Glutaminases regulate glutathione and oxidative stress in cancer.

Archives of Toxicology
José M MatésJavier Márquez

Abstract

Targeted therapies against cancer have improved both survival and quality of life of patients. However, metabolic rewiring evokes cellular mechanisms that reduce therapeutic mightiness. Resistant cells generate more glutathione, elicit nuclear factor erythroid 2-related factor 2 (NRF2) activation, and overexpress many anti-oxidative genes such as superoxide dismutase, catalase, glutathione peroxidase, and thioredoxin reductase, providing stronger antioxidant capacity to survive in a more oxidative environment due to the sharp rise in oxidative metabolism and reactive oxygen species generation. These changes dramatically alter tumour microenvironment and cellular metabolism itself. A rational design of therapeutic combination strategies is needed to flatten cellular homeostasis and accomplish a drop in cancer development. Context-dependent glutaminase isoenzymes show oncogenic and tumour suppressor properties, being mainly associated to MYC and p53, respectively. Glutaminases catalyze glutaminolysis in mitochondria, regulating oxidative phosphorylation, redox status and cell metabolism for tumour growth. In addition, the substrate and product of glutaminase reaction, glutamine and glutamate, respectively, can work as signalling ...Continue Reading

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Citations

Feb 22, 2021·Journal of Biomedical Science·Juan de Los Santos-JiménezJosé M Matés
Apr 28, 2021·Annual Review of Immunology·Elizabeth M SteinertNavdeep S Chandel
Jul 19, 2021·Neurochemistry International·José A Campos-SandovalJavier Márquez

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Methods Mentioned

BETA
nuclear translocation
GTPases
GTPase
transfection
xenografts
xenograft

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