Bag-1 proteins in oral squamous cell carcinoma

Wood, J; Lee, San San; Hague, Angela

doi:10.1016/j.oraloncology.2008.07.013

Cited by 12 publications

(10 citation statements)

References 76 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Nuclear Bag-1 was negatively correlated with lymphatic invasion and lymph node metastasis, whereas cytoplasmic Bag-1 correlated positively with invasive depth similar to the results obtained by analysis of Bag-1 mRNA. It has been documented that cytoplasmic expression is associated with metastasis of oral SCC to regional lymph nodes, consistent with the results of this study [6]. However, there are 2 reports showing that nuclear Bag-1 is more frequently expressed in distant metastatic cases of colorectal carcinoma and deeply invasive esophageal SCC [16,17].…”

Section: Discussionsupporting

confidence: 92%

“…Increasing evidence suggests that the biochemical events of apoptosis are controlled through the expression of many cellular proteins, including inducers (Bax, Bcl-Xs, Bad, Bak, and Bik) and inhibitors (Bcl-2, Bag-1, Bcl-XL, and Mcl-1) of cell death [6,24]. The current study demonstrated the distinct expression of Bag-1 protein isoforms in gastric carcinoma cell lines.…”

Section: Discussionsupporting

confidence: 55%

“…Bag-1 interacts with the adenosinetriphosphatase domain of heat shock protein (HSP70), leaving its peptide-binding domain available for further interactions with other protein substrates. The Bag-1 Cterminus also mediates interaction with the serine/threonine kinase Raf-1, which is normally activated by RAS to stimulate the mitogen-activated protein kinase signaling cascade, which is important for proliferation and survival [3][4][5][6]. Furthermore, several other proteins could interact with Bag-1, including heparin-binding epidermal growth factor (EGF)-like growth factor, hepatocyte growth factor receptor (HGF), platelet-derived growth factor receptor, the proteasome, the C-terminus of heat shock cognate protein (HSC) 70-interacting protein, and various hormone receptors, possibly mediated via the peptide binding activities of HSC70/HSP70 [3].…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Nuclear or cytoplasmic localization of Bag-1 distinctly correlates with pathologic behavior and outcome of gastric carcinomas

Zheng

Xing

et al. 2010

Human Pathology

View full text Add to dashboard Cite

Section: Discussionsupporting

confidence: 92%

Section: Discussionsupporting

confidence: 55%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Nuclear or cytoplasmic localization of Bag-1 distinctly correlates with pathologic behavior and outcome of gastric carcinomas

Zheng

Xing

et al. 2010

Human Pathology

View full text Add to dashboard Cite

“…Bcl-2-associated athanogene-1 (Bag-1) expression is deregulated in a variety of human tumours, including cancers of the breast, lung, colon, oesophagus, larynx, oral cavity and tongue (reviewed by Wood et al , 2009). The Bag-1 protein was first identified because of the interaction with Bcl-2, and was shown to enhance Bcl-2-mediated cell survival (Takayama et al , 1995).…”

mentioning

confidence: 99%

Co-overexpression of Bag-1 and heat shock protein 70 in human epidermal squamous cell carcinoma: Bag-1-mediated resistance to 5-fluorouracil-induced apoptosis

et al. 2011

View full text Add to dashboard Cite

Background:The aim was to determine whether Bcl-2-associated athanogene-1 (Bag-1) and/or its binding protein heat shock protein-70 (Hsp70) exhibit deregulated expression in epidermal squamous cell carcinoma (SCC) and whether Bag-1 confers apoptosis resistance.Method:Immunohistochemistry for Bag-1 and Hsp70 was performed on 60 epidermal SCC and 10 normal skin samples. The epidermal SCC cell line SCC-13 was treated with 5-fluorouracil (5-FU) after Bag-1 knockdown to determine whether high Bag-1 levels contribute to growth and/or apoptosis resistance.Results:Normal epithelium expressed primarily nuclear Bag-1. Most tumours showed reduced nuclear Bag-1 staining, but a subset exhibited strong Bag-1 staining, with cytoplasmic Bag-1 staining intensity correlating with cytoplasmic Hsp70 staining intensity (rs=0.462; P<0.001) and less differentiation (P<0.001). Bag-1 knockdown resulted in markedly reduced SCC-13 cell yield, increased spontaneous apoptosis and enhanced sensitivity to 5-FU-induced apoptosis. Apoptosis induced by 5-FU in the Bag-1-knockdown cells was significantly greater than the additive apoptotic effect of 5-FU or Bag-1 knockdown alone.Conclusions:Overexpression of Bag-1 and Hsp70 in poorly differentiated SCC may confer both enhanced tumour cell growth and apoptosis resistance. Bag-1 may contribute to the resistance of more advanced epidermal SCC to chemotherapy.

show abstract

“…In addition, BAG-1L, the only isoform that contains a nuclear localization signal, has transcriptional control functions as well (Gehring, 2009). In the last few years, many publications have shown the role of BAG-1 in cancer and its potential use as a prognostic indicator (Ni et al, 2013;Wood et al, 2009). However, little is known regarding a role in innate immunity.…”

Section: Bag-1 Is Necessary For the Effect Of Tnfa On Posttranslationmentioning

confidence: 99%

BAG-1M regulates keratin-associated Hsp70 chaperoning of aPKC in intestinal cells under inflammatory signaling

Mashukova

Kozhekbaeva

Forteza

et al. 2014

Journal of Cell Science

View full text Add to dashboard Cite

Atypical PKC (i/l and f; hereafter referred to as aPKC) is a key player in the acquisition of epithelial polarity and participates in other signaling cascades including the control of NF-kB signaling. This kinase is post-translationally regulated through Hsp70-mediated refolding. Previous work has shown that such a chaperoning activity is specifically localized to keratin intermediate filaments. Our work was performed with the goal of identifying the molecule(s) that block Hsp70 activity on keratin filaments during inflammation. A transcriptional screen allowed us to focus on BAG-1, a multifunctional protein that assists Hsp70 in nucleotide exchange but also blocks its activity at higher concentrations. We found the BAG-1 isoform BAG-1M upregulated threefold in human Caco-2 cells following stimulation with tumor necrosis factor receptor a (TNFa) to induce a pro-inflammatory response, and up to sixfold in mouse enterocytes following treatment with dextran sodium sulfate (DSS) to induce colitis. BAG-1M, but no other isoform, was found to copurify with intermediate filaments and block Hsp70 activity in the keratin fraction but not in the soluble fraction within the range of concentrations found in epithelial cells cultured under control and inflammation conditions. Constitutive expression of BAG-1M decreased levels of phosphorylated aPKC. By contrast, knockdown of BAG-1, blocked the TNFa-induced decrease of phosphorylated aPKC. We conclude that BAG-1M mediates Hsp70 inhibition downstream of NF-kB.

show abstract

Bag-1 proteins in oral squamous cell carcinoma

Cited by 12 publications

References 76 publications

Nuclear or cytoplasmic localization of Bag-1 distinctly correlates with pathologic behavior and outcome of gastric carcinomas

Nuclear or cytoplasmic localization of Bag-1 distinctly correlates with pathologic behavior and outcome of gastric carcinomas

Co-overexpression of Bag-1 and heat shock protein 70 in human epidermal squamous cell carcinoma: Bag-1-mediated resistance to 5-fluorouracil-induced apoptosis

BAG-1M regulates keratin-associated Hsp70 chaperoning of aPKC in intestinal cells under inflammatory signaling

Contact Info

Product

Resources

About