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The Journal of Clinical Investigation Jul 1965
Topics: Acatalasia; Anemia; Anemia, Hemolytic; Ascorbic Acid; Azides; Catalase; Cyanides; Erythrocyte Aging; Erythrocytes; Ethylmaleimide; Genetics, Medical; Glucose; Glucosephosphate Dehydrogenase Deficiency; Glucosephosphates; Glutathione; Hemoglobins; Hemolysis; Hexosephosphates; Humans; Metabolism, Inborn Errors; Methemoglobin; Peroxides; Pharmacology; Phenylhydrazines; Primaquine; Sulfhemoglobin; Sulfhydryl Compounds
PubMed: 14328395
DOI: 10.1172/JCI105225 -
Endocrine Journal Jan 2024We encountered five cases that exhibited false-high Hemoglobin A1c (HbA1c) levels when samples were examined using the enzyme-based NORUDIA N HbA1c kit. HbA1c levels...
We encountered five cases that exhibited false-high Hemoglobin A1c (HbA1c) levels when samples were examined using the enzyme-based NORUDIA N HbA1c kit. HbA1c levels were higher than those obtained using other methods, such as HPLC, immune-based methods, and other enzyme-based kits. This kit produced inaccurate results for HbA1c when residual peroxides were present in samples. The addition of peroxidase solution restored false-high HbA1c levels in the five cases, indicating that reduced catalase activity was responsible for these values because catalase eliminates peroxide. Catalase activity and gene mutations were examined in the five cases and an immunohistological analysis was performed to assess the expression of catalase. Cases #1 and 2 were diagnosed as acatalasemia and cases #3, 4, and 5 as hypocatalasemia based on compound heterozygous SNP and heterozygous splicing mutations in the catalase gene. Therefore, impaired catalase activity was responsible for false-high HbA1c levels measured by the NORUDIA N HbA1c kit.
Topics: Glycated Hemoglobin; Catalase; Antioxidants; Peroxidase
PubMed: 38030260
DOI: 10.1507/endocrj.EJ23-0212 -
Industrial Health 1983
Comparative Study Review
Topics: Acatalasia; Animals; Catalase; Cytochrome c Group; Erythrocytes; Ferritins; Hemin; Horseradish Peroxidase; Humans; Hydrogen Peroxide; Lactoperoxidase; Mercury; Methemoglobin; Mice; Oxidation-Reduction; Tissue Distribution
PubMed: 6317620
DOI: 10.2486/indhealth.21.219 -
The Journal of Clinical Investigation Apr 1960
Topics: Acatalasia; Catalase; Genetics, Medical; Heterozygote; Humans
PubMed: 13836629
DOI: 10.1172/JCI104075 -
BMC Nephrology Mar 2012Catalase is an important antioxidant enzyme that regulates the level of intracellular hydrogen peroxide and hydroxyl radicals. The effects of catalase deficiency on...
BACKGROUND
Catalase is an important antioxidant enzyme that regulates the level of intracellular hydrogen peroxide and hydroxyl radicals. The effects of catalase deficiency on albuminuria and progressive glomerulosclerosis have not yet been fully elucidated. The adriamycin (ADR) nephropathy model is considered to be an experimental model of focal segmental glomerulosclerosis. A functional catalase deficiency was hypothesized to exacerbate albuminuria and the progression of glomerulosclerosis in this model.
METHODS
ADR was intravenously administered to both homozygous acatalasemic mutant mice (C3H/AnLCs(b)Cs(b)) and control wild-type mice (C3H/AnLCs(a)Cs(a)). The functional and morphological alterations of the kidneys, including albuminuria, renal function, podocytic, glomerular and tubulointerstitial injuries, and the activities of catalase were then compared between the two groups up to 8 weeks after disease induction. Moreover, the presence of a mutation of the toll-like receptor 4 (tlr4) gene, which was previously reported in the C3H/HeJ strain, was investigated in both groups.
RESULTS
The ADR-treated mice developed significant albuminuria and glomerulosclerosis, and the degree of these conditions in the ADR-treated acatalasemic mice was higher than that in the wild-type mice. ADR induced progressive renal fibrosis, renal atrophy and lipid peroxide accumulation only in the acatalasemic mice. In addition, the level of catalase activity was significantly lower in the kidneys of the acatalasemic mice than in the wild-type mice during the experimental period. The catalase activity increased after ADR injection in wild-type mice, but the acatalasemic mice did not have the ability to increase their catalase activity under oxidative stress. The C3H/AnL strain was found to be negative for the tlr4 gene mutation.
CONCLUSIONS
These data indicate that catalase deficiency plays an important role in the progression of renal injury in the ADR nephropathy model.
Topics: Acatalasia; Albuminuria; Animals; Catalase; Disease Susceptibility; Doxorubicin; Kidney Diseases; Male; Mice; Mice, Inbred C3H; Mice, Knockout
PubMed: 22443450
DOI: 10.1186/1471-2369-13-14 -
Experimental Animals Oct 1999Acatalasemic Beagle dogs which were maintained in our laboratories showed no sign of catalase activity at all in the erythrocytes, and glutathione peroxidase and...
Acatalasemic Beagle dogs which were maintained in our laboratories showed no sign of catalase activity at all in the erythrocytes, and glutathione peroxidase and superoxide dismutase were at normal levels. Immunoblotting analysis demonstrated that no catalase protein is detectable in their erythrocytes. On the other hand, catalase activity was detected in other tissues and organs, albeit at varying, lower levels than in normal dogs. Quantitative immunoblotting analysis consistently demonstrated that the catalase protein is expressed in the liver and kidneys of acatalasemic dogs in proportion to the activity in these organs. The catalase mRNA expressions in the blood, liver and kidneys in acatalasemic dogs were almost the same as those in normal dogs. These results suggested that catalytically normal catalase protein is translated from mRNA in the tissues and organs including erythrocytes, but in erythrocytes this enzyme protein is disposed of by an unknown mechanism.
Topics: Acatalasia; Animals; Blotting, Northern; Catalase; Dog Diseases; Dogs; Erythrocytes; Glutathione Peroxidase; Immunoblotting; Kidney; Liver; Male; RNA, Messenger; Superoxide Dismutase; Tissue Distribution
PubMed: 10591001
DOI: 10.1538/expanim.48.229 -
American Journal of Respiratory and... Apr 2009Although reactive oxygen species (ROS) are generally considered to be proinflammatory and to contribute to cellular and organ dysfunction when present in excessive...
RATIONALE
Although reactive oxygen species (ROS) are generally considered to be proinflammatory and to contribute to cellular and organ dysfunction when present in excessive amounts, there is evidence that specific ROS, particularly hydrogen peroxide (H(2)O(2)), may have antiinflammatory properties.
OBJECTIVES
To address the role that increases in intracellular H(2)O(2) may play in acute inflammatory processes, we examined the effects of catalase inhibition or the absence of catalase on LPS-induced inflammatory responses.
METHODS
Neutrophils from control or acatalasemic mice, or control neutrophils incubated with the catalase inhibitor aminotriazole, were treated with LPS, and levels of reactive oxygen species, proteasomal activity, NF-kappaB activation, and proinflammatory cytokine expression were measured. Acute lung injury (ALI) was produced by intratracheal injection of LPS into control, acatalasemic-, or aminotriazole-treated mice.
MEASUREMENTS AND MAIN RESULTS
Intracellular levels of H(2)O(2) were increased in acatalasemic neutrophils and in neutrophils exposed to aminotriazole. Compared with LPS-stimulated neutrophils from control mice, neutrophils from acatalasemic mice or neutrophils treated with aminotriazole demonstrated reduced 20S and 26S proteasomal activity, IkappaB-alpha degradation, NF-kappaB nuclear accumulation, and production of the proinflammatory cytokines TNF-alpha and macrophage inhibitory protein (MIP)-2. The severity of LPS-induced ALI was less in acatalasemic mice and in mice treated with aminotriazole as compared with that found in control mice.
CONCLUSIONS
These results indicate that H(2)O(2) has antiinflammatory effects on neutrophil activation and inflammatory processes, such as ALI, in which activated neutrophils play a major role.
Topics: Acatalasia; Acute Lung Injury; Amitrole; Animals; Catalase; Disease Models, Animal; Enzyme Inhibitors; Hydrogen Peroxide; I-kappa B Proteins; Lipopolysaccharides; Male; Mice; Mice, Inbred C3H; Mice, Inbred C57BL; NF-KappaB Inhibitor alpha; NF-kappa B; Neutrophil Activation; Neutrophils
PubMed: 19151196
DOI: 10.1164/rccm.200806-851OC -
American Journal of Human Genetics Dec 1963
Topics: Acatalasia; Blood Chemical Analysis; Catalase; Chromosomes; Genetic Heterogeneity; Humans; Japan; Metabolic Diseases
PubMed: 14097235
DOI: No ID Found -
The Journal of Biological Chemistry Aug 2006The effects of hydrogen peroxide on normal and acatalasemic erythrocytes were examined. Severe hemolysis of acatalasemic erythrocytes and a small tyrosine radical signal...
The effects of hydrogen peroxide on normal and acatalasemic erythrocytes were examined. Severe hemolysis of acatalasemic erythrocytes and a small tyrosine radical signal (g = 2.005) associated with the formation of ferryl hemoglobin were observed upon the addition of less than 0.25 mM hydrogen peroxide. However, when the concentration of hydrogen peroxide was increased to 0.5 mM, acatalasemic erythrocytes became insoluble in water and increased the tyrosine radical signal. Polymerization of hemoglobin and aggregation of the erythrocytes were observed. On the other hand, normal erythrocytes exhibited only mild hemolysis by the addition of hydrogen peroxide under similar conditions. From these results, the scavenging of hydrogen peroxide by hemoglobin generates the ferryl hemoglobin species (H-Hb-Fe(IV)=O) plus protein-based radicals (*Hb-Fe(IV)=O). These species induce hemolysis of erythrocytes, polymerization of hemoglobin, and aggregation of the acatalasemic erythrocytes. A mechanism for the onset of Takarara disease is proposed.
Topics: Acatalasia; Animals; Dose-Response Relationship, Drug; Erythrocyte Aggregation; Erythrocytes; Hemoglobins; Hemolysis; Hydrogen Peroxide; Male; Mice; Mice, Inbred Strains; Polymers
PubMed: 16751193
DOI: 10.1074/jbc.M513818200 -
Kidney International Sep 2005Catalase is one of the important antioxidant enzymes regulating the levels of intracellular hydrogen peroxide and hydroxyl radical. The effect of catalase deficiency on...
BACKGROUND
Catalase is one of the important antioxidant enzymes regulating the levels of intracellular hydrogen peroxide and hydroxyl radical. The effect of catalase deficiency on progressive renal fibrosis has not been fully elucidated.
METHODS
Homozygous acatalasemic mutant mice (C3H/AnLCs(b)Cs(b)) and control wild-type mice (C3H/AnLCs(a)Cs(a)) were subjected to 5/6 nephrectomy. The functional and morphological alterations of the remnant kidneys, including tubulointerstitial fibrosis, epithelial to mesenchymal transition (EMT), peroxidation, antioxidant enzyme activity, and gene expression of EMT-related molecules were compared between the two groups at 6, 12, and 18 weeks after 5/6 nephrectomy.
RESULTS
The 5/6 nephrectomy resulted in albuminuria, decreased renal function, and tubulointerstitial fibrosis with accumulation of type I and type IV collagens in the remnant kidneys of both mouse groups. However, the degree of these changes was significantly higher in acatalasemic mice after 5/6 nephrectomy as compared with wild-type mice until week 18. EMT, a crucial phenotypic alteration of tubular epithelial cells, was observed in acatalasemic mice by electron microscopy and was associated with upregulation of EMT-related alpha-smooth muscle actin (alpha-SMA), transforming growth factor-beta1 (TGF-beta1), connective tissue growth factor (CTGF), and fibroblast specific protein-1 (FSP-1) gene expression. Significant increases in the tubulointerstitial deposition of lipid peroxidation products, including 4-hydroxy-2-nonenal and urinary excretion of 8-hydroxy-2'- deoxyguanosine were observed in the acatalasemic mice after 5/6 nephrectomy as compared with the wild-type mice. Glomerular sclerosis developed after tubulointerstitial injury in acatalasemic mice. The level of catalase activity remained low in the remnant kidneys of acatalasemic mice until week 18 without compensatory up-regulation of glutathione peroxidase or superoxide dismutase (SOD) activity. Finally, supplementation of a SOD mimetic tempol did not prevent peroxidation and tubulointerstitial fibrosis in the acatalasemic remnant kidneys.
CONCLUSION
These findings indicate that acatalasemia exacerbates renal oxidant tissue injury and sensitizes remnant kidneys to EMT and progressive renal fibrosis. This study suggests a central role for catalase in the defense against oxidant-mediated renal fibrosis.
Topics: Albuminuria; Animals; Antioxidants; Blood Pressure; Body Weight; Catalase; Collagen Type I; Collagen Type IV; Cyclic N-Oxides; Epithelial Cells; Fibrosis; Glutathione Peroxidase; Kidney Diseases; Kidney Glomerulus; Lipid Peroxidation; Male; Mesoderm; Mice; Mice, Inbred C3H; Mice, Mutant Strains; Nephrectomy; Organ Size; Oxidative Stress; Spin Labels; Superoxide Dismutase
PubMed: 16105032
DOI: 10.1111/j.1523-1755.2005.00494.x