p52-independent nuclear translocation of RelB promotes LPS-induced attachment
- Laboratory of Immunology, National Institute on Aging, NIH Biomedical Research Center, Baltimore, MD 21224 (United States)
The NF-{kappa}B signaling pathways have a critical role in the development and progression of various cancers. In this study, we demonstrated that the small cell lung cancer cell line (SCLC) H69 expressed a unique NF-{kappa}B profile as compared to other cancer cell lines. The p105/p50, p100/p52, c-Rel, and RelB protein and mRNA transcripts were absent in H69 cells but these cells expressed RelA/p65. The activation of H69 cells by lipopolysaccharide (LPS) resulted in the induction of RelB and p100 expression. The treatment also induced the nuclear translocation of RelB without the processing of p100 to p52. Furthermore, LPS-induced {beta}1 integrin expression and cellular attachment through an NF-{kappa}B-dependent mechanism. Blocking RelB expression prevented the increase in the expression of {beta}1 integrin and the attachment of H69. Taken together, the results suggest that RelB was responsible for the LPS-mediated attachment and may play an important role in the progression of some cancers.
- OSTI ID:
- 22199963
- Journal Information:
- Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 1 Vol. 391; ISSN 0006-291X; ISSN BBRCA9
- Country of Publication:
- United States
- Language:
- English
Similar Records
Zinc-finger protein 91 plays a key role in LIGHT-induced activation of non-canonical NF-{kappa}B pathway
p100, a precursor of NF-κB2, inhibits c-Rel and reduces the expression of IL-23 in dendritic cells