How does catalase protect cells

This study suggests that these fusion proteins can be potentially used as protein therapeutic agents in catalase-related disorders [ ]. Amyotrophic lateral sclerosis ALS is one of the most common types of progressive and fatal neurological disorders which results in loss of motor neurons mostly in the spinal cord and also to some extent in the motor cortex and brain stem.

Rather, the mutated SOD1 has toxic properties with no lowering of the enzymatic activity. This mutated SOD1 protein reacts with some anomalous substrates such as hydrogen peroxide using it as a substrate and produces the most reactive hydroxyl radical which can severely damage important biomolecules [ ]. Mutated SOD1 also has the potential to use peroxynitrite as an atypical substrate leading to the formation of 3-nitrotyrosine which results in the conversion of a functional protein into a nonfunctional one [ ].

Catalase can reduce the hydrogen peroxide concentration by detoxifying it. Therapeutic approaches using putrescine-modified catalase in the treatment of FALS have also been attempted [ ]. It was found that putrescine-catalase—a polyamine-modified catalase—delayed the progression of weakness in the FALS transgenic mouse model [ ].

Thus, the delay in development of clinical weakness in FALS transgenic mice makes the putrescine-modified catalase a good candidate as a therapeutic agent in diseases linked with catalase anomaly. In this connection, it must be mentioned that the putrescine-modified catalase has been reported to exhibit an augmented blood-brain barrier permeability property while maintaining its activity comparable to that of native catalase with intact delivery to the central nervous system after parenteral administration [ ].

Therefore, further studies with this molecule seem to be warranted. Investigations using synthetic SOD-catalase mimetic, increase in the lifespan of SOD2 nullizygous mice along with recovery from spongiform encephalopathy, and alleviation of mitochondrial defects were observed [ ].

Studies using type 1 and type 2 diabetic mice models with fold upregulated catalase expression showed amelioration in the functioning of the cardiomyocytes [ ]. Cardiomyopathy is related to improper functioning of heart muscles where the muscles become enlarged, thick, or stiff. It can lead to irregular heartbeats or heart failure. Many diabetic patients suffer from cardiomyopathy with structural and functional anomalies of the myocardium without exhibiting concomitant coronary artery disease or hypertension [ ].

As already discussed, catalase is interconnected to diabetes mellitus pathogenesis. It has been observed that a fold increase of catalase activity could drastically reduce the usual features of diabetic cardiomyopathy in the mouse model [ ].

Due to catalase overexpression, the morphological impairment of mitochondria and the myofibrils of heart tissue were prevented. The impaired cardiac contractility was also inhibited with decrease in the production of reactive oxygen species mediated by high glucose concentrations [ ].

So this approach could be an effective therapeutic approach for the treatment of diabetic cardiomyopathy. An increase in focus on the role of catalase in the pathogenesis of oxidative stress-related diseases and its therapeutic approach is needed. Catalase plays a significant role in hydrogen peroxide metabolism as a key regulator [ 28 , 29 , — ]. Some studies have also shown the involvement of catalase in controlling the concentration of hydrogen peroxide which is also involved in the signaling process [ — ].

Acatalasemia is a rare genetic disorder which is not as destructive as other diseases discussed here, but it could be a mediator in the development of other chronic diseases due to prolonged oxidative stress on the tissues. We have also discussed the risk of type 2 diabetes mellitus among acatalasemic patients. But more research on the biochemical, molecular, and clinical aspects of the disease is necessary. There are many more questions about acatalasemia and its relation to other diseases which need to be answered.

Therefore, further studies are needed to focus on catalase gene mutations and its relationship to acatalasemia and other diseases with decreased catalase activity so that the link can be understood more completely. The therapeutic approaches using catalase needs more experimental validation so that clinical trials can be initiated. Use of catalase as a medicine or therapy may be a new and broad field of study. Any novel finding about therapeutic uses of catalase will have a huge contribution in medical science.

Positive findings can direct towards its possible use for treatment of different oxidative stress-related diseases. Catalase is one of the crucial antioxidant enzymes which plays an important role by breaking down hydrogen peroxide and maintaining the cellular redox homeostasis. While there are many factors involved in the pathogenesis of these diseases, several studies from different laboratories have demonstrated that catalase has a relationship with the pathogenesis of these diseases.

Research in this area is being carried out by many scientists at different laboratories exploring different aspects of these diseases, but with an ever-increasing aging population, much remains to be achieved. On the other hand, the potential of catalase as a therapeutic drug in the treatment of several oxidative stress-related diseases is not adequate and is still being explored. Additional research is needed to confirm if catalase may be used as a drug in the treatment of various age-related disorders.

Supplementary Figure 1. In module 1, ACOX1 peroxisomal acyl coenzyme A oxidase , HSD17B4 peroxisomal multifunctional enzyme , and HAO1 hydroxyacid oxidase 1 are involved in the fatty acid oxidation pathway in the peroxisome while the protein DAO D amino acid oxidase is involved in the amino acid metabolism pathway in the peroxisome [ 4 — 6 ] Supplementary Figure 1. Supplementary Materials. This is an open access article distributed under the Creative Commons Attribution License , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Article of the Year Award: Outstanding research contributions of , as selected by our Chief Editors. Read the winning articles. Journal overview. Special Issues. Academic Editor: Cinzia Signorini. Received 25 Mar Revised 18 Jun Accepted 14 Aug Published 11 Nov Abstract Reactive species produced in the cell during normal cellular metabolism can chemically react with cellular biomolecules such as nucleic acids, proteins, and lipids, thereby causing their oxidative modifications leading to alterations in their compositions and potential damage to their cellular activities.

Introduction Reactive species RS are highly active moieties, some of which are direct oxidants, and some have oxygen or oxygen-like electronegative elements produced within the cell during cellular metabolism or under pathological conditions. Table 1. Examples of the various free radicals and other oxidants in the cell [ 2 ]. Figure 1. Relationship between catalase and other antioxidant enzymes. Figure 2. Figure 3.

Steps in catalase reaction: a first step; b second step. Table 2. Physicochemical characteristics of catalase from various sources. Figure 4. Figure 5. Figure 6. Association of catalase polymorphism with risk of some widespread diseases. Figure 7.

Prevalence of diabetes amongst males and females in some countries in data source: World Health Organization-Diabetes Country Profile Types Position of mutation Types of mutation Results of mutation Effect on catalase References Type A Insertion of GA at position in exon 2 occurs which is responsible for the increase of the repeat number from 4 to 5 Frame shift mutation Creates a TGA codon at position Lacks a histidine residue, an essential amino acid necessary for hydrogen peroxide binding [ ] Type B Insertion of G at position 79 of exon 2 Frame shift mutation Generates a stop codon TGA at position 58 A nonfunctional protein is produced [ ] Type C A substitution mutation of G to A at position 5 in intron 7 Splicing mutation No change in peptide chain Level of catalase protein expression is decreased [ , ] Type D Mutation of G to A at position 5 of exon 9 Coding region mutation Replaces the arginine residue to histidine or cysteine Lowering of catalase activity [ ].

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Anticancer Agents Med. Vetrano, A. ROS serve as normal signalling molecules, but unchecked they can damage a wide variety of molecules within cells, leading to oxidative stress. This is effective in the short-term, but high levels of oxidative stress can lead to serious tissue damage through excessive cell death and oxidative damage. To help protect against the destructive effects of ROS, aerobic organisms produce protective antioxidant enzymes such as catalase EC 1. It was the evolution of these enzymes that made oxidative cellular metabolism possible.

Catalases are produced by aerobic organisms ranging from bacteria to man.