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J. Biol. Chem., Vol. 279, Issue 35, 37061-37068, August 27, 2004

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 279/35/37061    most recent M403672200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Liao, L. Articles by Peng, J. Search for Related Content PubMed PubMed Citation Articles by Liao, L. Articles by Peng, J. Social Bookmarking                      What's this?

Proteomic Characterization of Postmortem Amyloid Plaques Isolated by Laser Capture Microdissection^*

Lujian Liao, Dongmei Cheng, Jian Wang, Duc M. Duong, Tatyana G. Losik, Marla Gearing¶, Howard D. Rees||, James J. Lah||, Allan I. Levey||, and Junmin Peng**

From the Department of Human Genetics, Center for Neurodegenerative Disease, the ^¶Department of Pathology and Laboratory Medicine, and the ^||Department of Neurology, Emory University School of Medicine, Atlanta, Georgia 30322

The presence of amyloid plaques in the brain is one of the pathological hallmarks of Alzheimer's disease (AD). We report here a comprehensive proteomic analysis of senile plaques from postmortem AD brain tissues. Senile plaques labeled with thioflavin-S were procured by laser capture microdissection, and their protein components were analyzed by liquid chromatography coupled with tandem mass spectrometry. We identified a total of 488 proteins coisolated with the plaques, and we found multiple phosphorylation sites on the neurofilament intermediate chain, implicating the complexity and diversity of cellular processes involved in the plaque formation. More significantly, we identified 26 proteins enriched in the plaques of two AD cases by quantitative comparison with surrounding non-plaque tissues. The localization of several proteins in the plaques was further confirmed by the approach of immunohistochemistry. In addition to previously identified plaque constituents, we discovered novel association of dynein heavy chain with the plaques in human postmortem brain and in a double transgenic AD mouse model, suggesting that neuronal transport may play a role in neuritic degeneration. Overall, our results revealed for the first time the sub-proteome of amyloid plaques that is important for further studies on disease biomarker identification and molecular mechanisms of AD pathogenesis.

Received for publication, April 2, 2004 , and in revised form, June 24, 2004.

^* 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 Table S1.

^** To whom correspondence should be addressed. E-mail: jpeng{at}genetics.emory.edu.

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