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Lysosomal Vesiculosis

Comparing with the pathological hallmark ‘granulo-vacuolar degenerations’ in Alzheimer’s disease, the postischemic monkey neurons were carefully observed with microscope. Intriguingly, we found very similar change, and identified it as ‘lysosomal vesiculosis’ by electron microscopy. However, the exact molecular and structural impacts of the Hsp70.1 disorder upon the lysosomal membrane are hardly elucidated in the human brain because of the practical and ethical problems. Accordingly, using the monkey brain tissues after in-vivo and in-vitro oxidative stresses, we studied molecular modifications of Hsp70.1 and its counterpart bis(monoacylglycero) phosphate (BMP), because these molecules are closely related to the lysosomal membrane stability by regulating acid sphingomyelinase. The aim of this study is to analyze influence of calpain activation and oxidative stress on the development of lysosomal vesiculosis, with particular attentions to Hsp70.1 and BMP. Since lysosomal vesiculosis was identified in neurons of both ischemic monkey and human Alzheimer neurons, it is suggested that a decreased lysosomal catabolism of membrane phospholipid might be a factor causing lysosomal destabilization. The aim of this study is to analyze influence of calpain activation and oxidative stress on the development of lysosomal vesiculosis, with particular attentions to Hsp70.1 and BMP. Since lysosomal vesiculosis was identified in neurons of both ischemic monkey and human Alzheimer neurons, it is suggested that a decreased lysosomal catabolism of membrane phospholipid might be a factor causing lysosomal destabilization. Tetsumori Yamashima, Calpain-Mediated Hsp70.1 Cleavage in Monkey CA1 after Ischemia Induces Similar ‘Lysosomal Vesiculosis’ to Alzheimer Neurons
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Last date updated on July, 2014

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