Review
Toward clinical application of the Keap1–Nrf2 pathway

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The Keap1–Nrf2 pathway plays a crucial role in determining the sensitivity of cells to chemical and/or oxidative insults by regulating the basal and inducible expression of detoxification and antioxidant enzymes, ABC transporters, and other stress response enzymes and/or proteins. Increasing attention has been focused on the roles that the Keap1–Nrf2 pathway plays in the protection of our body against drug toxicity and stress-induced diseases. Simultaneously, Nrf2 has been recognized to promote oncogenesis and resistance to chemotherapeutic drugs. Cancer cells hijack Nrf2 activity to support their malignant growth and thus Nrf2 has emerged as a therapeutic target. Translational studies of the Keap1–Nrf2 system, from mechanistic understanding to clinical applications, are now important to improve human health.

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Inducible cellular defense system

Mammalian cells are frequently exposed to extrinsically and intrinsically generated toxic substances and to oxidative insults that disrupt their normal function by damaging nucleic acids, proteins, and membrane lipids. To overcome such insults, cells are equipped with elaborate defense systems. The basal level expression of detoxification enzymes and xenobiotic transporters appears to be sufficient to protect cells against low level chemical and/or oxidative stresses. The body is also equipped

Target genes of Nrf2

Nrf2 dimerizes with members of the small Maf family and binds to antioxidant or electrophile response elements (AREs/EpREs) located in the regulatory regions of cellular defense enzyme genes [1]. Several Nrf2 target genes have been identified, and the number has increased through the analysis of the gene expression profiles of Nrf2-deficient mice [2]. Recent technical advances have enabled us to analyze the genome-wide distribution of Nrf2 and have provided us with comprehensive unbiased

Keap1 negatively regulates Nrf2

Keap1 is an adaptor protein for a Cul3-based ubiquitin E3 ligase 6, 7. Under normal conditions, Keap1 binds to Nrf2 in the cytoplasm and promotes the ubiquitination of Nrf2. Subsequently, Nrf2 protein is degraded by the proteasome. In the presence of Nrf2-inducing chemicals, the ubiquitin E3 ligase activity of the Keap1–Cul3 complex declines, and Nrf2 is stabilized (Figure 1). The stabilized Nrf2 accumulates in the nucleus and activates its target genes.

The function of Keap1 as a negative

Keap1 as a sensor of chemical and oxidative stresses

Many Nrf2-activating chemicals [e.g., diethyl maleate (DEM), tert-butylhydroquinone (tBHQ), sulforaphane (SFN), and 15-deoxy-Δ12,14-prostaglandin J2 (15d-PGJ2)] are electrophilic and are capable of reacting with nucleophilic thiols, including cysteine sulfhydryl groups [10]. Several independent research groups have employed mass spectrometry to identify the specific pattern of Keap1 cysteine modification generated by each Nrf2 inducer [11]. The modification of Keap1 at cysteine residues results

Molecular mechanisms of stress sensing by the Keap1–Nrf2 system

One of the most interesting mechanisms for the regulation of Nrf2 by Keap1 proposed to date is the ‘hinge and latch model’ [22] (Figure 1). This model is supported by single-particle electron microscopy data, which indicate that the overall structure of the Keap1 dimer resembles a cherry-bob with two globular units (the double glycine repeat and the C-terminal or DC domains) connected to a stem [the homodimerizing BTB (bric-a-brac, tramtrack, and broad complex) domains] [23]. The Keap1

Activation of Nrf2 as a potential therapeutic strategy

Targeted Nrf2 knockout (Nrf2−/−) mice exhibit markedly lower expression levels for cellular defense genes in various tissues [29]. Accordingly, Nrf2−/− mice are inherently more susceptible to drug-induced toxicity and oxidative stress-induced diseases, including acute lung injury, chronic obstructive pulmonary diseases, diabetic nephropathy, heart failure, and cancer [29]. In addition, the activation of Nrf2 by pharmacological (i.e., pretreatment with Nrf2 inducers) or genetic (i.e., the

Development of Nrf2 activators

Because many studies have demonstrated Nrf2 plays important roles in the protection against various diseases, including cancer, neurodegenerative disease, cardiovascular disease, acute lung injury, chronic obstructive pulmonary diseases, autoimmune disease, and inflammation [29], there is substantial interest in identifying and developing Nrf2 activators for therapeutic use. Some of the most promising Nrf2 inducers are a series of triterpenoids derived from oleanolic acid, which itself has

Search for novel Nrf2-activating drugs

The search for novel Nrf2 inducers will be accelerated by the development of screening systems that provide direct indications of Nrf2 activation or Keap1 modification. An example of such an assay is a reporter assay in which the reporter is fused to the N terminus of Nrf2 including Neh2 and Neh6 degron domains; this reporter is highly responsive to molecules that activate Nrf2 34, 35, 36, 37. In addition, in silico screening for chemicals capable of modifying Keap1, and thus likely to activate

Adverse effects due to the activation of Nrf2

Nrf2 activation may have a therapeutic potential. However, the lethality of Keap1 knockout mice indicates that constitutive activation of Nrf2 in the upper digestive tract tissues can result in serious adverse effects 8, 9. Multiple studies have demonstrated a link between oncogenesis and mutations in the Keap1–Nrf2 pathway that result in the constitutive activation of Nrf2 40, 41, 42. The resistance of cancer to chemotherapy has been attributed to an increase in Nrf2 signaling.

Role of Nrf2 in oncogenesis

Elevated NRF2 levels have been detected in various cancer tissues [41]. Somatic mutations in the KEAP1 gene, including missense mutations, insertions and deletions, have been identified in tumor tissues, most often in heterozygous form. Importantly, these mutations are associated with the stabilization of NRF2. As shown in Figure 3, a genetically engineered mouse model demonstrated that heterozygous, dominant-negative mutations in KEAP1 in cancer cells could lead to increases in NRF2 activity

Small-molecule inhibitors of Nrf2

In the context of the adverse roles that Nrf2 plays in diseases, the pharmacological inhibition of Nrf2 signaling could provide a promising strategy to improve the efficacy of treatment. Retinoic acid receptor α agonists have been shown to inhibit Nrf2 activity through their physical interaction with Nrf2, thus preventing Nrf2 from binding to the ARE and activating its target genes [58]. Similarly, brusatol, a component of the Brucea javanica shrub, was identified in a screen of natural

Unresolved questions and future studies

Recent studies have proven that Keap1 senses a wide range of Nrf2 activators 15, 16. However, the way in which Keap1 utilizes distinct sensing mechanisms through different cysteine residues is currently unknown. Further studies on the individual sensing mechanisms should provide the answer and give valuable insight to guide drug development.

With regard to the clinical application of Nrf2 activators, adverse effects still need to be rigorously explored. There is a growing concern that Nrf2

Concluding remarks

There have been significant advances in our understanding of the function and regulation of Nrf2. In particular, analyses of Nrf2-knockout mice [1] and the identification of Keap1 [6] have provided invaluable insights into the contribution of the Keap1–Nrf2 system to the stress response. This review has highlighted the potential therapeutic benefits of targeting Nrf2. Although a large body of evidence indicates that the activation of Nrf2 protects animals against a variety of diseases [29], the

Acknowledgments

This work was supported in part by Grants-in-Aids for Creative Scientific Research and Scientific Research from Japan Society for the Promotion of Science (JSPS), the Target Protein Program from the Ministry of Education, Culture, Sports, Science, and Technology (MEXT), the Tohoku University Global COE Program for Conquest of Signal Transduction Diseases with ‘Network Medicine’, CREST from Japan Science and Technology Agency (JST), and the NAITO foundation.

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