Different Subcellular Distribution of Caspase-3 and Caspase-7 following Fas-induced Apoptosis in Mouse Liver

Following treatment of mice with an agonistic antiFas antibody to induce massive hepatocyte apoptosis, we demonstrate a distinct subcellular localization of the effector caspases-3 and -7

Julia M. Chandler; Gerald M. Cohen; Marion MacFarlane


Scholarcy highlights

  • Apoptosis is a crucial mechanism by which multicellular organisms control cell numbers and ensure the removal of damaged or potentially harmful cells
  • The protection conferred by Z-VAD.fmk suggested a critical role for the activation of caspases in Fasinduced apoptosis in vivo, consistent with previous studies
  • In order to confirm the involvement of caspases in Fas-mediated apoptosis in vivo, their activation was assessed by measuring DEVDase in crude liver homogenates from control and treated mice
  • Treatment with the agonistic Fas antibody resulted in a marked increase in total liver DEVDase after 4 h in comparison with that in controls. These results demonstrated the activation of the effector caspase-3 and/or caspase-7 in Fas-induced apoptosis in vivo in agreement with in vitro studies, which have shown the activation of these caspases following treatment of cells with Fas or tumor necrosis factor
  • In order to further dissect the role of caspases in Fas-induced apoptosis in vivo, we examined DEVDase and caspase processing in subcellular liver fractions prepared from control and Fas-treated mice
  • We examined the fate of sterol regulatory element-binding protein 1, one of the few endoplasmic reticulum-associated proteins known to be cleaved in apoptosis
  • We have clearly shown that following Fas-induced apoptosis in vivo, active caspase-3 was located primarily in the cytosol, whereas active caspase-7 was associated with both the mitochondrial and microsomal fractions

Need more features? Save interactive summary cards to your Scholarcy Library.