Familial Alzheimer's disease mutations inhibit gamma-secretase-mediated liberation of beta-amyloid precursor protein carboxy-terminal fragment. - AlzForum Alzheimer Research Paper of the Week


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Home: Papers of the Week

Annotation

	Wiley JC, Hudson M, Kanning KC, Schecterson LC, Bothwell M. Familial Alzheimer's disease mutations inhibit gamma-secretase-mediated liberation of beta-amyloid precursor protein carboxy-terminal fragment. J Neurochem. 2005 Sep;94(5):1189-201. PubMed Abstract, View on AlzSWAN

	Comments on Paper and Primary News

	Comment by: Tommaso Russo, ARF Advisor
	Submitted 11 July 2005 \| Permalink	Posted 13 July 2005
	I recommend this paper

	Comment by: Takaomi Saido, ARF Advisor
	Submitted 9 July 2005 \| Permalink	Posted 13 July 2005
	I recommend this paper

	Comment by: Nikolaos K. Robakis
	Submitted 13 July 2005 \| Permalink	Posted 14 July 2005
	I recommend this paper FAD mutations inhibit cleavage at the ε site of many PS/γ-secretase substrates. Inhibition at the ε site is predicted to increase cleavage at the γ site, thus increasing Aβ production. This paper offers experimental evidence for this concept. View all comments by Nikolaos K. Robakis

	Comment by: Rachael Neve
	Submitted 12 July 2005 \| Permalink	Posted 14 July 2005
	I recommend this paper This very interesting article presents data to support the idea that both class II FAD APP mutations and FAD PS1 mutations not only increase levels of Aβ, but also decrease the level of AICD, called CTFγ by the authors. An extremely elegant genetic technique is used to reliably detect this labile fragment. The findings presented in this paper suggest that not only increased Aβ, but also decreased AICD (which normally regulates signaling and transcription) may contribute to the pathology caused by these mutants. View all comments by Rachael Neve

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REAGENTS/MATERIAL:

Western blots were probed with rabbit anti-Gal4 DNA binding domain antibody (Zymed, San Francisco, CA, or US Biologicals, Swampscott, MA).

b-amyloid sandwich ELISA assays were performed by coating 96-well Nunc MaxiSorp plates with the 6E10 capture antibody (Signet Laboratories, Dedham, MA, USA) generated against the amino-terminal region of the Ab peptide. The biotinylated secondary antibodies were either the Ab40-or the Ab42-specific.




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