Redox enzymes are essential components of the cellular defence system against oxidative stress, which is a common factor in various diseases. Therefore, understanding the role of bioactive nutraceuticals in modulating the activity of these enzymes holds immense therapeutic potential. This paper provides a comprehensive review of the regulation of redox enzymes in cell and animal models by food-derived bioactive nutraceuticals, focusing on polyphenols and peptides. Specifically, this paper discusses the regulation of superoxide dismutase (SOD), glutathione peroxidase (GPx), catalase (CAT), NAPDH oxidase, xanthine oxidase (XO), myeloperoxidase (MPO), and haem oxygenase (HO) in cell and animal models. Polyphenols, which are abundant in fruits, vegetables, and beverages, have diverse antioxidant properties, including direct scavenging of reactive oxygen species and regulation of transcription factors such as nuclear factor erythroid 2-related factor 2, which leads to the increased expression of the redoxenzymes SOD, HO, and GPx. Similarly, bioactive peptides from various food proteins can enhance antioxidative enzyme activity by regulating gene expression and directly activating the enzyme CAT. In other cases, an antioxidative response requires the downregulation or inhibition of the redox enzymes XO, MPO, and NAPDH oxidase. This paper highlights the potential of bioactive nutraceuticals in mitigating oxidative stress-related diseases and their mechanisms in modulating the redox enzyme expression or activity. Furthermore, the review highlights the need for further research to uncover new therapeutic strategies using nutraceuticals for enhancing cellular antioxidant defence mechanisms and improving health outcomes.
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http://dx.doi.org/10.1039/d4fo03549f | DOI Listing |
Int J Mol Sci
March 2025
Department of Bioscience and Bioinformatics, Graduate School of Computer Science and Systems Engineering, Kyushu Institute of Technology, 680-4 Kawazu, Iizuka 820-8502, Fukuoka, Japan.
Mammalian heme oxygenase (HO) catalyzes heme degradation using reducing equivalents supplied by NADPH-cytochrome P450 reductase (CPR). The tertiary structure of the catalytic domain of a constitutively expressed isoform of HO, HO-2, resembles that of the inductive isoform, HO-1, whereas HO-2 has two heme regulatory motifs (HRM) at the proximal portion of the C-terminus, where the disulfide linkage reflects cellular redox conditions and the second heme binding site is located. Here, we report the results of crosslinking experiments, which suggest that HRM is located near the FMN-binding domain of the CPR when it is complexed with HO-2.
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March 2025
Cawley Center for Translational Cancer Research, Helen F. Graham Cancer Center and Research Institute, ChristianaCare, 4701 Ogletown Stanton Rd Suite 4300, Newark, DE 19713, USA.
The metabolic enzyme aldehyde dehydrogenase 1A1 (ALDH1A1), a cancer stem cell marker associated with poor outcomes in breast cancer, has emerged as a promising therapeutic target in TNBC. The aim of this study was to investigate the role of ALDH1A1 in radiation resistance and redox stress in triple negative breast cancer (TNBC). Functional knockouts of ALDH1A1 were generated by the CRISPR/Cas9-mediated deletion of ALDH1A1 in the SUM159 cell line, and three distinct clonal populations were isolated.
View Article and Find Full Text PDFInt J Mol Sci
February 2025
Department of Biomedical and Neuromotor Sciences, University of Bologna, Piazza di Porta San Donato 2, 40126 Bologna, Italy.
deficiency disorder (CDD), a developmental encephalopathy caused by mutations in the cyclin-dependent kinase-like 5 () gene, is characterized by a complex and severe clinical picture, including early-onset epilepsy and cognitive, motor, visual, and gastrointestinal disturbances. This disease still lacks a medical treatment to mitigate, or reverse, its course and improve the patient's quality of life. Although CDD is primarily a genetic brain disorder, some evidence indicates systemic abnormalities, such as the presence of a redox imbalance in the plasma and skin fibroblasts from CDD patients and in the cardiac myocytes of a mouse model of CDD.
View Article and Find Full Text PDFInt J Mol Sci
February 2025
Neuroimmunology Group, Department of Medicine, University of Lleida-IRBLleida, 25198 Lleida, Spain.
Multiple sclerosis (MS) is characterized by demyelination and neuroinflammation, with oxidative stress playing a pivotal role in lesion pathology. This study aimed to investigate the differential cellular responses to myelin debris under varying oxidative states. Myelin oxidation was induced using a Cu-peroxide system, confirmed by elevated TBARS levels and autofluorescence.
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February 2025
Department of Biochemistry and Microbiology, Faculty of Science, Agriculture and Engineering, University of Zululand, KwaDlangezwa 3886, South Africa.
Cytochromes P450 are a superfamily of heme-containing monooxygenases involved in a variety of oxidative metabolic reactions, primarily catalyzing the insertion of an oxygen atom into a C-H bond. CYP102 represents the first example of a bacterial P450 that can be classified as a type II (eukaryotic-like) P450 and functions as a catalytically self-sufficient enzyme. These unique features have made CYP102 an attractive system for studying P450 structure and function.
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