A rare autosomal recessive disorder resulting from the absence of CATALASE activity. Though usually asymptomatic, a syndrome of oral ulcerations and gangrene may be present.

Hydrogen peroxide and coffee induce G:C-->T:A transversions in the lacI gene of catalase-defective Escherichia coli. (1/34)

The mutagenicity of hydrogen peroxide (H2O2) was compared with that of coffee, a complex mixture which generates H2O2. An Escherichia coli strain defective in catalase activity (katG katE double mutant) and carrying a single copy mucAB (pRW144) plasmid was constructed to enhance the mutagenic response to oxidants. The ability of the mucAB genes to influence the type, frequency and distribution of H2O2-induced mutations was also investigated in isogenic bacteria lacking pRW144. Induced mutational spectra were characterized and compared with that of spontaneous mutagenesis. A total of 444 independent forward mutations affecting the first 210 bp of the lacI gene were identified by DNA sequence analysis. The spontaneous mutation spectrum showed no bias (P = 0.52) for substitutions at G:C base pairs. In contrast, in the H2O2-induced spectrum substitutions occurred preferentially at G:C base pairs (P < 0.0001) with a preponderance of G:C-->T:A transversions (43.4% of H2O2-induced mutants versus 17.3% of spontaneous mutants). These data support the view that 7,8-dihydro-8-oxoguanine is the main premutagenic lesion induced by H2O2 and that catalase-defective bacteria have elevated levels of 8-oxoguanine in chromosome DNA after H2O2 exposure. Coffee produced a similar distribution of mutational events as H2O2 (P > 0.05), suggesting that this compound may be the main cause of the coffee-induced mutagenesis. The presence of plasmid pRW144 did not affect the frequency of H2O2-induced G:C-->T:A transversions, but caused an increase in A:T-->T:A transversions and a decrease in -1 base frameshifts. Although the frequencies of G:C-->T:A transversions were similar in all three induced spectra (H2O2 and coffee +/- pRW144), differences were observed in location of mutations throughout the target gene.  (+info)

Tissue and organ expression of catalase in acatalasemic beagle dogs. (2/34)

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.  (+info)

cDNA cloning and expression of mutant catalase from the hypocatalasemic mouse: comparison with the acatalasemic mutant. (3/34)

Mutant catalase cDNAs from the hypocatalasemic and acatalasemic mice were cloned and expressed in bacteria. A novel missense mutation, Asp (AAT) to Ser (AGT), was identified at amino acid position 439 of the hypocatalasemic catalase. Analysis of recombinant catalase mutants revealed that the mutation is responsible for the reduced activity of hypocatalasemic catalase and the unstable tetrameric structure of acatalasemic catalase was also suggested.  (+info)

Characterization of hydrogen peroxide removal reaction by hemoglobin in the presence of reduced pyridine nucleotides. (4/34)

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.  (+info)

Properties of acatalasic cells growing in vitro. (5/34)

Acatalasia, a disease due to homozygosity for a Mendelian gene, is characterized by the absence of the enzyme catalase from the tissues of the human body. Red cells from heterozygotes have enzyme activities about one-half normal. In this paper, the development of cell lines from skin biopsies on an affected homozygote, a heterozygote, and eight control patients is described. The cell type is the euploid "fibroblast." It was found that acatalasic cells lacked the enzyme, even after growing for many months in a medium rich in catalase. The control lines all had mean catalase activities double or more that of the heterozygous line. Selection experiments, in which the growth of cells exposed for 20 minutes to varying concentrations of hydrogen peroxide was measured, did not provide a system for preferentially eliminating acatalasic cells. Certain other experiments bearing on the enzymatic defect in this disease were performed.  (+info)

Acatalasemia sensitizes renal tubular epithelial cells to apoptosis and exacerbates renal fibrosis after unilateral ureteral obstruction. (6/34)

Tissue homeostasis is determined by the balance between oxidants and antioxidants. Catalase is an important antioxidant enzyme regulating the level of intracellular hydrogen peroxide and hydroxyl radicals. The effect of catalase deficiency on renal tubulointerstitial injury induced by unilateral ureteral obstruction (UUO) has been studied in homozygous acatalasemic mutant mice (C3H/AnLCs(b)Cs(b)) compared with wild-type mice (C3H/AnLCs(a)Cs(a)). Complete UUO caused interstitial cell infiltration, tubular dilation and atrophy, and interstitial fibrosis with accumulation of type IV collagen in obstructed kidneys (OBK) of both mouse groups. However, the degree of injury showed a significant increase in OBK of acatalasemic mice compared with that of wild-type mice until day 7. The deposition of lipid peroxidation products including 4-hydroxy-2-hexenal, malondialdehyde, and 4-hydroxy-2-nonenal was severer in dilated tubules of acatalasemic OBK. Apoptosis in tubular epithelial cells significantly increased in acatalasemic OBK at day 4. Expression of caspase-9, a marker of mitochondrial pathway-derived apoptosis, increased in dilated tubules of acatalasemic mice. The level of catalase activity remained low in acatalasemic OBK until day 7 without compensatory upregulation of glutathione peroxidase activity. The data indicate that acatalasemia exacerbated oxidation of renal tissue and sensitized tubular epithelial cells to apoptosis in OBK of UUO. This study demonstrates that catalase deficiency enhanced tubulointerstitial injury and fibrosis in a murine model of UUO and thus supports the protective role of catalase in this model.  (+info)

Inhibitory effects of prior low-dose X-ray irradiation on carbon tetrachloride-induced hepatopathy in acatalasemic mice. (7/34)

The catalase activities in blood and organs of the acatalasemic (C3H/AnLCs(b)Cs(b)) mouse of C3H strain are lower than those of the normal (C3H/AnLCs (a)Cs(a)) mouse. We examined the effects of prior low-dose (0.5 Gy) X-ray irradiation, which reduced the oxidative damage under carbon tetrachloride-induced hepatopathy in the acatalasemic or normal mice. The acatalasemic mice showed a significantly lower catalase activity and a significantly higher glutathione peroxidase activity compared with those in the normal mice. Moreover, low-dose irradiation increased the catalase activity in the acatalasemic mouse liver to a level similar to that of the normal mouse liver. Pathological examinations and analyses of blood glutamic oxaloacetic and glutamic pyruvic transaminase activity and lipid peroxide levels showed that carbon tetrachloride induced hepatopathy was inhibited by low-dose irradiation. These findings may indicate that the free radical reaction induced by the lack of catalase and the administration of carbon tetrachloride is more properly neutralized by high glutathione peroxidase activity and low-dose irradiation in the acatalasemic mouse liver.  (+info)

Telmisartan inhibits both oxidative stress and renal fibrosis after unilateral ureteral obstruction in acatalasemic mice. (8/34)

BACKGROUND: Reactive oxygen species are involved in many of the angiotensin II signalling pathways. We have thus investigated whether the angiotensin II type 1 (AT1) receptor antagonist, telmisartan, can inhibit the accelerated renal fibrosis and excess oxidative stress, which occurs after unilateral ureteral obstruction (UUO) in acatalasemic mice. METHODS: The effect of daily intraperitoneal injection of telmisartan (0.1-0.3 mg/kg body weight) on the renal tubulointerstitial injury induced by UUO has been studied in homozygous acatalasemic mutant mice (C3H/AnLCs b Cs b) and wild-type mice (C3H/AnLCs a Cs a). We evaluated the systemic blood pressure of the mice on the seventh day. In addition, the tubulointerstitial expression of collagens type I and type IV, the p22-, p47- and p67-phox subunits of NADPH oxidase, 4-hydroxy-2-nonenal, and 4-hydroxy-2-hexenal lipid peroxidation products were assessed by immunohistochemistry. The level of apoptosis was determined by terminal deoxynucleotidyl transferase nick end-labelling analysis, while the mRNA level of the p22-, p47- and p67-phox subunits was quantified by real-time PCR. The renal content of each of the antioxidant enzymes catalase, glutathione peroxidase and superoxide dismutase was determined by specific assay. RESULTS: Obstructed kidneys from acatalasemic mice exhibited increased tubulointerstitial deposition in dilated tubules of collagens type I and IV, lipid peroxidation products, and the p22/p47/p67-phox subunits of NADPH oxidase. The level of the p22/p47/p67-phox subunit mRNA, and of apoptosis in tubular epithelial cells, was also increased compared with those from wild-type kidneys. Treatment with telmisartan attenuated all of the changes and prevented renal fibrosis in a dose-dependent manner; despite the low dose (0.1 mg/kg). The treatment did not lower the systemic blood pressure. The catalase activity remained low in acatalasemic obstructed kidneys without compensatory upregulation of glutathione peroxidase or superoxide dismutase activity; the level of neither anti-oxidant enzymes in obstructed kidneys was affected by telmisartan. CONCLUSIONS: The AT1 receptor antagonist telmisartan ameliorated renal fibrosis after UUO by inhibition of oxidative stress, even under acatalasemic conditions.  (+info)

Acatalasia is a very rare inherited disorder that affects the body's ability to break down and remove hydrogen peroxide, a byproduct produced during normal cellular metabolism. This condition is caused by a deficiency or complete lack of the enzyme catalase, which is responsible for converting hydrogen peroxide into water and oxygen.

The medical definition of Acatalasia can be described as:

1. An autosomal recessive genetic disorder: Acatalasia is inherited in an autosomal recessive pattern, meaning that an individual must inherit two copies of the defective gene (one from each parent) to develop the condition. Individuals who inherit only one copy of the defective gene are carriers and do not typically show symptoms themselves.

2. Absence or deficiency of catalase enzyme: Acatalasia is characterized by a near-complete absence or significantly reduced levels of the catalase enzyme in the body, primarily in red blood cells and certain tissues such as the liver and spleen. This deficiency leads to an accumulation of hydrogen peroxide within cells.

3. Accumulation of hydrogen peroxide: The buildup of hydrogen peroxide can cause damage to cellular components, including proteins, lipids, and DNA, potentially leading to various health issues over time.

4. Clinical manifestations: Although Acatalasia is a rare condition, when it does occur, it can lead to several health problems, such as chronic granulomatous disease (CGD), which is characterized by recurrent bacterial and fungal infections due to impaired immune function. Additionally, individuals with Acatalasia may have an increased risk of developing certain types of cancer, particularly those related to the hematopoietic system (blood cells and bone marrow).

5. Diagnosis: Acatalasia can be diagnosed through various methods, including blood tests that measure catalase enzyme activity, genetic testing to identify mutations in the CAT gene (which encodes for the catalase enzyme), and clinical evaluation of symptoms and medical history.

6. Treatment and management: Currently, there is no specific treatment or cure for Acatalasia. Management typically focuses on addressing individual symptoms as they arise and implementing strategies to reduce the risk of complications. This may include antibiotics or antifungal medications to treat infections, cancer surveillance and prevention measures, and regular monitoring of overall health.

... is often the result of mutations in both copies of the CAT gene which codes for the enzyme catalase. There are ... Acatalasia is an autosomal recessive peroxisomal disorder caused by absent or very low levels of the enzyme catalase. Catalase ... Instead of a very bubbling reaction, blood turns brown-colored, which means the patient suffers from acatalasia.[citation ... Bissonnette, Bruno; Luginbuehl, Igor; Marciniak, Bruno; Dalens, Bernard J. (2006). "Acatalasia/Acatalasemia". Syndromes: Rapid ...
Acatalasia is a condition caused by homozygous mutations in CAT, resulting in a lack of catalase. Symptoms are mild and include ... Some humans have very low levels of catalase (acatalasia), yet show few ill effects. The increased oxidative stress that occurs ...
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... acatalasia MeSH C18.452.648.556.750.112 - adrenoleukodystrophy MeSH C18.452.648.556.750.200 - chondrodysplasia punctata, ...
... acatalasia MeSH C16.320.565.556.750.112 - adrenoleukodystrophy MeSH C16.320.565.556.750.200 - chondrodysplasia punctata, ...
Acatalasia is often the result of mutations in both copies of the CAT gene which codes for the enzyme catalase. There are ... Acatalasia is an autosomal recessive peroxisomal disorder caused by absent or very low levels of the enzyme catalase. Catalase ... Instead of a very bubbling reaction, blood turns brown-colored, which means the patient suffers from acatalasia.[citation ... Bissonnette, Bruno; Luginbuehl, Igor; Marciniak, Bruno; Dalens, Bernard J. (2006). "Acatalasia/Acatalasemia". Syndromes: Rapid ...
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Defects in CAT are the cause of acatalasia (ACATLAS) [MIM:115500]; also known as acatalasemia. This disease is characterized by ...
Alpha 1-antitrypsin deficiency - Cystic fibrosis - Amyloidosis (Familial Mediterranean fever) - Acatalasia. v • d • e ...
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Acatalasia Preferred Term Term UI T358366. Date10/12/1999. LexicalTag NON. ThesaurusID ... Acatalasia Preferred Concept UI. M0328366. Scope Note. A rare autosomal recessive disorder resulting from the absence of ... Acatalasia. Tree Number(s). C16.320.565.663.050. C18.452.648.663.050. Unique ID. D020642. RDF Unique Identifier. http://id.nlm. ...
Acatalasemia Japanese Type use Acatalasia Acatalasemia Swiss Type use Acatalasia Acatalasia Acathisia, Drug Induced use ...
ACATALASIA. ACATALASIA. ACATALASIA. ACCIDENTE CEREBROVASCULAR. CEREBROVASCULAR ACCIDENT. ACIDENTE CEREBROVASCULAR. ACEITE DE ...
ACATALASIA. ACATALASIA. ACATALASIA. ACCIDENTE CEREBROVASCULAR. CEREBROVASCULAR ACCIDENT. ACIDENTE CEREBROVASCULAR. ACEITE DE ...
ACATALASIA. ACATALASIA. ACATALASIA. ACCIDENTE CEREBROVASCULAR. CEREBROVASCULAR ACCIDENT. ACIDENTE CEREBROVASCULAR. ACEITE DE ...
ACATALASIA ACATALASIA ACATALASIA ACCESSORY NERVE DISEASES ENFERMEDADES DEL NERVIO ACCESORIO DOENÇAS DO NERVO ACESSÓRIO ...
ACATALASIA ACATALASIA ACATALASIA ACCESSORY NERVE DISEASES ENFERMEDADES DEL NERVIO ACCESORIO DOENÇAS DO NERVO ACESSÓRIO ...
ACATALASIA ACATALASIA ACATALASIA ACIDENTE CEREBROVASCULAR CEREBROVASCULAR ACCIDENT ACCIDENTE CEREBROVASCULAR ÁCIDO GLUCURÔNICO ...
ACATALASIA. ACATALASIA. ACATALASIA. ACCIDENTE CEREBROVASCULAR. CEREBROVASCULAR ACCIDENT. ACIDENTE CEREBROVASCULAR. ACEITE DE ...
ACATALASIA ACATALASIA ACATALASIA ACCESSORY NERVE DISEASES ENFERMEDADES DEL NERVIO ACCESORIO DOENÇAS DO NERVO ACESSÓRIO ...
ACATALASIA ACATALASIA ACATALASIA ACIDENTE CEREBROVASCULAR CEREBROVASCULAR ACCIDENT ACCIDENTE CEREBROVASCULAR ÁCIDO GLUCURÔNICO ...
ACATALASIA ACATALASIA ACATALASIA ACCESSORY NERVE DISEASES ENFERMEDADES DEL NERVIO ACCESORIO DOENÇAS DO NERVO ACESSÓRIO ...
ACATALASIA ACATALASIA ACATALASIA ACCESSORY NERVE DISEASES ENFERMEDADES DEL NERVIO ACCESORIO DOENÇAS DO NERVO ACESSÓRIO ...
Acatalasemia Japanese Type use Acatalasia Acatalasemia Swiss Type use Acatalasia Acatalasia Acathisia, Drug Induced use ...
Acatalasia Medicine & Life Sciences 100% * phenylhydrazine Medicine & Life Sciences 85% * Phenylhydrazine Chemical Compounds 67 ...
A deficiency of this enzyme results in ACATALASIA.. Myocardium. The muscle tissue of the HEART. It is composed of striated, ...
A deficiency of this enzyme results in ACATALASIA. Descriptor ID. D002374 MeSH Number(s). D08.811.682.732.332 ...
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Wolny od chorób genetycznych: (MLS, NCCD POAG, PK, IGS, FVII, O.I, Acatalasia, Lafora, PRA) N/N ... Wolny od chorób genetycznych: (MLS, NCCD POAG, PK, IGS, FVII, O.I, Acatalasia, Lafora, PRA) N/N ... Wolny od chorób genetycznych: (MLS , NCCD , POAG , PK , IGS , FVII , OI , Acatalasia , Lafora ) N/N ...
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  • A deficiency of this enzyme results in ACATALASIA. (uchicago.edu)
  • Acatalasia is an autosomal recessive peroxisomal disorder caused by absent or very low levels of the enzyme catalase. (wikipedia.org)
  • Acatalasia is often the result of mutations in both copies of the CAT gene which codes for the enzyme catalase. (wikipedia.org)