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Biochimica Et Biophysica Acta Jan 2003Hydrogen peroxide removal rates by hemoglobin were enhanced in the presence of reduced pyridine nucleotides. The species which had the activity to oxidize pyridine...
Hydrogen peroxide removal rates by hemoglobin were enhanced in the presence of reduced pyridine nucleotides. The species which had the activity to oxidize pyridine nucleotides was purified from human blood and identified as hemoglobin A. Hydrogen peroxide removal rates by hemoglobin A without reduced pyridine nucleotides at 0.2 mM hydrogen peroxide were 0.87+/-0.11 micromol/s/g hemoglobin, and the removal rates using 0.2 mM NADH and NADPH were 2.02+/-0.20 and 1.96+/-0.31 micromol/s/g hemoglobin, respectively. We deduced that the removal reaction by hemoglobin included formations of methemoglobin and the ferryl radical and reduction of the latter with pyridine nucleotides. The hydrogen peroxide removal ability by hemoglobin was less than that by catalase but was larger than that by glutathione peroxidase-glutathione reductase system at 0.2 mM hydrogen peroxide. Under acatalasemic conditions, it was suggested that NAD(P)H were important factors to prevent the oxidative degradation of hemoglobin.
Topics: Acatalasia; Adult; Animals; Catalase; Erythrocytes; Glutathione Peroxidase; Glutathione Reductase; Hemoglobins; Hemolysis; Humans; Hydrogen Peroxide; Male; Methemoglobin; Mice; Mice, Transgenic; Middle Aged; NADP; Oxidation-Reduction
PubMed: 12527406
DOI: 10.1016/s0925-4439(02)00213-2 -
The Journal of Clinical Investigation May 1998Chronic granulomatous disease (CGD) is a rare genetic disorder in which phagocytes fail to produce superoxide because of defects in one of several components of the...
Chronic granulomatous disease (CGD) is a rare genetic disorder in which phagocytes fail to produce superoxide because of defects in one of several components of the NADPH oxidase complex. As a result, patients develop recurrent life-threatening bacterial and fungal infections. The organisms to which CGD patients are most susceptible produce catalase, regarded as an important factor for microbial pathogenicity in CGD. To test the role of pathogen-derived catalase in CGD directly, we have generated isogenic strains of Aspergillus nidulans in which one or both of the catalase genes (catA and catB), have been deleted. We hypothesized that catalase negative mutants would be less virulent than the wild-type strain in experimental animal models. CGD mice were produced by disruption of the p47(phox) gene which encodes the 47-kD subunit of the NADPH oxidase. Wild-type A. nidulans inoculated intranasally caused fatal infection in CGD mice, but did not cause disease in wild-type littermates. Surprisingly, wild-type A. nidulans and the catA, catB, and catA/catB mutants were equally virulent in CGD mice. Histopathological studies of fatally infected CGD mice showed widely distributed lesions in the lungs regardless of the presence or absence of the catA and catB genes. Similar to the CGD model, catalase-deficient A. nidulans was highly virulent in cortisone-treated BALB/c mice. Taken together, these results indicate that catalases do not play a significant role in pathogenicity of A. nidulans in p47(phox)-/- mice, and therefore raise doubt about the central role of catalases as a fungal virulence factor in CGD.
Topics: Acatalasia; Animals; Aspergillosis; Aspergillus nidulans; Catalase; Cortisone; Disease Models, Animal; Fungal Proteins; Granulomatous Disease, Chronic; Hydrogen Peroxide; Immunosuppressive Agents; Lung; Mice; Mice, Knockout; NADPH Oxidases; Neutrophils; Phosphoproteins
PubMed: 9576747
DOI: 10.1172/JCI2301 -
Japanese Journal of Cancer Research :... Jul 1996Adult male and female acatalasemic (C3H/AnLCsbCsb),hypocatalasemic (C3H/AnLCscCsc) and normal mice of C3H strain fed on regular laboratory chow for 15 months showed an...
Adult male and female acatalasemic (C3H/AnLCsbCsb),hypocatalasemic (C3H/AnLCscCsc) and normal mice of C3H strain fed on regular laboratory chow for 15 months showed an increased incidence of spontaneous mammary tumor in the decreasing order of female acatalasemic, male acatalasemic, female hypocatalasemic and male hypocatalasemic mice. Normal mice did not develop mammary tumor. We conducted a prospective study with female acatalasemic mice, which showed the highest incidence of mammary tumor, to examine the preventive effect of vitamin E on mammary tumor. Female acatalasemic mice were fed on vitamin E-deficient (28 animals) and vitamin E-supplemented diet (25 animals) for 29 months. The incidence of mammary tumor in mice given the vitamin E-supplemented diet was 47%, while that in mice given vitamin E-deficient diet was 82% (P < 0.002). Mammary tumors were apparent after 9 months of vitamin E deprivation and after 14 months of vitamin E supplementation. Female normal mice did not develop mammary tumor during a comparable period of time. The mean catalase activity of mammary gland in acatalasemic mice was 18.8% of that in normal mice. The results indicate that vitamin E protects acatalasemic mice against the development of mammary tumor.
Topics: Acatalasia; Animals; Catalase; Female; Male; Mammary Neoplasms, Animal; Mice; Mice, Inbred C3H; Mice, Mutant Strains; Vitamin E
PubMed: 8698615
DOI: 10.1111/j.1349-7006.1996.tb00277.x -
Biochimica Et Biophysica Acta Aug 1997Hydrogen peroxide removal activities in normal and acatalasemic mouse hemolysates were examined to determine the optimal temperature of catalase. From thermal stability...
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.
Topics: Acatalasia; Animals; Catalase; Erythrocytes; Hemoglobin A; Hemoglobins; Hemolysis; Hydrogen Peroxide; Kinetics; Liver; Male; Methemoglobin; Mice; Mice, Inbred C3H; Temperature
PubMed: 9300794
DOI: 10.1016/s0925-4439(97)00024-0 -
Journal of Biochemistry Apr 1995To investigate the role of hydrogen peroxide in Cr(VI) toxicity in vivo toward bacterial cells, we examined the effect of Cr(VI), hydrogen peroxide, sodium azide, and...
To investigate the role of hydrogen peroxide in Cr(VI) toxicity in vivo toward bacterial cells, we examined the effect of Cr(VI), hydrogen peroxide, sodium azide, and mannitol on the viability of Escherichia coli. Bacterial cells were incubated for 1 h with shaking in the presence of Cr(VI), hydrogen peroxide, sodium azide as catalase inhibitor, and/or mannitol as radical scavenger. The colony-forming ability and double-strand DNA degradation were examined. The viability assays revealed that Cr(VI) toxicity depended on hydroxyl radicals generated in the reaction involving hydrogen peroxide and chromium. Moreover, incubation of E. coli cells with 10 mM Cr(VI) and 3 mM hydrogen peroxide caused the degradation of double-strand DNA in vivo, which was suppressed by the addition of mannitol. These results indicated that hydroxyl radicals generated in the incubation degraded DNA of E. coli cells, resulting in cell death. In the absence of added hydrogen peroxide, the intracellular concentration of hydrogen peroxide in E. coli was low (below 1 microM). A catalase-defective strain incubated in the absence of added hydrogen peroxide remained fully viable after 1 h but showed decreased viability after prolonged incubation (4-8 h). The addition of mannitol suppressed this decrease, suggesting that hydroxyl radicals may be involved in the expression of Cr(VI) toxicity even without added hydrogen peroxide.
Topics: Acatalasia; Catalase; Chromium; Chromosomes, Bacterial; DNA, Bacterial; Escherichia coli; Hydrogen Peroxide; Hydroxyl Radical; Mannitol; Oxidation-Reduction
PubMed: 7592539
DOI: 10.1093/oxfordjournals.jbchem.a124776 -
The Yale Journal of Biology and Medicine 1985Staphylococci pretreated with subminimal inhibitory concentrations (subMIC) of cell-wall active antibiotics exhibit increased susceptibility to killing by human...
Staphylococci pretreated with subminimal inhibitory concentrations (subMIC) of cell-wall active antibiotics exhibit increased susceptibility to killing by human polymorphonuclear leukocytes (PMNs), even when phagosome information is impaired by the mold metabolite, cytochalasin B. To investigate the role of specific bacterial factors in the process, studies were carried out with organisms lacking catalase (streptococci) or cell-wall autolytic enzymes and compared to findings with Staphylococcus aureus 502A. Neutrophil factors were studied using inhibitors, oxygen radical scavengers, myeloperoxidase (MPO)-deficient PMNs, or PMNs from a patient with chronic granulomatous disease (CGD). Documentation of the enhanced susceptibility of the streptococcal strains to killing by PMNs following subMIC penicillin pretreatment required the use of cytochalasin B. Enhancement of killing occurred independent of the presence or absence of bacterial autolysins or catalase. SubMIC penicillin pretreatment of S. pneumoniae R36A specifically promoted the susceptibility of these organisms to killing by myeloperoxidase (MPO)-mediated mechanisms (enhancement lost using MPO-deficient or azide-treated cells). Factors other than MPO or toxic oxygen products generated by the PMN respiratory burst are responsible for enhanced killing of penicillin-pretreated S. aureus 502A (enhancement preserved using MPO-deficient, azide-treated, or chronic granulomatous disease patient cells). These studies define methods to study the interaction of antimicrobial agents and PMNs in the killing of microorganisms. They also demonstrate that penicillin treatment can change the susceptibility of gram-positive cocci to the action of specific PMN microbicidal mechanisms. The mechanism of the enhancement appears to be bacterial strain-dependent and not predictable by bacterial autolysin or catalase activity.
Topics: Acatalasia; Cytochalasins; Humans; In Vitro Techniques; Neutrophils; Penicillin G; Phagocytosis; Staphylococcus aureus; Streptococcus pneumoniae; Streptococcus sanguis
PubMed: 4036175
DOI: No ID Found -
Journal of Bacteriology Dec 1997Only a single superoxide dismutase (SodA) was detected in Bacillus subtilis, and growing cells of a sodA mutant exhibited paraquat sensitivity as well as a growth defect... (Comparative Study)
Comparative Study
Only a single superoxide dismutase (SodA) was detected in Bacillus subtilis, and growing cells of a sodA mutant exhibited paraquat sensitivity as well as a growth defect and reduced survival at an elevated temperature. However, the sodA mutation had no effect on the heat or hydrogen peroxide resistance of wild-type spores or spores lacking the two major DNA protective alpha/beta-type small, acid-soluble, spore proteins (termed alpha(-)beta(-) spores). Spores also had only a single catalase (KatX), as the two catalases found in growing cells (KatA and KatB) were absent. While a katA mutation greatly decreased the hydrogen peroxide resistance of growing cells, as found previously, katA, katB, and katX mutations had no effect on the heat or hydrogen peroxide resistance of wild-type or alpha(-)beta(-) spores. Inactivation of the mrgA gene, which codes for a DNA-binding protein that can protect growing cells against hydrogen peroxide, also had no effect on spore hydrogen peroxide resistance. Inactivation of genes coding for alkyl hydroperoxide reductase, which has been shown to decrease growing cell resistance to alkyl hydroperoxides, had no effect on spore resistance to such compounds or on spore resistance to heat and hydrogen peroxide. However, Western blot analysis showed that at least one alkyl hydroperoxide reductase subunit was present in spores. Together these results indicate that proteins that play a role in the resistance of growing cells to oxidizing agents play no role in spore resistance. A likely reason for this lack of a protective role for spore enzymes is the inactivity of enzymes within the dormant spore.
Topics: Acatalasia; Bacillus subtilis; Bacterial Proteins; Catalase; Cell Division; DNA-Binding Proteins; Hot Temperature; Oxidants; Oxidoreductases; Paraquat; Peroxidases; Peroxides; Peroxiredoxins; Spores, Bacterial; Superoxide Dismutase
PubMed: 9393707
DOI: 10.1128/jb.179.23.7420-7425.1997 -
The Tohoku Journal of Experimental... Jul 1974
Topics: Abdominal Muscles; Acatalasia; Appendix; Catalase; Humans; Immunodiffusion; Japan; Liver; Muscles; Temperature
PubMed: 4281545
DOI: 10.1620/tjem.113.239 -
Biochimica Et Biophysica Acta Feb 2010Human acatalasemia may be a risk factor for the development of diabetes mellitus. However, the mechanism by which diabetes is induced is still poorly understood. The...
Human acatalasemia may be a risk factor for the development of diabetes mellitus. However, the mechanism by which diabetes is induced is still poorly understood. The impact of catalase deficiency on the onset of diabetes has been studied in homozygous acatalasemic mutant mice or control wild-type mice by intraperitoneal injection of diabetogenic alloxan. The incidence of diabetes was higher in acatalasemic mice treated with a high dose (180 mg/kg body weight) of alloxan. A higher dose of alloxan accelerated severe atrophy of pancreatic islets and induced pancreatic beta cell apoptosis in acatalasemic mice in comparison to wild-type mice. Catalase activity remained low in the acatalasemic pancreas without the significant compensatory up-regulation of glutathione peroxidase or superoxide dismutase. Furthermore, daily intraperitoneal injection of angiotensin II type 1 (AT1) receptor antagonist telmisartan (0.1 mg/kg body weight) prevented the development of alloxan-induced hyperglycemia in acatalasemic mice. This study suggests that catalase plays a crucial role in the defense against oxidative-stress-mediated pancreatic beta cell death in an alloxan-induced diabetes mouse model. Treatment with telmisartan may prevent the onset of alloxan-induced diabetes even under acatalasemic conditions.
Topics: Acatalasia; Alloxan; Angiotensin II Type 1 Receptor Blockers; Animals; Apoptosis; Benzimidazoles; Benzoates; Blood Glucose; Body Weight; Catalase; Cell Death; Diabetes Mellitus, Experimental; Glutathione Peroxidase; Homozygote; Hyperglycemia; Insulin-Secreting Cells; Male; Mice; Mice, Inbred C3H; Mice, Knockout; Mice, Mutant Strains; Superoxide Dismutase; Telmisartan
PubMed: 19883754
DOI: 10.1016/j.bbadis.2009.10.009 -
The Tohoku Journal of Experimental... Sep 1977The activities of superoxide dismutase and glutathione peroxidase in the red cells of normal and acatalasemia bloods were compared. Superoxide dismutase activity in the...
The activities of superoxide dismutase and glutathione peroxidase in the red cells of normal and acatalasemia bloods were compared. Superoxide dismutase activity in the red cells of Japanese acatalasemia blood was higher than in normal control, while glutathione peroxidase activity remained within normal limits. Cyanide sensitivity of superoxide dismutase in the red cells of acatalasemia blood was similar to that in normal control.
Topics: Catalase; Erythrocytes; Glutathione Peroxidase; Humans; Peroxidases; Superoxide Dismutase
PubMed: 918979
DOI: 10.1620/tjem.123.95