scholarly journals An in vitro and in vivo study of gemcitabine-loaded albumin nanoparticles in a pancreatic cancer cell line

2015 ◽  
pp. 6825 ◽  
Author(s):  
Xinzhe Yu ◽  
Xinming Pu ◽  
Chao Xie ◽  
Yunlong Song ◽  
Hang He ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Cancer Cell ◽  
Pancreatic Cancer Cell ◽  
In Vivo Study ◽  
Albumin Nanoparticles

scholarly journals Deferasirox, an oral iron chelator, with gemcitabine synergistically inhibits pancreatic cancer cell growth in vitro and in vivo

Oncotarget ◽  
2018 ◽  
Vol 9 (47) ◽  
pp. 28434-28444 ◽  
Author(s):  
Shuhei Shinoda ◽  
Seiji Kaino ◽  
Shogo Amano ◽  
Hirofumi Harima ◽  
Toshihiko Matsumoto ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Cell Growth ◽  
Cancer Cell ◽  
Pancreatic Cancer Cell ◽  
Iron Chelator ◽  
Oral Iron ◽  
Cancer Cell Growth ◽  
Oral Iron Chelator

Cordycepin inhibits pancreatic cancer cell growth in vitro and in vivo via targeting FGFR2 and blocking ERK signaling

2020 ◽  
Vol 18 (5) ◽  
pp. 345-355
Author(s):  
Xue-Ying LI ◽  
Homng TAO ◽  
Can JIN ◽  
Zhen-Yun DU ◽  
Wen-Feng LIAO ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Cell Growth ◽  
Cancer Cell ◽  
Pancreatic Cancer Cell ◽  
Erk Signaling ◽  
Cancer Cell Growth

EXPRESSION OF FGFR1-IIIB INHIBITS PANCREATIC CANCER CELL GROWTH IN VITRO AND IN VIVO

Pancreas ◽  
2006 ◽  
Vol 33 (4) ◽  
pp. 475
Author(s):  
M. Kornmann ◽  
S. Zhou ◽  
D. Henne-Bruns ◽  
M. Korc ◽  
M. Bachem ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Cell Growth ◽  
Cancer Cell ◽  
Pancreatic Cancer Cell ◽  
Cancer Cell Growth

Components of the phosphatidylserine endoplasmic reticulum to plasma membrane transport mechanism as targets for KRAS inhibition in pancreatic cancer

2021 ◽  
Vol 118 (51) ◽  
pp. e2114126118
Author(s):  
Walaa E. Kattan ◽  
Junchen Liu ◽  
Dina Montufar-Solis ◽  
Hong Liang ◽  
Bhargavi Brahmendra Barathi ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Cancer Cell ◽  
Transport Mechanism ◽  
Pancreatic Cancer Cell ◽  
Antiviral Agent ◽  
Pancreatic Tumors

KRAS is mutated in 90% of human pancreatic ductal adenocarcinomas (PDACs). To function, KRAS must localize to the plasma membrane (PM) via a C-terminal membrane anchor that specifically engages phosphatidylserine (PtdSer). This anchor-binding specificity renders KRAS–PM localization and signaling capacity critically dependent on PM PtdSer content. We now show that the PtdSer lipid transport proteins, ORP5 and ORP8, which are essential for maintaining PM PtdSer levels and hence KRAS PM localization, are required for KRAS oncogenesis. Knockdown of either protein, separately or simultaneously, abrogated growth of KRAS-mutant but not KRAS–wild-type pancreatic cancer cell xenografts. ORP5 or ORP8 knockout also abrogated tumor growth in an immune-competent orthotopic pancreatic cancer mouse model. Analysis of human datasets revealed that all components of this PtdSer transport mechanism, including the PM-localized EFR3A-PI4KIIIα complex that generates phosphatidylinositol-4-phosphate (PI4P), and endoplasmic reticulum (ER)–localized SAC1 phosphatase that hydrolyzes counter transported PI4P, are significantly up-regulated in pancreatic tumors compared to normal tissue. Taken together, these results support targeting PI4KIIIα in KRAS-mutant cancers to deplete the PM-to-ER PI4P gradient, reducing PM PtdSer content. We therefore repurposed the US Food and Drug Administration–approved hepatitis C antiviral agent, simeprevir, as a PI4KIIIα inhibitor In a PDAC setting. Simeprevir potently mislocalized KRAS from the PM, reduced the clonogenic potential of pancreatic cancer cell lines in vitro, and abrogated the growth of KRAS-dependent tumors in vivo with enhanced efficacy when combined with MAPK and PI3K inhibitors. We conclude that the cellular ER-to-PM PtdSer transport mechanism is essential for KRAS PM localization and oncogenesis and is accessible to therapeutic intervention.

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