Park J, Kim I, Oh Y J, Lee K, Han P L, Choi E J
Cell Biology Laboratory, Hanhyo Institute of Technology, 461-6, Jeonmin-dong, Yuseong-ku, Taejon 305-390, Korea.
J Biol Chem. 1997 Jul 4;272(27):16725-8. doi: 10.1074/jbc.272.27.16725.
Bcl-2 is an intracellular membrane-associated protein that prevents cell death induced by a variety of apoptotic stimuli. A mechanism by which Bcl-2 exerts an anti-cell death effect is, however, not fully understood. In the present study, Bcl-2 suppressed cell death of N18TG neuroglioma cells caused by various apoptotic stresses, including etoposide, staurosporine, anisomycin, and ultraviolet irradiation. Concomitantly, Bcl-2 disrupted a signaling cascade to the c-Jun N-terminal kinase activation induced by the apoptotic stresses. Bcl-2 also prevented the etoposide-induced stimulation of MEKK1. Furthermore, overexpression of c-Jun N-terminal kinase antagonized the death-protective function of Bcl-2. These data suggest that suppression of the c-Jun N-terminal kinase signaling pathway may be critical for Bcl-2 action.
Bcl-2是一种细胞内与膜相关的蛋白质，可防止由多种凋亡刺激诱导的细胞死亡。然而，Bcl-2发挥抗细胞死亡作用的机制尚未完全阐明。在本研究中，Bcl-2抑制了由多种凋亡应激（包括依托泊苷、星形孢菌素、茴香霉素和紫外线照射）引起的N18TG神经胶质瘤细胞的死亡。同时，Bcl-2破坏了由凋亡应激诱导的c-Jun N端激酶激活的信号级联反应。Bcl-2还阻止了依托泊苷诱导的MEKK1刺激。此外，c-Jun N端激酶的过表达拮抗了Bcl-2的死亡保护功能。这些数据表明，抑制c-Jun N端激酶信号通路可能对Bcl-2的作用至关重要。
