کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1933068 1050600 2009 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Mechanism of cytotoxicity mediated by the C31 fragment of the amyloid precursor protein
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Mechanism of cytotoxicity mediated by the C31 fragment of the amyloid precursor protein
چکیده انگلیسی

The cytoplasmic tail of the amyloid precursor protein (APP) contains two putatively cytotoxic peptides, Jcasp and C31, derived by caspase cleavage of APP. Jcasp is a fragment starting from the ε-secretase site to position 664, while C31 is a fragment from position 665 to the C-terminus. Our studies now showed that compared to C31, Jcasp appeared to play a minor role in cytotoxicity. In particular, inhibition of Jcasp generation by treatment of γ-secretase inhibitor did not lead to any attenuation of C31-induced toxicity. Secondly, because C31 toxicity is largely absent in cells lacking endogenous APP, we determined, using a split β-galactosidase complementary assay to monitor protein–protein interactions, the presence of APP associated complexes. Our results demonstrated that both APP homomeric and C31/APP heteromeric complexes were correlated with cell death, indicating that C31 complexes with APP to recruit the interacting partners that initiate the signals related to cellular toxicity.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 388, Issue 2, 16 October 2009, Pages 450–455
نویسندگان
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