ArticleOncology letters2015
Type II cyclic guanosine monophosphate-dependent protein kinase inhibits epidermal growth factor receptor activation in different cancer cell lines.
Article in Oncology letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed, 3 citations in OpenAlex.
- Cyclic Guanosine Monophosphate (cGMP)-Dependent Protein Kinase II Blocks Epidermal Growth Factor (EGF)/Epidermal Growth Factor Receptor (EGFR)-Induced Biological Effects on Osteosarcoma Cells.Medical science monitor : international medical journal of experimental and clinical research · 2018Article
- Protein Kinases Type II (PKG II) Combined with L-Arginine Significantly Ameliorated Xenograft Tumor Development: Is L-Arginine a Potential Alternative in PKG II Activation?Medical science monitor : international medical journal of experimental and clinical research · 2018Article
- The constitutively active PKG II mutant effectively inhibits gastric cancer developmentTherapeutic advances in medical oncology · 2018Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Previous data has revealed that type II cyclic guanosine monophosphate-dependent protein kinase (PKG II) inhibits epidermal growth factor (EGF)-induced phosphorylation/activation of the epidermal growth factor receptor (EGFR) and mitogen-activated protein kinase/extracellular-signal-regulated kinase (MAPK/ERK) in gastric cancer cells. The aim of the present study was to determine whether PKG II inhibited EGF-induced phosphorylation/activation of EGFR and MAPK/ERK in cell lines derived from different cancer tissues. SW480, HepG2, OS-RC-2, A549, MCF-7 and U251 cells were transfected with adenoviral constructs encoding PKG II cDNA (Ad-PKG II) to upregulate the expression of PKG II, and then treated with 8-(4-chlorophenylthio)guanosine 3',5'-cyclic monophosphate (8-pCPT-cGMP) in order to activate the kinase. Western blot analysis was performed to investigate the phosphorylation of EGFR and MAPK/ERK. The results demonstrated that treatment with 100 ng/ml EGF for 5 min increased the tyrosine (Tyr)1068 phosphorylation of EGFR and the threonine 202/Tyr204 phosphorylation of MAPK/ERK. Transfecting the cells with Ad-PKG II, and stimulating the kinases with 8-pCPT-cGMP efficiently inhibited the EGF-induced phosphorylation of EGFR and MAPK/ERK. The results revealed that PKG II had an inhibitory effect upon EGFR activation and the consequent MAPK/ERK-mediated signaling of cell lines derived from the various cancer tissues.
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Registered trials
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