scholarly journals Co-expression of fatty acid synthase and caveolin-1 in pancreatic ductal adenocarcinoma: Implications for tumor progression and clinical outcome

Cell Cycle ◽  
2008 ◽  
Vol 7 (19) ◽  
pp. 3021-3025 ◽  
Author(s):  
Agnieszka K. Witkiewicz ◽  
Katherine Nguyen ◽  
Abhijit Dasgupta ◽  
Eugene P. Kennedy ◽  
Charles J. Yeo ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Clinical Outcome ◽  
Tumor Progression ◽  
Pancreatic Ductal Adenocarcinoma ◽  
Fatty Acid Synthase ◽  
Ductal Adenocarcinoma ◽  
Caveolin 1

scholarly journals LINC00842 inactivates transcription co-regulator PGC-1α to promote pancreatic cancer malignancy through metabolic remodelling

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Xudong Huang ◽  
Ling Pan ◽  
Zhixiang Zuo ◽  
Mei Li ◽  
Lingxing Zeng ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Acid Synthesis ◽  
Ductal Adenocarcinoma ◽  
High Concentration ◽  
Metabolic Switch ◽  
Non Coding Rna ◽  
Xenograft Models ◽  
Transcription Factor Yy1 ◽  
Catabolic Process

AbstractThe molecular mechanism underlying pancreatic ductal adenocarcinoma (PDAC) malignancy remains unclear. Here, we characterize a long intergenic non-coding RNA LINC00842 that plays a role in PDAC progression. LINC00842 expression is upregulated in PDAC and induced by high concentration of glucose via transcription factor YY1. LINC00842 binds to and prevents acetylated PGC-1α from deacetylation by deacetylase SIRT1 to form PGC-1α, an important transcription co-factor in regulating cellular metabolism. LINC00842 overexpression causes metabolic switch from mitochondrial oxidative catabolic process to fatty acid synthesis, enhancing the malignant phenotypes of PDAC cells. High LINC00842 levels are correlated with elevated acetylated- PGC-1α levels in PDAC and poor patient survival. Decreasing LINC00842 level and inhibiting fatty acid synthase activity significantly repress PDAC growth and invasiveness in mouse pancreatic xenograft or patient-derived xenograft models. These results demonstrate that LINC00842 plays a role in promoting PDAC malignancy and thus might serve as a druggable target.

Caveolin-1 and Pancreatic Ductal Adenocarcinoma

2011 ◽  
pp. 43-52
Author(s):  
David W. Rittenhouse ◽  
Oeendree Mukherjee ◽  
Nathan G. Richards ◽  
Charles J. Yeo ◽  
Agnieszka K. Witkiewicz ◽  
...  
Keyword(s):  
Pancreatic Ductal Adenocarcinoma ◽  
Ductal Adenocarcinoma ◽  
Caveolin 1

scholarly journals Genotype tunes pancreatic ductal adenocarcinoma tissue tension to induce matricellular fibrosis and tumor progression

2016 ◽  
Vol 22 (5) ◽  
pp. 497-505 ◽  
Author(s):  
Hanane Laklai ◽  
Yekaterina A Miroshnikova ◽  
Michael W Pickup ◽  
Eric A Collisson ◽  
Grace E Kim ◽  
...  
Keyword(s):  
Tumor Progression ◽  
Pancreatic Ductal Adenocarcinoma ◽  
Ductal Adenocarcinoma ◽  
Tissue Tension

scholarly journals Caveolin-1 interacts with a lipid raft-associated population of fatty acid synthase

Cell Cycle ◽  
2008 ◽  
Vol 7 (14) ◽  
pp. 2257-2267 ◽  
Author(s):  
Dolores Di Vizio ◽  
Rosalyn M. Adam ◽  
Jayoung Kim ◽  
Robert Kim ◽  
Federica Sotgia ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Lipid Raft ◽  
Fatty Acid Synthase ◽  
Caveolin 1

scholarly journals Caveolin-1 is required for the upregulation of fatty acid synthase (FASN), a tumor promoter, during prostate cancer progression

2007 ◽  
Vol 6 (8) ◽  
pp. 1269-1274 ◽  
Author(s):  
Dolores Di Vizio ◽  
Federica Sotgia ◽  
Terence M. Williams ◽  
Ghada S. Hassan ◽  
Franco Capozza ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Fatty Acid ◽  
Cancer Progression ◽  
Fatty Acid Synthase ◽  
Tumor Promoter ◽  
Prostate Cancer Progression ◽  
Caveolin 1

scholarly journals Impact of caveolin-1 expression on prognosis of pancreatic ductal adenocarcinoma

2002 ◽  
Vol 87 (10) ◽  
pp. 1140-1144 ◽  
Author(s):  
M Suzuoki ◽  
M Miyamoto ◽  
K Kato ◽  
K Hiraoka ◽  
T Oshikiri ◽  
...  
Keyword(s):  
Pancreatic Ductal Adenocarcinoma ◽  
Ductal Adenocarcinoma ◽  
Caveolin 1

scholarly journals IGFBP2 promotes tumor progression by inducing alternative polarization of macrophages in pancreatic ductal adenocarcinoma through the STAT3 pathway

2021 ◽  
Vol 500 ◽  
pp. 132-146
Author(s):  
Longhao Sun ◽  
Xuebin Zhang ◽  
Qianqian Song ◽  
Liang Liu ◽  
Elizabeth Forbes ◽  
...  
Keyword(s):  
Tumor Progression ◽  
Pancreatic Ductal Adenocarcinoma ◽  
Ductal Adenocarcinoma ◽  
Stat3 Pathway

scholarly journals Contribution of nuclear BCL10 expression to tumor progression and poor prognosis of advanced and/or metastatic pancreatic ductal adenocarcinoma by activating NF-κB-related signaling

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Sung-Hsin Kuo ◽  
Shih-Hung Yang ◽  
Ming-Feng Wei ◽  
Hsiao-Wei Lee ◽  
Yu-Wen Tien ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Tumor Progression ◽  
Pancreatic Ductal Adenocarcinoma ◽  
Cell Lines ◽  
Poor Prognosis ◽  
Cyclin B1 ◽  
Ductal Adenocarcinoma ◽  
Clinical Samples ◽  
Wild Type ◽  
Pdac Cell

Abstract Background We previously demonstrated that nuclear BCL10 translocation participates in the instigation of NF-κB in breast cancer and lymphoma cell lines. In this study, we assessed whether nuclear BCL10 translocation is clinically significant in advanced and metastatic pancreatic ductal adenocarcinoma (PDAC). Method and materials We analyzed the expression of BCL10-, cell cycle-, and NF-κB- related signaling molecules, and the DNA-binding activity of NF-κB in three PDAC cell lines (mutant KRAS lines: PANC-1 and AsPC-1; wild-type KRAS line: BxPC-3) using BCL10 short hairpin RNA (shBCL10). To assess the anti-tumor effect of BCL10 knockdown in PDAC xenograft model, PANC-1 cells treated with or without shBCL10 transfection were inoculated into the flanks of mice. We assessed the expression patterns of BCL10 and NF-κB in tumor cells in 136 patients with recurrent, advanced, and metastatic PDAC using immunohistochemical staining. Results We revealed that shBCL10 transfection caused cytoplasmic translocation of BCL10 from the nuclei, inhibited cell viability, and enhanced the cytotoxicities of gemcitabine and oxaliplatin in three PDAC cell lines. Inhibition of BCL10 differentially blocked cell cycle progression in PDAC cell lines. Arrest at G1 phase was noted in wild-type KRAS cell lines; and arrest at G2/M phase was noted in mutant KRAS cell lines. Furthermore, shBCL10 transfection downregulated the expression of phospho-CDC2, phospho-CDC25C, Cyclin B1 (PANC-1), Cyclins A, D1, and E, CDK2, and CDK4 (BxPC-3), p-IκBα, nuclear expression of BCL10, BCL3, and NF-κB (p65), and attenuated the NF-κB pathway activation and its downstream molecule, c-Myc, while inhibition of BCL10 upregulated expression of p21, and p27 in both PANC-1 and BxPC-3 cells. In a PANC-1-xenograft mouse model, inhibition of BCL10 expression also attenuated the tumor growth of PDAC. In clinical samples, nuclear BCL10 expression was closely associated with nuclear NF-κB expression (p < 0.001), and patients with nuclear BCL10 expression had the worse median overall survival than those without nuclear BCL10 expression (6.90 months versus 9.53 months, p = 0.019). Conclusion Nuclear BCL10 translocation activates NF-κB signaling and contributes to tumor progression and poor prognosis of advanced/metastatic PDAC.

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