catalase

Overview

Catalase is a heme-containing antioxidant enzyme that catalyzes the decomposition of hydrogen peroxide into water and oxygen. By removing hydrogen peroxide, it helps limit oxidative damage to lipids, proteins, and nucleic acids and works in concert with other redox defenses such as superoxide dismutase, glutathione peroxidase, and the broader Nrf2-associated antioxidant genes network. Catalase is therefore a central component of cellular antioxidant homeostasis and is frequently used as a biochemical readout of oxidative stress in biomedical research.

In recent literature, catalase has also appeared as a therapeutic target, a biomimetic function, or a catalytic activity incorporated into nanomaterials and hydrogels. Studies have examined catalase in contexts including renal ischemia-reperfusion injury, cataract, hepatocellular carcinoma, interstitial cystitis/bladder pain syndrome, chronic mountain sickness, neurodegeneration, diabetes-related tissue injury, and nanoparticle-induced oxidative stress. Across these settings, catalase is typically discussed in relation to reactive oxygen species, mitochondrial dysfunction, ferroptosis, senescence markers such as p16 and p21, and signaling pathways including PI3K/Akt signaling pathway, FOXO3, SIRT1/HIF-1α pathway, and Nrf2-related antioxidant responses.

Focus of Latest Publications

Recent publications portray catalase in three main roles: as an endogenous antioxidant marker, as a mechanistic node in oxidative-stress biology, and as a functional component of engineered therapeutic systems.

Several studies used catalase activity as a biomarker of oxidative injury or treatment response. In animal and cellular models, catalase levels were reported to fall during toxic or disease-associated stress and rise after protective interventions. Examples include acrylamide toxicity in Nile tilapia, carbendazim exposure in fish, polystyrene nanoplastic exposure in goldfish, UVB-induced skin photodamage, doxorubicin-induced neurotoxicity, and diabetic reproductive injury. In these settings, catalase was measured alongside superoxide dismutase, glutathione, malondialdehyde, and total antioxidant capacity to characterize redox imbalance. Protective agents such as metformin, zingerone, pinostrobin, silybin-collagen XVII composite nanoemulsion, Chlorophytum borivilianum, and encapsulated pomegranate peel polyphenols were reported to restore catalase activity and reduce oxidative damage.

Catalase also appeared as a mechanistic target in pathway-focused studies. One report on Tibetan medicine Bawei Chenxiang Wan described attenuation of chronic mountain sickness through the AKT/FOXO3a/CAT axis, linking catalase to FOXO3-mediated antioxidant regulation. Another study on SIRT1 and UVA-induced photoaging found that SIRT1 could transcriptionally upregulate CAT together with SOD2 and HO-1, supporting a role for catalase in anti-photoaging defense. In colorectal cancer cells, PhIP exposure was associated with altered catalase and SOD2 expression, while glioma research reported suppression of catalase activity under oxidative stress conditions. These findings place catalase within broader redox and survival networks involving PI3K/Akt signaling pathway, nuclear factor kappa B, and Nrf2-associated antioxidant genes.

A second major theme is catalase as a therapeutic mimic or engineered functional element. Multiple nanomaterials were designed with catalase-like activity or were directly functionalized with catalase. Examples include Mn-chelating L-serine nanoarchitectures with SOD- and catalase-like activity for renal ischemia-reperfusion injury, cerium oxide nanozymes that mimic catalase through a Ce3+/Ce4+ redox cycle for cataract treatment, ROS-responsive nanodiscs with intrinsic SOD/catalase-mimetic activity for bladder pain syndrome, Mg/Mn-based nanozymes in injectable hydrogels for periodontal bone resorption, and black phosphorus nanosheets covalently functionalized with catalase for photo-/radio-therapy of hepatocellular carcinoma. These studies emphasize catalase as a practical antioxidant function that can be engineered into biomaterials to scavenge reactive oxygen species, improve mitochondrial function, and support tissue repair or anticancer therapy.

Catalase was also used experimentally as a ROS scavenger or comparator in mechanistic studies. In ZnO nanoparticle exposure in Caenorhabditis elegans, catalase helped establish that mitochondrial electron transport chain-derived ROS contributed to ferritinophagy-mediated ferroptosis and developmental delay. In other work, catalase was part of antioxidant panels used to assess the effects of cumin oil, grape seed oil nanoemulsion, royal jelly, tea polyphenol-chitosan composites, black maca nano-emulsion, Artemisia diet, and other interventions. These studies collectively reinforce catalase as a standard indicator of oxidative stress and a functional mediator of antioxidant defense.