ArticleJournal of bioenergetics and biomembranes2021
HSP70 inhibition suppressed glioma cell viability during hypoxia/reoxygenation by inhibiting the ERK1/2 and PI3K/AKT signaling pathways.
Article in Journal of bioenergetics and biomembranes, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- ThemicroPublication biology · 2026Article
- Promising Potential of Edaravone-Loaded Nanogel in Ameliorating of Stroke in Rats: The Modulation of Immune Response.BioMed research international · 2026Article
- Glioblastoma cell motility and invasion is regulated by membrane-associated heat shock protein Hsp70.Journal of neuro-oncology · 2025Article
- Proteomic Analysis Revealed the Potential Role of MAGE-D2 in the Therapeutic Targeting of Triple-Negative Breast Cancer.Molecular & cellular proteomics : MCP · 2024Article
- HSP70 Family in Cancer: Signaling Mechanisms and Therapeutic Advances.Biomolecules · 2023Review
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Authors and funding
7 authors.
Funding
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Abstract
Heat shock protein 70 (HSP70) can regulate astrocyte viability under hypoxic and ischemic conditions. However, the protective mechanism involved is not completely clear. This study aimed to investigate whether HSP70 protects U87 glioma cells against hypoxic damage via the extracellular signal-regulated kinases 1/2 (ERK1/2) and phosphoinositide 3-kinase/protein kinase B (PI3K/AKT) signaling pathways. Lentivirus-mediated HSP70-siRNA was used for HSP70 silencing. U87 glioma cells with lentiviral infection were exposed to hypoxia for 4, 8, 12, and 24 h, respectively, followed by a 24-h reoxygenation treatment. A Cell-Counting Kit-8 was then used to evaluate the viability of the U87 glioma cells. Reverse transcription quantitative polymerase chain reaction (RT-qPCR) and western blotting were performed to determine the mRNA and protein levels, respectively. The expression of HSP70, p-ERK1/2, p-AKT, and U87 cell viability were increased after 8 h of hypoxia/24 h of reoxygenation (P < 0.01). However, HSP70 silencing significantly decreased the U87 cell viability after the hypoxia/reoxygenation treatment (P < 0.01). The protein expressions of p-ERK1/2 and p-AKT also decreased in HSP70-silenced U87 cells (P < 0.01). In conclusion, HSP70 inhibition suppressed the viability of U87 glioma cells during hypoxia/reoxygenation (at least partially) by inhibiting the ERK1/2 and PI3K/AKT signaling pathways. This study may help to understand the molecular mechanisms underlying the progression and development of cerebral hypoxia-ischemia.
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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.