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PubMed2004

Overexpression of Cu/Zn-superoxide dismutase and/or catalase in mice inhibits aorta smooth muscle cell proliferation.

BACKGROUND: Increasing evidence demonstrates that reactive oxygen species, for example, superoxide (O(2)(-.)) and hydrogen peroxide (H(2)O(2)), promote vascular smooth muscle cell (VSMC) proliferation, and that superoxide dismutase (SOD) and catalase work in concert to scavenge O(2)(-.) and H(2)O(2). This report examined the effect of overexpressing Cu/Zn-SOD or catalase on epidermal growth factor (EGF)-induced proliferation and mitogen-activated protein kinase (MAPK) phosphorylation in VSMCs. METHODS: The VSMCs were obtained from the aorta of wild-type mice and transgenic mice overexpressing Cu/Zn-SOD and catalase in combination or overexpressing Cu/Zn-SOD or catalase alone. The VSMC proliferation was measured by cell counting and bromodeoxyuridine incorporation assay. The MAPK phosphorylation was determined with Western blotting. RESULTS: Treatment of wild-type VSMCs with EGF significantly increased proliferation and phosphorylation of extracellular signal-regulated kinases (ERK1/2) and p38 MAPK. Overexpression of Cu/Zn-SOD or catalase attenuated EGF-induced phosphorylation of ERK1/2 and p38 MAPK and suppressed EGF-induced proliferation in VSMCs. For example, the EGF-induced phosphorylation of ERK1/2 and p38 MAPK and EGF-induced proliferation in VSMCs overexpressing Cu/Zn-SOD or catalase were significantly less than in wild-type VSMCs. Moreover, VSMCs overexpressing Cu/Zn-SOD and catalase in combination showed significantly less proliferation and less phosphorylation of the MAPKs than those overexpressing Cu/Zn-SOD or catalase alone. CONCLUSIONS: Overexpression of Cu/Zn-SOD and catalase in combination is more efficient in inhibiting VSMC proliferation and MAPK phosphorylation than overexpression of Cu/Zn-SOD or catalase alone.

Animals↗
PubMed2004

Ethanol intake and motor sensitization: the role of brain catalase activity in mice with different genotypes.

The C57BL/6J strain of inbred mice shows a characteristic pattern of ethanol-induced behaviors: very weak acute locomotor stimulation, a lack of locomotor-sensitizing effect of ethanol, and a high level of ethanol intake. This strain has relatively low levels of activity of the ethanol metabolizing enzyme catalase, and it has been proposed that brain catalase plays a role in the modulation of some behavioral effects of ethanol. In the first study of the present paper, we investigated the effects of pharmacological manipulations of brain catalase activity on C57BL/6J mice in acute ethanol-induced locomotion and ethanol intake. Results indicated that the reduction in motor activity produced by ethanol was reversed by pretreatment with catalase potentiators and it was enhanced by catalase inhibitors. In addition, ethanol intake was highly correlated with brain catalase activity in mice treated with a catalase potentiator. In the second study, F1 hybrid mice (SWXB6) from the outbred Swiss-Webster mice and the inbred C57BL/6J mice were used. Basal brain catalase activity levels of F1 mice were intermediate between to those of the two progenitor genotypes. That profile of catalase activity was parallel to the acute-ethanol-induced locomotion and to repeated-ethanol-induced motor sensitization effects observed across the three types of mice. These data suggest that brain catalase activity modifications in the C57BL/6J strain change the pattern of several ethanol-related behaviors in this inbred mouse.

Alcohol Drinking↗
PubMed1998

Regulation of cyclo-oxygenase gene expression in rat smooth muscle cells by catalase.

We have studied, in detail, the effect of catalase, one of the naturally occurring antioxidant enzymes, on the expression of cyclo-oxygenase (COX) mRNA and protein in rat aortic smooth muscle cells (RASMC). The activity of COX enzyme within the cells was also determined. Catalase either alone or in combination with interleukin-1beta (IL-1beta) enhanced mRNA and protein expression for cyclo-oxygenase 2 (COX-2) in a concentration-dependent manner. However, it did not affect the expression of mRNA or protein for cyclo-oxygenase 1 (COX-1). The expression of mRNA for COX-2 induced by catalase was blocked completely by actinomycin D (ACT) or cycloheximide (CHX). In comparison, expression of mRNA for COX-2 stimulated by IL-1beta was inhibited by actinomycin D, but not by cycloheximide. This suggests that induction of the synthesis of mRNA for COX-2 by catalase and IL-1beta involves different mechanisms. In particular, the induction of mRNA for COX-2 by catalase requires on-going protein and RNA synthesis, but the induction following exposure to IL-1beta does not. The increase in expression of mRNA for COX-2 induced by catalase may be related to the ability of catalase to stimulate cyclic AMP response element (CRE) and NF-IL6 transcription factors, but not nuclear factor kappa B (NF-kappaB), for electrophoretic mobility shift assays (EMSA) showed that catalase enhanced nuclear factor binding to cyclic AMP response element and NF-IL6 but not to NF-kappaB. Catalase exerted a biphasic effect on prostaglandin synthesis. At low concentrations it enhanced prostaglandin production, but at high concentrations it tended to inhibit it. These findings suggest that catalase has differential and multiple effects on COX expression and activity in rat aortic smooth muscle cells.

Animals↗
PubMed1996

Inhibition of catalase in mesencephalic cultures by L-DOPA and dopamine.

Catalase activity in cell cultures of fetal rat mesencephalon was decreased by 42 and 50%, respectively, after exposure to L-3,4-dihydroxyphenylalanine (L-DOPA, 100 microM) or dopamine (100 microM) for 48 h. Catalase activity was also decreased 21% by 10 microM hydroquinone. Ascorbic acid (200 microM), an agent that suppresses the autoxidation of L-DOPA and dopamine, blocked the anti-catalase effect of L-DOPA, but not that of dopamine. Inhibitors of the A and B forms of monoamine oxidase (20 microM clorgyline plus 20 microM pargyline) had no effect on the anti-catalase action of either L-DOPA or dopamine. The latter results suggest that products of the oxidative deamination of dopamine by monoamine oxidase are not involved in the suppression of catalase activity. However, autoxidation reactions of L-DOPA may play a role since ascorbate suppressed the anti-catalase effect of L-DOPA. On the contrary, the basis for the failure of ascorbate to similarly block the anti-catalase effect of dopamine is uncertain. L-DOPA and dopamine (25 microM) also inhibited crystalline catalase in solution after incubation for 1 h at neutral pH (40-50% inhibition). Inhibition was blocked by 0.45 M ethanol, indicating a need for autoxidation and the formation of compound II, which is an enzymatically inactive form of catalase. The ability to model the enzyme inhibition in purely chemical experiments indicates a probable mechanism for loss of enzymatic activity in cell cultures. Inhibition of catalase may contribute to cell damage during incubation of cultures with L-DOPA, dopamine, or other autoxidizable compounds.

Animals↗
PubMed1997

Comparison of catalase in diploid and haploid Rana rugosa using heat and chemical inactivation techniques.

The present study examines differences in the hydrogen peroxide (H2O2) detoxifying enzyme, catalase, found in the tails and livers of diploid and haploid Rana rugosa. Investigative techniques include measurement of catalase activity and tests for temperature stability and chemical inhibition. Catalase from the tails of pre-climactic (stage XXIII) haploids was found to be over three times as H2O2 destructive as catalase from similar tails of diploids. Catalase from the livers of newly metamorphosed (stage XXV) froglets, on the other hand, displayed only one third the activity seen in diploid livers. The catalase in haploid tail and liver proved to be more heat resistant, retaining 40-60% of its original activity after 5 min of treatment at 55 degrees C, whereas diploid catalase was totally inactivated under the same conditions. Haploid and diploid catalase also responded differently to inhibition using urea and aminotriazole. These differences suggest that haploid catalase has diverged from normal diploid catalase through molecular modification, resulting in abnormal systems for H2O2 metabolism, which in turn are thought to be responsible for organ dysfunction and early death seen in haploid individuals.

Amitrole↗
PubMed1999

Reduced levels of catalase activity potentiate MPP+-induced toxicity: comparison between MN9D cells and CHO cells.

1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) has been shown to be toxic by inducing oxygen free radicals in the mammalian nervous system, especially in the nigrostriatal dopaminergic system. The present study was designed to compare the toxic effects of MPP+, the active metabolite of MPTP, in MN9D neuronal cells that exhibit relatively low levels of catalase activity, as compared to CHO cells, which exhibit high levels of catalase activity. The survival of the MN9D cells in the presence of 250 microM MPP+ was less than 10%, whereas CHO cells exhibited 70% survival at the same concentration of MPP+. The ED50 values of MPP+ in MN9D and CHO cell lines were 60-600 microM, respectively. MN9D cells contain less catalase, an enzyme believed to be involved in the detoxification of free radicals compared to CHO cells. The catalase activity was 2 Units/mg protein in MN9D cells and 30 U/mg protein in CHO cells. The catalase activity in CHO cells increased with increasing MPP+ concentrations from 100-500 microM, however, it decreased at 1 mM MPP+. In contrast, catalase activity in MN9D remained the same at all MPP+ concentrations. When the CHO cells were pre-treated with 10-25 mM 3-aminotriazole (3-AT), which inhibits catalase activity, and exposed to MPP+ at various concentrations, they became susceptible to MPP+. It is evident from these data that the differential susceptibility to MPP+ in these two cell lines are due to differences in catalase activity. In addition, the inhibition of constituentive catalase activity in CHO cells by 3-AT treatment enhances their susceptibility. In conclusion, the study demonstrates that catalase activity represents an important defence mechanism in MPTP-induced toxicity.

1-Methyl-4-phenylpyridinium↗
PubMed1999

Maternal administration of superoxide dismutase and catalase in phenytoin teratogenicity.

Embryonic bioactivation and formation of reactive oxygen species (ROS) are implicated in the mechanism of phenytoin teratogenicity. This in vivo study in pregnant CD-1 mice evaluated whether maternal administration of the antioxidative enzymes superoxide dismutase (SOD) and/or catalase conjugated with polyethylene glycol (PEG) could reduce phenytoin teratogenicity. Initial studies showed that pretreatment with PEG-SOD alone (0.5-20 KU/kg i.p. 4 or 8 h before phenytoin) actually increased the teratogenicity of phenytoin (65 mg/kg i.p. on gestational days [GD] 11 and 12, or 12 and 13) (p < .05), and appeared to increase embryonic protein oxidation. Combined pretreatment with PEG-SOD and PEG-catalase (10 KU/kg 8 or 12 h before phenytoin) was not embryo-protective, nor was PEG-catalase alone, although PEG-catalase alone reduced phenytoin-initiated protein oxidation in maternal liver (p < .05). However, time-response studies with PEG-catalase (10 KU/kg) on GDs 11, or 11 and 12, showed maximal 50-100% increases in embryonic activity sustained for 8-24 h after maternal injection (p < .05), and dose-response studies (10-50 KU/kg) at 8 h showed maximal respective 4-fold and 2-fold increases in maternal and embryonic activities with a 50 KU/kg dose (p < .05). In controls, embryonic catalase activity was about 4% of that in maternal liver, although with catalase treatment, enhanced embryonic activity was about 2% of enhanced maternal activity (p < .05). PEG-catalase pretreatment (10-50 KU/kg 8 h before phenytoin) also produced a dose-dependent inhibition of phenytoin teratogenicity, with maximal decreases in fetal cleft palates, resorptions and postpartum lethality at a 50 KU/kg dose (p < .05). This is the first evidence that maternal administration of PEG-catalase can substantially enhance embryonic activity, and that in vivo phenytoin teratogenicity can be modulated by antioxidative enzymes. Both the SOD-mediated enhancement of phenytoin teratogenicity, and the inhibition of phenytoin teratogenicity by catalase, indicate a critical role for ROS in the teratologic mechanism, and the teratologic importance of antioxidative balance.

Abnormalities, Drug-Induced↗
PubMed1995

Crystal structure of catalase HPII from Escherichia coli.

BACKGROUND: Catalase is a ubiquitous enzyme present in both the prokaryotic and eukaryotic cells of aerobic organisms. It serves, in part, to protect the cell from the toxic effects of small peroxides. Escherichia coli produces two catalases, HPI and HPII, that are quite distinct from other catalases in physical structure and catalytic properties. HPII, studied in this work, is encoded by the katE gene, and has been characterized as an oligomeric, monofunctional catalase containing one cis-heme d prosthetic group per subunit of 753 residues. RESULTS: The crystal structure of catalase HPII from E. coli has been determined to 2.8 A resolution. The asymmetric unit of the crystal contains a whole molecule, which is a tetramer with accurate 222 point group symmetry. In the model built, that includes residues 27-753 and one heme group per monomer, strict non-crystallographic symmetry has been maintained. The crystallographic agreement R-factor is 20.1% for 58,477 reflections in the resolution shell 8.0-2.8 A. CONCLUSIONS: Despite differences in size and chemical properties, which were suggestive of a unique catalase, the deduced structure of HPII is related to the structure of catalase from Penicillium vitale, whose sequence is not yet known. In particular, both molecules have an additional C-terminal domain that is absent in the bovine catalase. This extra domain contains a Rossmann fold but no bound nucleotides have been detected, and its physiological role is unknown. In HPII, the heme group is modified to a heme d and inverted with respect to the orientation determined in all previously reported heme catalases. HPII is the largest catalase for which the structure has been determined to almost atomic resolution.

Amino Acid Sequence↗
PubMed2003

Catalase is regulated by ubiquitination and proteosomal degradation. Role of the c-Abl and Arg tyrosine kinases.

Catalase is a major effector in the defense of aerobic cells against oxidative stress. Recent studies have shown that catalase activity is stimulated by the c-Abl and Arg tyrosine kinases. Little, however, is otherwise known about the mechanisms responsible for catalase regulation. The present work demonstrates that mouse cells deficient in both c-Abl and Arg exhibit increased catalase stability. The results also show that catalase is subject to ubiquitination and degradation by the 26S proteosome. Significantly, ubiquitination of catalase is dependent on c-Abl- and Arg-mediated phosphorylation of catalase on both Y231 and Y386. In concert with these results, human 293 cells expressing catalase mutated at Y231 and Y386 exhibit attenuated levels of reactive oxygen species when exposed to hydrogen peroxide. These findings indicate that, in addition to stimulating catalase activity, c-Abl and Arg promote catalase degradation in the oxidative stress response.

Animals↗
PubMedDate not supplied

Purification and characterization of a novel thermo-alkali-stable catalase from Thermus brockianus.

A novel thermo-alkali-stable catalase from Thermus brockianus was purified and characterized. The protein was purified from a T. brockianus cell extract in a three-step procedure that resulted in 65-fold purification to a specific activity of 5300 U/mg. The enzyme consisted of four identical subunits of 42.5 kDa as determined by SDS-PAGE and a total molecular mass measured by gel filtration of 178 kDa. The catalase was active over a temperature range from 30 to 94 degrees C and a pH range from 6 to 10, with optimum activity occurring at 90 degrees C and pH 8. At pH 8, the enzyme was extremely stable at elevated temperatures with half-lives of 330 h at 80 degrees C and 3 h at 90 degrees C. The enzyme also demonstrated excellent stability at 70 degrees C and alkaline pH with measured half-lives of 510 h and 360 h at pHs of 9 and 10, respectively. The enzyme had an unusual pyridine hemochrome spectrum and appears to utilize eight molecules of heme c per tetramer rather than protoheme IX present in the majority of catalases studied to date. The absorption spectrum suggested that the heme iron of the catalase was in a 6-coordinate low spin state rather than the typical 5-coordinate high spin state. A K(m) of 35.5 mM and a V(max) of 20.3 mM/min.mg protein for hydrogen peroxide was measured, and the enzyme was not inhibited by hydrogen peroxide at concentrations up to 450 mM. The enzyme was strongly inhibited by cyanide and the traditional catalase inhibitor 3-amino-1,2,4-triazole. The enzyme also showed no peroxidase activity to peroxidase substrates o-dianisidine and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), a trait of typical monofunctional catalases. However, unlike traditional monofunctional catalases, the T. brockianus catalase was easily reduced by dithionite, a characteristic of catalase-peroxidases. The above properties indicate that this catalase has potential for applications in industrial bleaching processes to remove residual hydrogen peroxide from process streams.

Alkalies↗
PubMed2026

A redox-regulated RCC1-like protein controls catalase activity in Arabidopsis.

Reactive oxygen species (ROS) regulate plant growth and stress responses. Catalases play a central role in detoxifying hydrogen peroxide, predominantly within peroxisomes, yet key aspects of catalase regulation remain incompletely understood. Using affinity purification of the UV-B photoreceptor UVR8 coupled with mass spectrometry, we identified CATALASE-INTERACTING RCC1-LIKE 1 (CAIR1), which interacts with all three Arabidopsis catalases and their chaperone NO CATALASE ACTIVITY 1. Loss of CAIR1 reduces catalase activity and causes oxidative stress sensitivity, impaired root growth, and alkaline sensitivity, resembling cat2 and nca1 mutants. CAIR1 promotes peroxisomal import and proper localization of CAT2, preventing CAT2 aggregation and maintaining its activity. CAIR1 undergoes reversible redox-dependent oligomerization that enhances catalase binding, whereas mutation of Cys-356 and Cys-545 compromises this interaction and fails to rescue the oxidative stress sensitivity of cair1 mutants. UV-B weakens CAIR1-catalase interactions and suppresses catalase activity, linking light signalling with redox homeostasis. These findings identify CAIR1 as a redox-responsive regulator of catalase localization and activity.

Arabidopsis↗
PubMed2003

A comparative study between catalase gene therapy and the cardioprotector monohydroxyethylrutoside (MonoHER) in protecting against doxorubicin-induced cardiotoxicity in vitro.

Cardiotoxicity is the main dose-limiting side effect of doxorubicin in the clinic. Being a free radical producer, doxorubicin affects the heart specifically because of its low antioxidant capacity. Among those antioxidants, catalase is present in very low levels in the heart compared to other organs. Since catalase is an essential enzyme in detoxifying hydrogen peroxide, the aim of the present study was to investigate the protective effect of catalase as delivered by an adenovirus vector against doxorubicin-induced cardiotoxicity in cultured neonatal rat cardiac myocytes (NeRCaMs). 7-Monohydroxyethylrutoside (MonoHER), a potent cardioprotector currently under clinical investigations, was included in the study as a reference. Neonatal rat cardiac myocytes were infected with different multiplicity of infections (MOIs) of adenovirus encoding catalase (AdCat). A control infection with an adenovirus vector encoding a nonrelated protein was included. The activity and content of catalase in infected cells were determined during 3 days postinfection. One group of NeRCaMs was infected with AdCat before treatment with doxorubicin (0-50 microM). The second and third group were treated with doxorubicin (0-50 microM) with and without 1 mM monohydroxyethylrutoside (monoHER), respectively. The LDH release and viability of treated cells were measured 24 and 48 h after doxorubicin treatment. The beating rate was followed in three other groups of cells receiving the same treatments within 3 days after doxorubicin (0-100 microM) treatment. Catalase activity increased in AdCat-infected cells, with different MOIs, starting from the second day after infection as compared to the mock-infected cells (P<0.03). At the third day of infection, an MOI of more than 50 caused cytopathic effects, which hampered the use of higher viral titres. With an MOI of 50, catalase activity increased 3.5-fold in AdCat-infected cells 3 days postinfection (P=0.021) compared to mock-infected cells. The beating rate and survival of NeRCaMs decreased in a concentration and time-dependent manner after doxorubicin treatment (P<0.0005). This cytotoxicity was associated with an increase in the LDH release from the treated cells (P<0.0005). The cells stopped beating 24 h after treatment with >50 microM doxorubicin. A 3.5-fold increase in the activity of catalase did not protect NeRCaMs against any of the cytotoxic effects of doxorubicin on NeRCaMs. In contrast, monoHER (1 mM) significantly protected NeRCaMs against the lethal effects of doxorubicin on the survival, LDH release and the beating rate of NeRCaMs (P<0.004) during 48 h after doxorubicin treatment. This protection resulted in a prolongation of the beating of doxorubicin-treated cells after the end of the experiment (i.e. >72 h). The present study (1) illustrates that the cytotoxicity of high MOI of AdCat (>50) limited the possibility to increase catalase activity more than 3.5-fold, which was not enough to protect infected NeRCaMs against doxorubicin-induced cardiotoxicity and (2) confirms the efficacy of monoHER as a cardioprotector. Thus, the use of monoHER proves more suitable for the prevention of doxorubicin-induced cardiotoxicity than catalase gene transfer employing adenovirus vectors.

Adenoviridae↗
PubMed1998

Identification and characterization of autoantibodies against catalase and alpha-enolase in patients with primary sclerosing cholangitis.

Primary sclerosing cholangitis (PSC) is a chronic cholestatic liver disease of unknown aetiology. Recent studies have shown that genetic factors and both cellular and humoral immunological abnormalities are important in the pathogenesis of PSC. The most prominent autoantibodies in PSC are anti-neutrophil cytoplasmic antibodies (ANCA). The autoepitopes of ANCA in PSC are not well defined. The aim of this study was to identify corresponding ANCA autoantigens in patients with PSC. A biochemical approach with enrichment and partial purification of soluble neutrophil proteins, detection of autoantibodies by Western blot and partial amino acid sequencing were used. Two new autoantigen/autoantibody systems in patients with PSC were detected: catalase and alpha-enolase. The presence of catalase autoantibodies in 9/15 (60%) and alpha-enolase autoantibodies in 4/15 (27%) was confirmed by ELISA and Western blot. Furthermore, we showed immunoreactions of PSC sera with human biliary epithelial cells, showed the reduction of fluorescence in anti-catalase absorption experiments and observed partial co-localization of anti-catalase antibodies and PSC sera in double-staining experiments on biliary epithelial cells. The anti-catalase antibody-positive PSC patients had a more severe course of disease with a significantly higher alkaline phosphatase compared with the anti-catalase-negative PSC patients (P < 0.06). All ulcerative colitis control sera were anti-catalase antibody-negative. The identified antigens catalase and alpha-enolase can partly explain the ANCA fluorescence on ethanol-fixed and formaldehyde-fixed granulocytes in patients with PSC. Catalase is an important anti-oxidant enzyme and prevents cell damage from highly reactive oxygen-derived free radicals. Catalase autoantibodies might play a pathogenic role in patients with PSC. Our findings support the hypothesis that oxidative stress is one of the pathogenic mechanisms in patients with PSC.

Amino Acid Sequence↗
PubMed1999

Overexpression of catalase in cytosolic or mitochondrial compartment protects HepG2 cells against oxidative injury.

HepG2 cells were transfected with vectors containing human catalase cDNA and catalase cDNA with a mitochondrial leader sequence to allow comparison of the effectiveness of catalase overexpressed in the cytosolic or mitochondrial compartments to protect against oxidant-induced injury. Overexpression of catalase in cytosol and in mitochondria was confirmed by Western blot, and activity measurement and stable cell lines were established. The intracellular level of H(2)O(2) induced by exogenously added H(2)O(2) or antimycin A was lower in C33 cell lines overexpressing catalase in the cytosol and mC5 cell lines overexpressing catalase in the mitochondria as compared with Hp cell lines transfected with empty vector. Cell death caused by H(2)O(2), antimycin A, and menadione was considerably suppressed in both the mC5 and C33 cell lines. C33 and mC5 cells were also more resistant to apoptosis induced by H(2)O(2) and to the loss of mitochondrial membrane potential induced by H(2)O(2) and antimycin A. In view of the comparable protection by catalase overexpressed in the cytosol versus the mitochondria, catalase produced in both cellular compartments might act as a sink to decompose H(2)O(2) and move diffusable H(2)O(2) down its concentration gradient. The present study suggests that catalase in cytosol and catalase in mitochondria are capable of protecting HepG2 cells against cytotoxicity or apoptosis induced by oxidative stress.

Antimycin A↗
PubMed1997

Zinc induces catalase expression in cultured fetal human retinal pigment epithelial cells.

PURPOSE: We have previously shown that an experimental, low-zinc environment decreased catalase activity in cultured human fetal retinal pigment epithelial (RPE) cells. The purpose of this study was to investigate the effect of zinc supplementation on catalase expression in cultured human fetal RPE cells. METHODS: Confluent fetal RPE cells incubated in Coon's modified Ham's F12 (CMF-12) were treated (18 h) with zinc chloride (ZnCl2) (15, 30, or 100 microM) to assess changes in catalase enzyme activity or for 6 h to assess the induction of catalase mRNA by Northern analysis and in situ hybridization. RPE cells were also treated with 30 microM ZnCl2 for 2, 6, 24, 48 and 72 h to assess the time course of changes in catalase enzyme activity, changes in mRNA levels and status of the Sp1 transcription factor. RESULTS: Catalase activity was increased above control by the addition of 15, 30 and 100 microM ZnCl2. Catalase gene expression was induced by 30 microM zinc in 6 h, but decreased to non-treated control levels by 24 h. The transcription factor Sp1 was also activated by zinc treatment (30 microM) which peaked at 2 h and declined to non-treated control levels by 24 h. Catalase enzyme activity peaked at 24 h and decreased to control levels by 72 h. CONCLUSIONS: Our results demonstrate that zinc treatment of RPE cells increases catalase expression and activates the transcription factor Sp1. The results suggest zinc may play a role in the transcriptional regulation of catalase in RPE cells.

Blotting, Northern↗
PubMed1974

Nafenopin-induced hepatic microbody (peroxisome) proliferation and catalase synthesis in rats and mice. Absence of sex difference in response.

Nafenopin (2-methyl-2[p-(1,2,3,4-tetrahydro-1-naphthyl)phenoxy]-propionic acid; Su-13437), a potent hypolipidemic compound, was administered in varying concentrations in ground Purina Chow to male and female rats, wild type (Cs(a) strain) mice and acatalasemic (Cs(b) strain) mice to determine the hepatic microbody proliferative and catalase-inducing effects. In all groups of animals, administration of nafenopin at dietary levels of 0.125% and 0.25% produced a significant and sustained increase in the number of peroxisomes. The hepatic microbody proliferation in both male and female rats and wild type Cs(a) strain mice treated with nafenopin was of the same magnitude and was associated with a two-fold increase in catalase activity and in the concentration of catalase protein. The increase in microbody population in acatalasemic mice, although not accompanied by increase in catalase activity, was associated with a twofold increase in the amount of catalase protein. The absence of sex difference in microbody proliferative response in nafenopin-treated rats and wild type mice is of particular significance, since ethyl-alpha-p-chlorophenoxyisobutyrate (CPIB)-induced microbody proliferation and increase in catalase activity occurred only in males. Nafenopin can, therefore, be used as an inducer of microbody proliferation and of catalase synthesis in both sexes of rats and mice. The serum glycerol-glycerides were markedly lowered in all the animals given nafenopin, which paralleled the increase in liver catalase. All the above effects of nafenopin were fully reversed when the drug was withdrawn from the diet of male rats. During reversal, several microbody nucleoids were seen free in the hyaloplasm or in the dilated endoplasmic reticulum channels resulting from a rapid reduction in microbody matrix proteins after the withdrawal of nafenopin from the diet. Because of microbody proliferation and catalase induction with increasing number of hypolipidemic compounds, additional studies are necessary to determine the interrelationships of microbody proliferation, catalase induction, and hypolipidemia.

Animals↗
PubMed1990

Modulation of catalase activities in murine epidermal cells as a function of differentiation and exposure to 12-O-tetradecanoylphorbol-13-acetate.

A procedure was developed for the per cell estimation of catalase activities in suspensions and cultures of murine epidermal keratinocytes (MEKs). Per cell catalase activity in MEKs cultured in low Ca2+ medium was relatively constant during the proliferation phase of culturing, but increased approximately 100% within 24 h of cessation of cell division. 12-O-Tetradecanoylphorbol-13-acetate (TPA) treatment of proliferating MEKs cultured in low Ca2+ medium resulted in (i) an initial suppression of proliferation, (ii) the accelerated detachment and differentiation of detached MEKs and (iii) a suppression of catalase induction in the detached population. Induction of MEK differentiation by raising the medium Ca2+ concentration resulted in rapid inhibition of cell division and approximately 200% increases in per cell catalase activities. Addition of TPA immediately prior to Ca2+ shift completely suppressed the Ca2(+)-dependent increases in activity. However, the addition of TPA 48 h after the induction of differentiation by Ca2+ shift had no effects on the elevated, pre-existing catalase activities. Per cell catalase activities varied in vivo with the stage of MEK differentiation. Specifically, the lowest and highest per cell activities (approximately 4-fold difference) were measured in enriched basal cell and spinous cell populations respectively. Catalase activity in the more differentiated MEKs was reduced approximately 33% within 24 h of topical treatment of dorsal skin with a promoting dose of TPA. However, catalase activity in enriched basal cell preparations was unaffected. Collectively, these studies demonstrate that per cell catalase activities increase as MEKs differentiate, and that TPA suppresses the increases in catalase activities that normally occur during differentiation.

Animals↗
PubMed1997

Catalase is a sink for H2O2 and is indispensable for stress defence in C3 plants.

Hydrogen peroxide (H2O2) has been implicated in many stress conditions. Control of H2O2 levels is complex and dissection of mechanisms generating and relieving H2O2 stress is difficult, particularly in intact plants. We have used transgenic tobacco with approximately 10% wild-type catalase activity to study the role of catalase and effects of H2O2 stress in plants. Catalase-deficient plants showed no visible disorders at low light, but in elevated light rapidly developed white necrotic lesions on the leaves. Lesion formation required photorespiratory activity since damage was prevented under elevated CO2. Accumulation of H2O2 was not detected during leaf necrosis. Alternative H2O2-scavenging mechanisms may have compensated for reduced catalase activity, as shown by increased ascorbate peroxidase and glutathione peroxidase levels. Leaf necrosis correlated with accumulation of oxidized glutathione and a 4-fold decrease in ascorbate, indicating that catalase is critical for maintaining the redox balance during oxidative stress. Such control may not be limited to peroxisomal H2O2 production. Catalase functions as a cellular sink for H2O2, as evidenced by complementation of catalase deficiency by exogenous catalase, and comparison of catalase-deficient and control leaf discs in removing external H2O2. Stress analysis revealed increased susceptibility of catalase-deficient plants to paraquat, salt and ozone, but not to chilling.

Ascorbate Peroxidases↗