ArticleJournal of applied physiology (Bethesda, Md. : 1985)2012
Heat shock protein 70 (Hsp70) inhibits oxidative phosphorylation and compensates ATP balance through enhanced glycolytic activity.
Article in Journal of applied physiology (Bethesda, Md. : 1985), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 65 citations in OpenAlex.
- Heat Shock Proteins and Exercise in Skeletal Muscle Insulin Resistance: Protective Mechanisms and Therapeutic Potential.International journal of molecular sciences · 2026Review
- Article
- Post-warming quality of goat oocytes under heat shock stress: A study of the maturation rate, heat shock protein-70, adenosine triphosphate, and glutathione levels.Veterinary world · 2025Article
- Inhibition of protein or glutamine biosynthesis affect the light-induced dephosphorylation of the SBiP1 chaperone in Symbiodiniaceae.Bioscience reports · 2025Article
- Exploring Epigenetic and Genetic Modulation in Animal Responses to Thermal Stress.Molecular biotechnology · 2025Review
- C-Terminal Hsp90 Inhibitors Overcome MEK and BRAF Inhibitor Resistance in Melanoma.Journal of cellular and molecular medicine · 2025Article
- Metabolic and stress response adaptations in T cells to fever and physiological heat.Trends in immunology · 2025Review
- Review
- Early detection and progression of insulin resistance revealed by impaired organismal anti-inflammatory heat shock response during ex vivo whole-blood heat challenge.Clinical science (London, England : 1979) · 2025Article
- What's cooking? The effect of temperature on the immune response.Frontiers in immunology · 2025Review
- The role of heat shock protein 70 on oocyte apoptosis during vitrification.Open veterinary journal · 2025Review
- Proteomic Analysis of HepG2 Cells Reveals FAT10 and BAG2 Signaling Pathways Affected by a Protease Inhibitor fromTurkish journal of pharmaceutical sciences · 2024Article
- Heat shock response during the resolution of inflammation and its progressive suppression in chronic-degenerative inflammatory diseases.Cell stress & chaperones · 2024Review
- Metabolic Oscillations and Glycolytic Phenotypes of Cancer Cells.International journal of molecular sciences · 2023Article
- Suboptimal Mitochondrial Activity Facilitates Nuclear Heat Shock Responses for Proteostasis and Genome Stability.Molecules and cells · 2023Article
- Culturing characteristics of Hanwoo myosatellite cells and C2C12 cells incubated at 37°C and 39°C for cultured meat.Journal of animal science and technology · 2023Article
- The heart-brain axis: A proteomics study of meditation on the cardiovascular system of Tibetan Monks.EBioMedicine · 2022Article
- The Effects of Heat Shock Protein 70 Addition in the Culture Medium on the Development and Quality of In Vitro Produced Heat Shocked Bovine Embryos.Animals : an open access journal from MDPI · 2021Article
- Comparative Expression Profiling and Sequence Characterization of ATP1A1 Gene Associated with Heat Tolerance in Tropically Adapted Cattle.Animals : an open access journal from MDPI · 2021Article
- Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To address possible effects of heat shock protein 70 (Hsp70) on energy metabolism, we established a cell line expressing different levels of Hsp70 and evaluated changes in glucose and lactate metabolites, as well as ATP levels accordingly. In addition, activities of enzymes involved in glycolysis [phosphofructokinase (PFK) and lactate dehydrogenase (LDH)], Krebs cycle [citric synthase (CS)], and oxidative phosphorylation {NADH dehydrogenase [complex I (CI)] and ubiquinol:cytochrome-c reductase [complex III (CIII)]} were analyzed. The results show that both glucose consumption and lactate excretion were elevated significantly in cells expressing increased levels of Hsp70. Simultaneously, the activities of glycolytic enzymes PFK and LDH were increased markedly in cells overexpressing Hsp70. Activities of enzymes CI and CIII, both involved in oxidative phosphorylation, decreased upon increased expression of Hsp70. These findings were supported by nonsignificant reductions of CS activities in cells that overexpressed Hsp70, whereas intracellular ATP levels remained constant over a wide range of Hsp70 expression. In conclusion, overexpression of Hsp70 in HeLa cells results in downregulation of oxidative phosphorylation, in particular, multiprotein CIII, the main source of reactive oxygen species. In exchange, upregulation of the glycolytic pathway compensates for the homeostasis of cellular ATP supply.
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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.