ArticleFree radical research2003
Phospholipid hydroperoxide glutathione peroxidase induces a delay in G1 of the cell cycle.
Article in Free radical research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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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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
17 citing papers in PubMed, 34 citations in OpenAlex.
- Targeting glutathione peroxidase 4 in ferroptosis: from immune regulation to pharmacological development and translational applications.Frontiers in pharmacology · 2026Review
- Glutathione peroxidase 4 overexpression induces anomalous subdiffusion and impairs glioblastoma cell growth.Journal of biological engineering · 2024Article
- Regulation of Mitochondrial Dynamics in Parkinson's Disease-Is 2-Methoxyestradiol a Missing Piece?Antioxidants (Basel, Switzerland) · 2021Review
- Arachidonate 12-lipoxygenase and 12-hydroxyeicosatetraenoic acid contribute to stromal aging-induced progression of pancreatic cancer.The Journal of biological chemistry · 2020Article
- Understanding the Redox Biology of Selenium in the Search of Targeted Cancer Therapies.Antioxidants (Basel, Switzerland) · 2020Review
- Simultaneous detection of the enzyme activities of GPx1 and GPx4 guide optimization of selenium in cell biological experiments.Redox biology · 2020Article
- Triphenylphosphonium derivatives disrupt metabolism and inhibit melanoma growth in vivo when delivered via a thermosensitive hydrogel.PloS one · 2020Article
- Ferroptosis at the crossroads of cancer-acquired drug resistance and immune evasion.Nature reviews. Cancer · 2019Review
- Fatty Acid-Stimulated Insulin Secretion vs. Lipotoxicity.Molecules (Basel, Switzerland) · 2018Review
- Comparison of the seleno-transcriptome expression between human non-cancerous mammary epithelial cells and two human breast cancer cell lines.Oncology letters · 2017Article
- Nrf2 modulates cell proliferation and antioxidants defenses during liver regeneration induced by partial hepatectomy.International journal of clinical and experimental pathology · 2017Article
- An Assay for the Rate of Removal of Extracellular Hydrogen Peroxide by Cells.Redox biology · 2013Article
- Redox homeostasis in pancreatic β cells.Oxidative medicine and cellular longevity · 2012Review
- Glutathione peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities.Antioxidants & redox signaling · 2011Review
- The beneficial effects of pentoxifylline on caerulein-induced acute pancreatitis in rats.Digestive diseases and sciences · 2009Article
- Mitochondria: a hub of redox activities and cellular distress control.Molecular and cellular biochemistry · 2007Review
- Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Phospholipid hydroperoxide glutathione peroxidase (PhGPx) is an antioxidant enzyme that reduces cellular phospholipid hydroperoxides (PLOOHs) to alcohols. Cellular peroxide tone has been implicated in cell growth and differentiation. By reducing the PLOOH level in the cell membrane, PhGPx regulates the peroxide tone and thereby might be involved in cell growth. We hypothesized that overexpression of PhGPx in human breast cancer cells would decrease their growth rate. We stably transfected MCF-7 cells (Wt) with L-PhGPx and measured cell doubling time, plating efficiency, and cell cycle phase transit times. P-4 cells (8-fold increase in PhGPx activity) showed a 2-fold increase in doubling time; doubling time increased directly with PhGPx activity (r = 0.95). The higher the PhGPx activity, the lower the plating efficiency (r = -0.86). The profile of other antioxidant enzymes was unchanged. Overexpression of PhGPx lowered the steady-state level of PLOOH (by > 60%). Results from bromodeoxyuridine pulse-chase experiments and flow cytometry indicate that PhGPx induced a delay in MCF-7 proliferation that was primarily due to a slower progression from G1 to S. These results support the hypothesis that PhGPx plays a regulatory role in the progression of MCF-7 cells from G1 to S possibly by regulating the steady-state levels of PLOOH. These data suggest that PhGPx can lower the peroxide tone, which might change the cellular redox environment resulting in a delay in G1 transit. Thus, PhGPx could be an important factor in cell growth.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.