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STAT3-mediated transcription of Bcl-2, Mcl-1 and c-IAP2 prevents apoptosis in polyamine-depleted cells
Open accessAbstract
Activation of STAT3 (signal transducer and activator of transcription 3) plays a crucial role in cell survival and proliferation. The aim of the present study was to clarify the role of STAT3 signalling in the protection of polyamine-depleted intestinal epithelial cells against TNF-α (tumour necrosis factor-α)-induced apoptosis. Polyamine depletion by DFMO (α-difluoromethylornithine) caused phosphorylation of STAT3 at Tyr-705 and Ser-727. Phospho-Tyr-705 STAT3 was immunolocalized at the cell periphery and nucleus, whereas phospho-Ser-727 STAT3 was predominantly detected in the nucleus of polyamine-depleted cells. Sustained phosphorylation of STAT3 at tyrosine residues was observed in polyamine-depleted cells after exposure to TNF-α. Inhibition of STAT3 activation by AG490 or cell-membrane-permeant inhibitory peptide (PpYLKTK; where pY represents phospho-Tyr) increased the sensitivity of polyamine-depleted cells to apoptosis. Expression of DN-STAT3 (dominant negative-STAT3) completely eliminated the protective effect of DFMO against TNF-α-induced apoptosis. Polyamine depletion increased mRNA and protein levels for Bcl-2, Mcl-1 (myeloid cell leukaemia-1) and c-IAP2 (inhibitor of apoptosis protein-2). Significantly higher levels of Bcl-2 and c-IAP2 proteins were observed in polyamine-depleted cells before and after 9 h of TNF-α treatment. Inhibition of STAT3 by AG490 and DN-STAT3 decreased Bcl-2 promoter activity. DN-STAT3 decreased mRNA and protein levels for Bcl-2, Mcl-1 and c-IAP2 in polyamine-depleted cells. siRNA (small interfering RNA)-mediated inhibition of Bcl-2, Mcl-1 and c-IAP2 protein levels increased TNF-α-induced apoptosis. DN-STAT3 induced the activation of caspase-3 and PARP [poly(ADP-ribose) polymerase] cleavage in polyamine-depleted cells. These results suggest that activation of STAT3 in response to polyamine depletion increases the transcription and subsequent expression of anti-apoptotic Bcl-2 and IAP family proteins and thereby promotes survival of cells against TNF-α-induced apoptosis.
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Cited by
Na, H.-K., & Surh, Y.-J. (2008) · Food and Chemical Toxicology · doi:10.1016/j.fct.2007.10.006 · Cited by 485
AGGARWAL, B. B., SETHI, G., AHN, K. S., SANDUR, S. K., PANDEY, M. K., KUNNUMAKKARA, A. B., SUNG, B., & ICHIKAWA, H. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1378.063 · Cited by 398
Qu, Y., Zhang, Q., Cai, X., Li, F., Ma, Z., Xu, M., & Lu, L. (2017) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13170 · Cited by 389
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Gaudino, S. J., & Kumar, P. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00360 · Cited by 298
Metadata
- Authors
- Bhattacharya, S., Ray, R. M., & Johnson, L. R.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2005-11-22
- Volume
- 392
- Issue
- 2
- Pages
- 335-344
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1987388371
- Cited by
- 291
- References
- 4
- FWCI
- 3.82
- Type
- journal article
- Language
- en
- Open access
- bronze
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