashi Yagi, Takashi Kawasaki, Atsuko Kobayashi, Shunsuke Yuba, Hironobu Naiki^¶, and Yuji Goto²

From the Institute for Protein Research, Osaka University, and CREST, Japan Science and Technology Agency, Yamadaoka 3-2, Suita, Osaka 565-0871, the National Institute of Advanced Industrial Science and Technology, Research Institute for Cell Engineering, Midorigaoka 1-8-31, Ikeda, Osaka 563-8577, and the ^¶Department of Pathological Sciences, Faculty of Medical Sciences, University of Fukui and CREST, Japan Science and Technology Agency, Matsuoka, Fukui 910-1193, Japan

In Alzheimer disease, amyloid , a 39-43-residue peptide produced by cleavage from a large amyloid precursor protein, undergoes conformational change to form amyloid fibrils and deposits as senile amyloid plaques in the extracellular cerebral cortices of the brain. However, the mechanism of how the intrinsically linear amyloid fibrils form spherical senile plaques is unknown. With total internal reflection fluorescence microscopy combined with the use of thioflavin T, an amyloid-specific fluorescence dye, we succeeded in observing the formation of the senile plaque-like spherulitic structures with diameters of around 15 µm on the chemically modified quartz surface. Real-time observation at a single fibrillar level revealed that, in the absence of tight contact with the surface, the cooperative and radial growth of amyloid fibrils from the core leads to a huge spherulitic structure. The results suggest the underlying physicochemical mechanism of senile plaque formation, essential for obtaining insight into prevention of Alzheimer disease.

Received for publication, June 26, 2006 , and in revised form, August 24, 2006.

^* This work was supported by grants from the Takeda Science Foundation and by Grant-in-Aid 40153770 from the Japanese Ministry of Education, Culture, Sports, Science and Technology on Priority Areas. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement"in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains three supplemental figures, two supplemental references, and two movies.

¹ A recipient of a Japan Society for Promotion of Science (JSPS) Post Doctoral Fellowship.

² To whom correspondence should be addressed. Fax: 81-6-6879-8616; E-mail: ygoto{at}protein.osaka-u.ac.jp.

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				D. Ozawa, H. Yagi, T. Ban, A. Kameda, T. Kawakami, H. Naiki, and Y. Goto Destruction of Amyloid Fibrils of a {beta}2-Microglobulin Fragment by Laser Beam Irradiation J. Biol. Chem., January 9, 2009; 284(2): 1009 - 1017. [Abstract] [Full Text] [PDF]