NDLI: Formation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells

Content Provider	PubMed Central
Author	Mukai, Hideyuki Isagawa, Takayuki Goyama, Emiko Tanaka, Shuhei Bence, Neil F. Tamura, Atsuo Ono, Yoshitaka Kopito, Ron R.
Copyright Year	2005
Abstract	Huntington's disease is a progressive neurodegenerative disorder caused by a polyglutamine repeat expansion in the first exon of the huntingtin (Htt) protein. N-terminal Htt peptides with polyglutamine tracts in the pathological range (51–122 glutamines) form high-molecular-weight protein aggregates with fibrillar morphology in vitro, and they form discrete inclusion bodies in a cell-culture model. However, in some studies, formation of discrete Htt inclusions does not correlate well with cell death. We coexpressed N-terminal Htt fragments containing 91 glutamines fused to different affinity tags in HEK293 cells, and we isolated small aggregates by double sequential-affinity chromatography to assure the isolation of multimeric molecules. Transmission electron microscopy and atomic force microscopy revealed the isolated aggregates as globules or clusters of globules 4–50 nm in diameter without any detectable fibrillar species. Because small nonfibrillar oligomers, not mature fibrils, recently have been suggested to be the principal cytotoxic species in neurodegenerative disease, these Htt globular aggregates formed in cells may represent the pathogenic form of mutant Htt.
Related Links	http://dx.doi.org/10.1073/pnas.0409283102
Ending Page	10892
Page Count	6
Starting Page	10887
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	31
Volume Number	102
Language	English
Publisher	National Academy of Sciences
Publisher Date	2005-08-02
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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