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Suppression of intracellular hydrogen peroxide generation and catalase levels in CD8+ T-lymphocytes from HIV+ individuals.

CD8+ T-lymphocytes from HIV+ individuals contain short telomeres, a sign of cell senescence. To test our hypothesis that the cell type is functionally defective in the biochemical indices related to cell proliferation, we investigated the profiles of intracellularly generated H2O2 levels with or without PMA as well as immunoreactive catalase levels using flow cytometric method. We observed that, in HIV+ but not in HIV- individuals, the constitutively generated H2O2 level was significantly lower in CD8+ T-cells compared with CD4+ T-cells. Importantly, activated effector CD8+CD28- cells showed remarkably low H2O2 levels compared with CD8+CD28+ cells, and the latter in HIV+ individuals also showed low levels. A similar defect of CD8+ cells of HIV+ individuals was also seen with H2O2 levels stimulated with PMA in the presence of a catalase inhibitor. Furthermore, the immunoreactive catalase content was lower in CD8+ cells compared with CD4+ cells only in HIV+ individuals. These results suggest that CD8+ T-lymphocytes are functionally defective with the constitutively generated and PMA-elicited levels of H2O2 and the corresponding scavenger. Diminished immunocompetence of HIV+ individuals may be caused, in part, by the functional defect of CD8+ T-cells.

Adult↗

Effect of the in vivo catalase inhibition on aminonucleoside nephrosis.

Reactive oxygen species have been involved in the pathophysiology of puromycin aminonucleoside (PAN)-nephrosis. The role of H2O2 in these rats may be studied modulating the amount or activity of catalase, which breakdowns H2O2 to water and oxygen. To explore the role of H2O2 in this experimental model, we studied the effect of the in vivo catalase inhibiton with 3-amino-1,2,4-triazole (ATZ) on the course of PAN-nephrosis. Four groups of rats were studied: control rats (CT group), PAN-injected rats (PAN group), ATZ-injected rats (ATZ group), and ATZ- and PAN-injected rats (ATZPAN group). Rats were placed in metabolic cages to collect 24 h urine along the study, ATZ (1 g/kg) was given 24 h before PAN injection (75 mg/kg), and the proteinuria was measured on days 0, 2, 4, 6, 8, and 10. Proteinuria started before (day 4) and was significantly higher on days 6, 8, and 10 in the ATZPAN group than in the PAN group. On day 10, hypercholesterolemia was significantly higher in the ATZPAN group than in the PAN group. These data indicate that the in vivo catalase inhibition magnifies PAN-nephrosis, suggesting that H2O2 is produced in vivo and involved in the renal damage in this experimental disease.

Amitrole↗

Retroviral-mediated correction of DNA repair defect in xeroderma pigmentosum cells is associated with recovery of catalase activity.

Xeroderma pigmentosum (XP) is a rare inherited disease associated with photosensitivity, a very high susceptibility to develop neoplasm on sun-exposed skin and neurological abnormalities for some patients. We previously reported that diploid cell lines established from XP skin biopsies present an abnormal low level of catalase activity, which is involved in the defense against oxygen free radicals. This biochemical dysfunction, probably involved in the skin cancer formation, has been difficult to be directly related to the nucleotide excision repair (NER) defect in XP. In this paper we report that the retroviral-mediated transduction of XP diploid cells by the XPC and XPD/ERCC2 cDNAs fully and stably corrects the NER defect in terms of survival and unscheduled DNA synthesis (UDS) after ultraviolet (UV) irradiation. The catalase activity in transduced cells was recovered up to normal levels only in cells transduced with repair genes correcting the repair defect. These results imply that: (i) the reduced catalase activity in XP, which might result from cellular depletion of its NADPH cofactor, is directly related to impaired DNA repair, and (ii) this depletion might be one of the multiple cellular consequences of XP inborn defect.

Catalase↗

Protective effects of ibuprofen and its major metabolites against in vitro inactivation of catalase and fumarase: relevance to cataract.

Ibuprofen and its major metabolites were incubated with catalase and fumarase, in the presence of protein-modifying biomolecules, to explore the mode of action of ibuprofen in protection against cataract. Both 2 and 10 mM ibuprofen/metabolites protected catalase against fructose-, cyanate- and prednisolone-induced inactivation; the carboxy-metabolite gave the highest protection (31%). The 2 mM ibuprofen/metabolites protected fumarase against fructose- and cyanate-induced inactivation by up to 26%, but had no effect on prednisolone-induced inactivation. Ibuprofen/metabolites did not bind to catalase or fumarase. They penetrated into the lens in vitro. When in the lens, the metabolites may reduce the risk of cataract by protecting lenticular enzymes.

Animals↗

Characterization of hydrogen peroxide removal activities in mouse hemolysates: catalase activity and hydrogen peroxide removal activity by hemoglobin.

Hydrogen peroxide removal activities in normal and acatalasemic mouse hemolysates were examined to determine the optimal temperature of catalase. From thermal stability of the removal activities in hemolysates, the removal activities were divided into two activities. The removal activity deactivated at lower temperature was catalase, and the 50% inactivation was observed after 10 min incubation at 47.2 +/- 0.5 degrees C for normal hemolysates and 34.0 +/- 0.8 degrees C for acatalasemic ones. The removal activity deactivated at a higher temperature remained after the addition of sodium azide, and the 50% inactivation was observed at 63.5 +/- 1.4 degrees C. After separation of the removal activities by carboxymethyl-cellulose column chromatography, the removal activity deactivated at higher temperature was attributed to the activity by hemoglobin. From Lineweaver-Burk plot analysis of the removal rates by hemoglobin at 37 degrees C, the Michaelis constant for hydrogen peroxide and the maximum velocity were 201 +/- 53 microM and 5.37 +/- 1.39 micromol/s per g of Hb, respectively. Removal rates by hemoglobin in mouse hemolysates at 37 degrees C in 70 microM hydrogen peroxide were 1.32 +/- 0.12 micromol/s per g of Hb. Catalase activity (k/g Hb: rate constant related to the hemoglobin content) in normal mouse hemolysates was 104 +/- 12 at 25 degrees C and 117 +/- 10 at 37 degrees C, and that in acatalasemic hemolysates was 10.5 +/- 1.7 at 25 degrees C. These results indicate that activity of hydrogen peroxide removal by hemoglobin is substantial and the activity in acatalasemic hemolysates is predominant at low concentration of hydrogen peroxide.

Acatalasia↗

UV photolysis of catalase revisited: a spectral study of photolytic intermediates.

The 365-nm irradiation of 4.6 microM (approximately equal to 1.1 mg/ml) catalase solutions in pH 7.4 phosphate buffer induces spectral modifications. Difference spectra show maxima at 434, 555, 584 nm at the beginning of the irradiation, then a final spectrum with a maximum at 568 nm and a shoulder at 530 nm is observed. These results suggest the formation of compound III (oxyferrous catalase) and compound II, respectively. In deaerated 0.1 M, pH 8.7 borate buffer, the ferrous catalase is characterized by maxima at 563 and 594 nm. Hydrogen donors such as ethyl alcohol, formate and p-cresol inhibit, but citrate ions enhance the formation of these intermediates. A mechanism involving Fe(III) reduction according to an internal electron transfer is proposed.

Animals↗

Effects of glutathione peroxidase and catalase on hemolysis and methemoglobin modifications induced by photooxidized psoralen.

Psoralen photooxidation products (POP products) were obtained by UVA irradiation (365 nm, 180-640 W/m2) of an aqueous psoralen solution with fluences of 0-800 kJ/m2. Preincubation of POP products with glutathione peroxidase (GSHPer) or catalase, as well as presence of catalase during UVA irradiation of the aqueous psoralen solution did not influence their hemolytic activity. However, both GSHPer and catalase inhibited POP-induced conversion of methemoglobin. This indicates that hydrogen peroxide and psoralen peroxides destructible by GSHPer, which are being produced during psoralen photooxidation, do not possess hemolytic activity. Furthermore, hydrogen peroxide does not appear to serve as an intermediate in the process of hemolysin formation. Hydrogen peroxide generated during psoralen photooxidation is apparently the main POP product responsible for MetHb conversion.

Catalase↗

Catalase-negative Actinomyces neuii subsp. neuii isolated from an infected mammary prosthesis.

In this case report a catalase-negative strain of Actinomyces neuii subsp. neuii is described as the possible causative agent of an infected mammary prosthesis. DNA hybridization studies and 16S rRNA analysis confirmed that the strain belongs to the species Actinomyces neuii subsp. neuii. Since this strain is the first A. neuii subsp. neuii strain reported to be catalase negative, the catalase reaction should no longer be considered a key reaction for the diagnosis of this species but must be interpreted in conjunction with other characteristics.

Actinomyces↗

Catalase HPII of Escherichia coli catalyzes the conversion of protoheme to cis-heme d.

Catalase HPII from aerobically grown Escherichia coli normally contains heme d but cultures grown with poor or no aeration produce HPII containing a mixture of heme d and protoheme IX. The protoheme component of HPII from anaerobically grown cells is converted into heme d during treatment of the purified enzyme with hydrogen peroxide. It is concluded that heme d found in catalase HPII is formed by the cis-hydroxylation of protoheme in a reaction catalyzed by catalase HPII using hydrogen peroxide as a substrate. The distal His128 residue of HPII is absolutely required for the protoheme to heme d conversion. Two mutant enzymes, Ala128 and Asn128, are catalytically inactive and contain only protoheme, which is unaffected by hydrogen peroxide treatment. The Asn201 residue is not an absolute requirement for heme conversion. The mutant enzyme Ala201 contains predominantly heme d and is partially active. However, insertion of a histidyl residue to give the His201 enzyme interferes with the heme conversion reaction. This mutant form is isolated as a protoheme enzyme with limited activity, and a reversible conversion to a heme d-like species occurs in vitro in the presence of continuously generated hydrogen peroxide.

Amino Acid Sequence↗

The balance between Cu,Zn-superoxide dismutase and catalase affects the sensitivity of mouse epidermal cells to oxidative stress.

Oxidants are toxic, but at low doses they can stimulate rather than inhibit the growth of mammalian cells and play a role in the etiology of cancer and fibrosis. The effect of oxidants on cells is modulated by multiple interacting antioxidant defense systems. We have studied the individual roles and the interaction of Cu,Zn-superoxide dismutase (SOD) and catalase (CAT) in transfectants with human cDNAs of mouse epidermal cells JB6 clone 41. Since only moderate increases in these enzymes are physiologically meaningful, we chose the following five clones for in-depth characterization: CAT 4 and CAT 12 with 2.6-fold and 4.2-fold increased catalase activities, respectively, SOD 15 and SOD 3 with 2.3-fold and 3.6-fold increased Cu,Zn-SOD activities, respectively, and SOCAT 3 with a 3-fold higher catalase activity and 1.7-fold higher Cu,Zn-SOD activity than the parent JB6 clone 41. While the increases in enzyme activities were moderate, the human cDNAs were highly expressed in the transfectants. As demonstrated for the clone SOD 15, this discordance between message concentrations and enzyme activities may be due to the low stability of the human Cu,Zn-SOD mRNA in the mouse recipient cells. According to immunoblots the content of Mn-SOD was unaltered in the transfectants. While the activities of glutathione peroxidase were comparable in all strains, the concentrations of reduced glutathione (GSH) were significantly lower in SOD 3 and SOD 15. This decrease in GSH may reflect a chronic prooxidant state in these Cu,Zn-SOD overproducers.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

Formation of a tyrosyl radical intermediate in Proteus mirabilis catalase by directed mutagenesis and consequences for nucleotide reactivity.

Proteus mirabilis catalase (PMC) belongs to the family of NADPH binding catalases. The function of NADPH in these enzymes is still a matter of debate. This study presents the effects of two independent phenylalanine mutations (F194 and F215), located between NADPH and heme in the PMC structure. The phenylalanines were replaced with tyrosines which we predicted could carry radicals in a NADPH-heme electron transfer. The X-ray crystal structures of the two mutants indicated that neither the binding site of NADPH nor the immediate environment of the residues was affected by the mutations. Measurements using H2O2 as a substrate confirmed that the variants were as active as the native enzyme. With equivalent amounts of peroxoacetic acid, wild-type PMC, F215Y PMC, and beef liver catalase (BLC) formed a stable compound I, while the F194Y PMC variant produced a compound I which was rapidly transformed into compound II and a tyrosyl radical. EPR studies showed that this radical, generated by the oxidation of Y194, was not related to the previously observed radical in BLC, located on Y369. In the presence of excess NADPH, compound I was reduced to a resting enzyme (k(obs) = 1.7 min(-1)) in a two-electron process. This was independent of the enzyme's origin and did not require any thus far identified tyrosyl radicals. Conversely, the presence of a tyrosyl radical in F194Y PMC greatly enhanced the oxidation of reduced beta-nicotinamide mononucleotide under a steady-state H2O2 flow with observable compound II. This process could involve a one-electron reduction of compound I via Y194.

Animals↗

Hydroperoxidase II of Escherichia coli exhibits enhanced resistance to proteolytic cleavage compared to other catalases.

Catalase (hydroperoxidase) HPII of Escherichia coli is the largest catalase so far characterized, existing as a homotetramer of 84 kDa subunits. Each subunit has a core structure that closely resembles small subunit catalases, supplemented with an extended N-terminal sequence and compact flavodoxin-like C-terminal domain. Treatment of HPII with trypsin, chymotrypsin, or proteinase K, under conditions of limited digestion, resulted in cleavage of 72-74 residues from the N-terminus of each subunit that created a homotetramer of 76 kDa subunits with 80% of wild-type activity. Longer treatment with proteinase K removed the C-terminal domain, producing a transient 59 kDa subunit which was subsequently cleaved into two fragments, 26 and 32 kDa. The tetrameric structure was retained despite this fragmentation, with four intermediates being observed between the 336 kDa native form and the 236 kDa fully truncated form corresponding to tetramers with a decreasing complement of C-termini (4, 3, 2, and 1). The truncated tetramers retained 80% of wild-type activity. The T(m) for loss of activity during heating was decreased from 85 to 77 degrees C by removal of the N-terminal sequence and to 59 degrees C by removal of the C-terminal domain, revealing the importance of the C-terminal domain in enzyme stability. The sites of cleavage were determined by N- and C-terminal sequencing, and two were located on the surface of the tetramer with a third being exposed by removal of the C-terminal domain.

Amino Acid Sequence↗

Catalase-peroxidase active site restructuring by a distant and "inactive" domain.

Catalase-peroxidases are composed of two peroxidase-like domains. The N-terminal domain contains the heme-dependent, bifunctional active site. The C-terminal domain does not bind heme, has no catalytic activity, and is separated from the active site by >30 A. Nevertheless, without the C-terminal domain, the N-terminal domain exhibits neither catalase nor peroxidase activity due to the apparent coordination of the distal histidine to the heme iron. Here we report the ability of the separately expressed and isolated C-terminal domain (KatG(C)) to restructure the N-terminal domain (KatG(N)) to its bifunctional conformation. Addition of equimolar KatG(C) to KatG(N) decreased the hexacoordinate low-spin heme complex and increased the high-spin species (pentacoordinate and hexacoordinate). EPR spectra of the domain mixture showed a distribution between high-spin species nearly identical to that of wild-type KatG. The CD spectrum for the 1:1 physical mixture of the domains was identical to an arithmetic composite of individual spectra for KatG(N) and KatG(C). Both physical and arithmetic mixtures were nearly identical to the spectrum for wild-type KatG, suggesting that major shifts in secondary structure did not accompany active site reconfiguration. With the shift in heme environment, the parallel return of catalase and peroxidase activity was observed. Inclusion of bovine serum albumin instead of KatG(C) produced no activity, indicating that specific interdomain interactions were required to reestablish the bifunctional active site. Apparent constants for reactivation (k(react) approximately 4 x 10(-3) min(-1)) indicate that a slow process like movement of established structural elements may precede the restructuring of the heme environment and return of catalytic activity.

Binding Sites↗

Catalase HPII from Escherichia coli exhibits enhanced resistance to denaturation.

Catalase HPII from Escherichia coli is a homotetramer of 753 residue subunits. The multimer displays a number of unusual structural features, including interwoven subunits and a covalent bond between Tyr415 and His392, that would contribute to its rigidity and stability. As the temperature of a solution of HPII in 50 mM potassium phosphate buffer (pH 7) is raised from 50 to 92 degrees C, the enzyme begins to lose activity at 78 degrees C and 50% inactivation has occurred at 83 degrees C. The inactivation is accompanied by absorbance changes at 280 and 407 nm and by changes in the CD spectrum consistent with small changes in secondary structure. The subunits in the dimer structure remain associated at 95 degrees C and show a significant level of dissociation only at 100 degrees C. The exceptional stability of the dimer association is consistent with the interwoven nature of the subunits and provides an explanation for the resistance to inactivation of the enzyme. For comparison, catalase-peroxidase HPI of E. coli and bovine liver catalase are 50% inactivated at 53 and 56 degrees C, respectively. In 5.6 M urea, HPII exhibits a coincidence of inactivation, CD spectral change, and dissociation of the dimer structure with a midpoint of 65 degrees C. The inactive mutant variants of HPII which fold poorly during synthesis and which lack the Tyr-His covalent bond undergo spectral changes in the 78 to 84 degrees C range, revealing that the extra covalent linkage is not important in the enhanced resistance to denaturation and that problems in the folding pathway do not affect the ultimate stability of the folded structure.

Catalase↗

Effects of ionic and zwitterionic surfactants on the stabilization of bovine catalase.

The activity and stability of beef liver catalase have been investigated in the presence of different ionic and zwitterionic surfactants. All cationic and zwitterionic surfactants used in this work have no effect on the initial activity of catalase, but several of them allow the enzyme to retain a high residual activity for longer periods of time than those observed in the absence of any additives. However, the interactions between surfactants and catalase appear to be very peculiar, and certain zwitterionic surfactants have been found to remarkably slow down enzyme degradation, with the enzyme completely preserving its activity after several weeks at temperatures of up to 30 degrees C. This effect is probably due to an interaction between the surfactant and the intersubunit region of the protein; this interaction could stabilize the quaternary structure of the enzyme.

Animals↗

"Bridging hydroxide effect" on mu-carboxylato coordination and electrochemical potentials of bimetallic centers: Mn2(II,II) and Mn2(III,III) complexes as functional models of dimanganese catalases.

Synthesis, solution structures, and electrochemistry of several dinuclear Mn2(II,II) complexes (1-4) and Mn2(III,III) complexes (6 and 8), derived from a functional catalase mimic [(L1,2)Mn2(II,II)(mu 13-O2CCH3)]2+ (1) are described that enable testing of the role of intramolecular hydroxide ligands on the redox properties. Addition of 1 equiv of hydroxide to 1 or 3 forms [(L1,2)Mn2(II,II)(mu 13-O2CCH3)(mu- OH)]+ (7A or 7B, respectively), possessing two six-coordinate Mn(II) ions bridged by hydroxide and acetato ligands. Two-electron oxidation of 7 with O2 occurs by forming [(L1,2)Mn2(III,III)(mu 1,3-O2CCH3)(mu-OH)]3+ (8) and H2O2 with no ligand rearrangements in methanol. Reaction of 8 with 2-3 equiv hydroxide forms [(L1,2)Mn2(III,III)(mu-O)(OH)(O2CCH3)]+ in which deprotonation of mu-OH- to yield mu-O2- favors subsequent addition of a terminal hydroxide ligand, accommodated by a bridging-to-terminal "carboxylate-shift". Preservation of six-coordinate Mn(II) ions throughout all hydroxide-induced transformations is observed, including oxidation by O2. Cyclic voltammetry reveals that addition of mu-OH- converts the two-electron redox couple II,II/III,III for complexes 1-4 to sequential one-electron couples at lower reduction potentials, yielding substantial stabilization of the II,III and III,III oxidation states by delta E = 440 and 730 mV, respectively. Binding of a second OH- to 7A or 7B forms (L1,2)Mn2(II,II)(mu 13-O2CCH3)(OH)2, containing two six-coordinate Mn(II) ions with two terminal hydroxides and a mu 1,3-bridging acetato. Electrochemistry reveals that displacement of the bridging hydroxide to a terminal site upon addition of the second OH- restores a two-electron redox couple II,II/III,III but now at a higher reduction potential with considerable loss of the electrochemical stabilization energy provided by the mu-OH- (delta E = 250 and 350 mV loss for Mn2(II,II) and Mn2(III,III), (respectively). These results indicate a considerably stronger influence of bridging vs terminal hydroxide ligands in stabilizing the higher oxidation states and separating the one-electron redox potentials of bimetallic centers. By contrast, in the absence of mu-OH- bridges the longer separation with the mu 1,3-carboxylato bridge in dimanganese(II,II) complexes leads to nearly complete uncoupling of the Mn(II) oxidation potentials, thus yielding a two-electron redox transition to (III,III). We hypothesize that this "bridging hydroxide effect" may be due to both greater screening of the repulsive intermetallic electric potential energy and increased resonance stabilization of the mixed-valence (II,III) oxidation state by charge delocalization . These data provide a physicochemical basis for interpretation of the catalase activity of these complexes and of dimanganese catalase enzymes (see the following manuscript).

Catalase↗

Thermal stability of catalases active in dormant saffron (Crocus sativus L.) corms.

Catalase activity was detected in crude extract prepared from dormant saffron (Crocus sativus L.) corms. The activity was independent of pH in the range 6.0-11.0. Thermostability studies suggested the presence of three isoenzymes with transition temperatures of 30 degrees C, 45 degrees C and 60 degrees C, respectively, as given by Arrhenius plots. When stained for catalase activity gel electropherograms of extract revealed 3 distinct bands with apparent molecular weight of 323,000, 295,000 and 268,000, respectively. Thus it appeared that at least three isoenzymes of catalase were present in dormant saffron corms.

Catalase↗

EPC-K1, a hydroxyl radical scavenger, prevents 6-hydroxydopamine-induced dopamine depletion in the mouse striatum by up-regulation of catalase activity.

We examined the effect of pretreatment with EPC-K1, a potent hydroxyl radical scavenger, on 6-hydroxydopamine (6-OHDA)-induced reduction of dopamine (DA) and its metabolites in the mouse striatum. EPC-K1 was mixed with diet (0.2%, wt/wt) for 1 or 2 weeks, and then 6-OHDA (60 microg in 2 microl of saline solution) was injected intracereberoventricularly. Mice continued to be fed EPC-K1-containing diet for another one week before they were sacrificed. The concentrations of DA and its metabolites in the striatum were measured by high performance liquid chromatography. 6-OHDA reduced the level of DA and its metabolites in the striatum. Pretreatment with EPC-K1 for 2 weeks, but not for 1 week, abrogated the neurotoxic effect of 6-OHDA on striatal concentrations of DA and its metabolites. Measurement of striatal concentrations of thiobarbituric acid reactive substances, glutathione, and malonaldehyde plus 4-hydroxynonenal, and the activities of superoxide dismutase and catalase in EPC-K1 treated mice showed an increase in catalase activity after 2 weeks of such treatment. No other changes in anti-oxidants levels were noted. Our results suggest that EPC-K1 counteracts the neurotoxicity of 6-OHDA by increasing catalase activities.

3,4-Dihydroxyphenylacetic Acid↗