Why catalase hydrogen peroxide

Various studies have shown that the catalase levels in the epidermis of vitiligo patients are lower as compared to those of the healthy control subjects [ , ] with a resultant increase in the concentration of hydrogen peroxide. In the cell, hydroxyl radicals can be produced spontaneously from hydrogen peroxide through photochemical reduction, i. These hydroxyl radicals are able to oxidize lipids in the cell membrane.

This may be the cause behind damage of keratinocytes and melanocytes in the epidermal layer of the skin in such patients [ — ]. Moreover, the inhibitory effect of hydrogen peroxide or allelic modification of the CAT gene results in low catalase activity. However, it has been observed that there is an erratic relationship between catalase polymorphism and vitiligo.

But the results were not observed to be consistent. Though the results are inconsistent from population studies, an interconnection between the pathogenesis and catalase may still be possible as scattered demonstrations are reported in the literature. Therefore, further studies to understand the link is necessary.

Acatalasemia AC is a hereditary disorder which is linked with the anomaly of catalase enzyme affecting its activity. In , Takahara, a Japanese otolaryngologist, first reported this disorder [ , ]. He found that four out of seven races in Japan had the same genetic flaw [ ]. His ex vivo experiments consisted of filling the mouth ulcer of a diseased patient with hydrogen peroxide.

Since no bubble formation was observed, he concluded that a catalase or its enzymatic activity is absent in the saliva of the patients. In honor of his primary findings, this disease was christened as the Takahara disease. Acatalasemia and hypocatalasemia signify homozygotes and heterozygotes, respectively.

The heterozygote of acatalasemia shows half of the catalase activity than normal and this phenotype is known as hypocatalasemia [ ]. Depending on the geographical location from where it has been first studied, there are different types of acatalasemia described as Japanese, Swiss, Hungarian, German, and Peruvian types. Approximately acatalasemic patients have been reported to date from all over the world.

Two kinds of mutations in the catalase gene have been reported to be involved in the Japanese acatalasemia. A splicing mutation has been held responsible for Japanese acatalasemia I where a substitution of a guanine residue with adenine residue at position 5 of intron 4 disturbed the splicing pattern of the RNA product producing a defective protein [ ].

In Japanese acatalasemia II, a frame shift mutation occurs due to the deletion of thymine in position of exon 4 which modifies the amino acid sequence and produces a new TGA stop codon at the 3 terminal. Translation of this mutated strand produces a polypeptide of amino acid residues. This is a truncated protein that is unstable and nonfunctional [ ]. Aebi et al. The study on the fibroblast from Swiss acatalasemia patients suggests that structural mutations in the CAT gene are responsible for inactivation of catalase [ ].

Goth, a Hungarian biochemist, first described Hungarian acatalasemia in after studying the disease in two Hungarian sisters. He found that the catalase activities in the blood of these two acatalasemic sisters were 4. Studies at his laboratory led Goth to suggest that mutations of the CAT gene and resultant structural changes in the catalase protein are responsible for Hungarian acatalasemia.

This laboratory also reported that there was a risk of diabetes mellitus amongst the Hungarian acatalasemic family members though further biochemical and genetic analysis needs to be performed to validate the hypothesis that acatalasemic patients have more chance of developing diabetes mellitus [ 79 ]. There are generally four types of Hungarian acatalasemia which varies according to the different site of gene mutation in the DNA.

The same is represented in Table 3. Catalase is one of the most important antioxidant enzymes. As it decomposes hydrogen peroxide to innocuous products such as water and oxygen, catalase is used against numerous oxidative stress-related diseases as a therapeutic agent. The difficulty in application remains in delivering the catalase enzyme to the appropriate site in adequate amounts. Poly lactic co-glycolic acid nanoparticles have been used for delivering catalase to human neuronal cells, and the protection by these catalase-loaded nanoparticles against oxidative stress was evaluated [ ].

The nanoparticle-loaded catalase showed significant positive effect on neuronal cells preexposed to hydrogen peroxide reducing the hydrogen peroxide-mediated protein oxidation, DNA damage, mitochondrial membrane transition pore opening, and loss of membrane integrity. Thus, the study suggests that nanoparticle-loaded catalase may be used as a therapeutic agent in oxidative stress-related neurological diseases [ ]. EUK is a salen-manganese complex which has both high catalase and superoxide dismutase activity.

It was concluded from these studies on the rat stroke model that EUK may play a protective role in management of this disease. To study the effect of these fusion proteins under oxidative stress conditions, mammalian cell lines HeLa, PC12 were transduced with purified fusion Tat-CAT and 9Arg-CAT protein and these cells were exposed to hydrogen peroxide. It was found that the viability of the transduced cells increased significantly. It was also observed that when the Tat-CAT and 9Arg-CAT fusion proteins were sprayed over animal skin, it could penetrate the epidermis and dermis layers of the skin.

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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Journal of Applied Animal Research , 48 1 , You should have seen more foam being produced once you added another tablespoon of hydrogen peroxide to cup one, which should have resulted in a similar amount of foam as in cup two. However, at some point you will reach a substrate concentration at which the enzyme gets saturated and becomes the limiting factor.

In this case you have to add more enzyme to speed up the reaction again. Many other factors affect the activity of enzymes as well. Most enzymes only function under optimal environmental conditions. If the pH or temperature deviates from these conditions too much, the enzyme reaction slows down significantly or does not work at all.

You might have noticed that when doing the extra steps in the procedure. Cleanup Pour all the solutions into the sink and clean all the spoons with warm water and dish soap. Wipe your work area with a wet paper towel and wash your hands with water and soap. This activity brought to you in partnership with Science Buddies. Already a subscriber? Sign in. Thanks for reading Scientific American. Create your free account or Sign in to continue.

See Subscription Options. Go Paperless with Digital. Key concepts Biology Biochemistry Enzymes Physiology Chemistry Introduction Have you ever wondered how all the food that you eat gets digested? Materials Safety goggles or protective glasses Five teaspoons of dish soap One package of dry yeast Hydrogen peroxide, 3 percent at least mL Three tablespoons One teaspoon Five ounce disposable plastic cups Tap water Measuring cup Permanent marker Paper towel Workspace that can get wet and won't be damaged by any spilled hydrogen peroxide or food-colored water Food coloring optional Preparation Take one cup and dissolve the dry yeast in about one-half cup of warm tap water.

The water shouldn't be too hot but close to body temperature 37 Celsius. Let the dissolved yeast rest for at least five minutes. Use the permanent marker to label the remaining four cups from one to four. To all the labeled cups, add one teaspoon of dish soap. To cup one no further additions are made at this point.

Before using the hydrogen peroxide, put on your safety goggles to protect your eyes. In case you spill hydrogen peroxide, clean it up with a wet paper towel. If you get it on your skin, make sure to rinse the affected area with plenty of water. To cup two, add one tablespoon of 3 percent hydrogen peroxide solution.

Use a fresh spoon for the hydrogen peroxide. To cup three, add two tablespoons of the hydrogen peroxide. To cup four, add three tablespoons of the hydrogen peroxide. Optionally, you can add a drop of food color to each of the labeled cups. You can choose a different color for each one for easy identification Procedure Take cup number one and place it in front of you on the work area. With a fresh tablespoon, add one tablespoon of the dissolved yeast solution to the cup and swirl it slightly.

What happens after you add the yeast? Do you see a reaction happening? Place cup number two in front of you and again add one tablespoon of yeast solution to the cup. Once you add the enzyme, does the catalase react with the hydrogen peroxide? Can you see the reaction products being formed? Add one tablespoon of yeast solution to cup number three.