Selected article for: "cell cell and proteolytic cleavage"
Author: Kim, Sang Chan; Park, Sook Jahr; Lee, Jong Rok; Seo, Jung Cheol; Yang, Chae Ha; Byun, Sung Hui
Title: Cytoprotective Activity of Glycyrrhizae radix Extract Against Arsenite-induced Cytotoxicity
  • Document date: 2007_3_25
    • ID: 0c5p8sjk_17
    Snippet: Caspase-3 is a key mediator of apoptosis and responsible for the proteolytic cleavage of many key proteins such as PARP. Activation of caspase-3 requires proteolytic processing of procaspase-3 into activated p17 and p12 fragments. To measure caspase-3 cleavage, H4IIE cells were pre-treated with licorice for 12 h, and then incubated with licorice with or without 400 mM of As for the next 12 h. The cells were washed with PBS and 0.5 ml of ice-cold .....
    Document: Caspase-3 is a key mediator of apoptosis and responsible for the proteolytic cleavage of many key proteins such as PARP. Activation of caspase-3 requires proteolytic processing of procaspase-3 into activated p17 and p12 fragments. To measure caspase-3 cleavage, H4IIE cells were pre-treated with licorice for 12 h, and then incubated with licorice with or without 400 mM of As for the next 12 h. The cells were washed with PBS and 0.5 ml of ice-cold cell lysis buffer (Cell signaling, MA, USA), after which 1 mM PMSF was added to each plate (100 mm) on ice. After 5 min, cells were scraped off the plate, sonicated on ice and microcentrifuged for 10 min at 4 C. The supernatant was collected and applied to cleaved caspase-3 sandwich ELISA kit (Cell signaling, MA, USA) according to the manufacturer's instructions.

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