Involvement of diacylglycerol produced by phospholipase D activation in Aβ-induced reduction of sAPPα secretion in SH-SY5Y neuroblastoma cells.
作者： Fuminori Tanabe , Tomoko Nakajima , Masahiko Ito
DOI: 10.1016/J.BBRC.2014.03.038
关键词:
摘要: Abstract We previously reported that the thiol proteinase inhibitor, E-64-d, ameliorated amyloid β (Aβ)-induced reduction of soluble precursor protein α (sAPPα) secretion by reversing ceramide-induced kinase C down-regulation in SH-SY5Y neuroblastoma cells. In present study, we showed Aβ (1–42) peptide enhanced diacylglycerol (DAG) production phospholipase D (PLD) activation these subsequently examined whether PLD was involved Aβ-induced sAPPα and 2 μM CAY10593, which selectively inhibits PLD2, secretion, whereas 50 nM PLD1, did not. Moreover, 50 µM propranolol, a phosphatidic acid phosphohydrolase also suggesting DAG may be responsible for sAPPα. affects analog reduced addition, ceramide stimulating neutral sphingomyelinase (N-SMase) activity. demonstrated stimulates N-SMase activity Here, inhibition PLD2 CAY10593 suppressed activation. Taken together, results suggest produced through pathway is
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