Activation of c-Jun N-terminal kinase antagonizes an anti-apoptotic action of Bcl-2
Jihyun Park, Injung Kim, Young Jun Oh, Ko Woon Lee, Pyung Lim Han, Eui Ju Choi
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.
Journal of Biological Chemistry
https://doi.org/10.1074/jbc.272.27.16725
Published - 1997 Jul 4
JNK Mitogen-Activated Protein Kinases
Cell death
Intracellular Membranes
Staurosporine
Park, J., Kim, I., Oh, Y. J., Lee, K. W., Han, P. L., & Choi, E. J. (1997). Activation of c-Jun N-terminal kinase antagonizes an anti-apoptotic action of Bcl-2. Journal of Biological Chemistry, 272(27), 16725-16728. https://doi.org/10.1074/jbc.272.27.16725
Activation of c-Jun N-terminal kinase antagonizes an anti-apoptotic action of Bcl-2. / Park, Jihyun; Kim, Injung; Oh, Young Jun; Lee, Ko Woon; Han, Pyung Lim; Choi, Eui Ju.
In: Journal of Biological Chemistry, Vol. 272, No. 27, 04.07.1997, p. 16725-16728.
Park, J, Kim, I, Oh, YJ, Lee, KW, Han, PL & Choi, EJ 1997, 'Activation of c-Jun N-terminal kinase antagonizes an anti-apoptotic action of Bcl-2', Journal of Biological Chemistry, vol. 272, no. 27, pp. 16725-16728. https://doi.org/10.1074/jbc.272.27.16725
Park J, Kim I, Oh YJ, Lee KW, Han PL, Choi EJ. Activation of c-Jun N-terminal kinase antagonizes an anti-apoptotic action of Bcl-2. Journal of Biological Chemistry. 1997 Jul 4;272(27):16725-16728. https://doi.org/10.1074/jbc.272.27.16725
Park, Jihyun ; Kim, Injung ; Oh, Young Jun ; Lee, Ko Woon ; Han, Pyung Lim ; Choi, Eui Ju. / Activation of c-Jun N-terminal kinase antagonizes an anti-apoptotic action of Bcl-2. In: Journal of Biological Chemistry. 1997 ; Vol. 272, No. 27. pp. 16725-16728.
@article{0a969c1d986e4f70bae6919e6319b727,
title = "Activation of c-Jun N-terminal kinase antagonizes an anti-apoptotic action of Bcl-2",
abstract = "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.",
author = "Jihyun Park and Injung Kim and Oh, {Young Jun} and Lee, {Ko Woon} and Han, {Pyung Lim} and Choi, {Eui Ju}",
doi = "10.1074/jbc.272.27.16725",
journal = "Journal of Biological Chemistry",
T1 - Activation of c-Jun N-terminal kinase antagonizes an anti-apoptotic action of Bcl-2
AU - Park, Jihyun
AU - Kim, Injung
AU - Oh, Young Jun
AU - Lee, Ko Woon
AU - Han, Pyung Lim
AU - Choi, Eui Ju
N2 - 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.
AB - 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.
U2 - 10.1074/jbc.272.27.16725
DO - 10.1074/jbc.272.27.16725
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
10.1074/jbc.272.27.16725