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Han Y Kim Y Kang H Hong SH Kim YH Lim DS Park C Yun YS Song JY 《Apoptosis : an international journal on programmed cell death》2006,11(4):581-588
N-acetylphytosphingosine (NAPS), a sphingolipid derivative, is one of the well-known signal molecules that mediates various
cellular functions, including cell growth, differentiation, and apoptosis. In this study, we demonstrated that NAPS induces
apoptosis of Jurkat cells by activating Bak, but not Bax, which are both members of a proapoptotic subfamily of the Bcl-2
proteins. NAPS activated caspase-8 in a FADD-independent manner, but the lack of caspase-8 did not suppress the activation
of caspase-3 and -9 and cell death, indicating that caspase-8 activation does not play an important role in NAPS-induced cell
death. The overexpression of Bcl-xL, an anti-apoptotic protein, completely inhibited the activation of the caspases and apoptosis, assuming that NAPS-induced
apoptosis was initiated by the mitochondria. The expression levels of pro- and anti-apoptotic Bcl-2 family members were not
changed by the NAPS treatment. However, Bad was translocated from the cytosol into the mitochondria, where it bound to Bcl-xL, and Bak was dissociated from Bcl-xL and conformationally changed. Taken together, these findings indicate that NAPS induced apoptosis of Jurkat cells in a mitochondria-dependent
manner that was controlled by the translocation of Bad and the conformational change in Bak.
These authors contributed equally to this paper 相似文献
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