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10.1016/j.bpj.2014.07.074

http://scihub22266oqcxt.onion/10.1016/j.bpj.2014.07.074
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C4190645!4190645!25296312
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suck abstract from ncbi


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pmid25296312      Biophys+J 2014 ; 107 (7): 1601-8
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  • Beta-Amyloid Oligomers Activate Apoptotic BAK Pore for Cytochrome c Release #MMPMID25296312
  • Kim J; Yang Y; Song S; Na JH; Oh K; Jeong C; Yu Y; Shin YK
  • Biophys J 2014[Oct]; 107 (7): 1601-8 PMID25296312show ga
  • In Alzheimer?s disease, cytochrome c-dependent apoptosis is a crucial pathway in neuronal cell death. Although beta-amyloid (A?) oligomers are known to be the neurotoxins responsible for neuronal cell death, the underlying mechanisms remain largely elusive. Here, we report that the oligomeric form of synthetic A? of 42 amino acids elicits death of HT-22 cells. But, when expression of a bcl-2 family protein BAK is suppressed by siRNA, A? oligomer-induced cell death was reduced. Furthermore, significant reduction of cytochrome c release was observed with mitochondria isolated from BAK siRNA-treated HT-22 cells. Our in vitro experiments demonstrate that A? oligomers bind to BAK on the membrane and induce apoptotic BAK pores and cytochrome c release. Thus, the results suggest that A? oligomers function as apoptotic ligands and hijack the intrinsic apoptotic pathway to cause unintended neuronal cell death.
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