ArticleOncology reports2014
Knockdown of glucose-regulated protein 78 enhances poly(ADP-ribose) polymerase cleavage in human pancreatic cancer cells exposed to endoplasmic reticulum stress.
Article in Oncology reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Article
- Changes in Pancreatic Senescence Mediate Pancreatic Diseases.International journal of molecular sciences · 2023Review
- Co-Occurrence of Hepatitis A Infection and Chronic Liver Disease.International journal of molecular sciences · 2020Review
- Thapsigargin promotes colorectal cancer cell migration through upregulation of lncRNA MALAT1.Oncology reports · 2020Article
- Proteomic analysis of retinal pigment epithelium cells after exposure to UVA radiation.BMC ophthalmology · 2019Article
- Compound K Induces Endoplasmic Reticulum Stress and Apoptosis in Human Liver Cancer Cells by Regulating STAT3.Molecules (Basel, Switzerland) · 2018Article
- Endoplasmic reticulum chaperone glucose-regulated protein 78 in gastric cancer: An emerging biomarker.Oncology letters · 2018Review
- Endoplasmic reticulum stress plays an important role in methotrexate-related cognitive impairment in adult rats.International journal of clinical and experimental pathology · 2017Article
- TTF1-NPs Induce ERS-Mediated Apoptosis and Inhibit Human Hepatoma Cell Growth In Vitro and In Vivo.Oncology research · 2016Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The present study examined the expression of glucose‑regulated protein 78 (GRP78/Bip) in human pancreatic cancer cell lines and the effect of knockdown of GRP78 on the cleavage of poly(ADP-ribose) polymerase (PARP). Human pancreatic cancer cell lines (KP-2, MIAPaCa-2, Panc-1 and SUIT-2), constitutively expressed GRP78. We also demonstrated that ER stress induced by thapsigargin upregulated protein levels of GRP78. In the presence of thapsigargin, knockdown of GRP78 enhanced the PARP cleavage in the human pancreatic cancer cells. These results provide evidence that GRP78 is a potential therapeutic target for 'difficult-to-treat' pancreatic cancer, in which ER stress signaling in part falls into disorder.
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Registered trials
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