Disease relevance of CAT

• Antioxidants, including bovine liver catalase, bovine erythrocyte CuZn-SOD, sodium selenite and Trolox, a water soluble vitamin E analogue, as well as hypoxia, inhibited dexamethasone-induced apoptosis [1].
• Activity, peroxide compound formation, and heme d synthesis in Escherichia coli HPII catalase [2].
• Similar spectral changes in the presence of DTE and NADPH were displayed by a bacterial catalase from Proteus mirabilis [3].
• The increased frequency of chromosomal aberrations and the cytotoxicity of hypoxanthine plus xanthine oxidase were not affected by superoxide dismutase, but were strongly inhibited by catalase [4].
• Using whey as substrate, catalase, haemoglobin combined with ascorbic acid and xanthine oxidase inhibitors all provided protection against oxygen toxicity for a strain of Staphylococcus aureus and of Streptococcus agalactiae [5].

High impact information on CAT

• In addition, bovine catalase uses unbound NAD(P)H to prevent substrate inactivation without displacing catalase-bound NADP(+) [6].
• TNF alpha treatment (100 U/ml for 6 h) decreased total GSH content and concomitantly increased the oxidized GSH content, but did not alter the cellular catalase activity [7].
• Furthermore, the addition of catalase (3000 U/ml) to corneas incubated with G/GO for 6 hours markedly reduced the production of LCFs [8].
• Inactivation of catalase by phenylhydrazine. Formation of a stable aryl-iron heme complex [9].
• The absolute chirality of N-ethylprotoporphyrin IX isolated from catalase inactivated with ethylhydrazine confirms that the prosthetic heme has the same chiral orientation in the active site as it does in hemoglobin [9].

Chemical compound and disease context of CAT

• Neither hypoxia, hyperoxia, or hypoxia followed by reoxygenation altered H2O2 generation at the intracellular site accessible to peroxisomal catalase [10].
• The effect of haematin and catalase on Streptococcus faecalis var. zymogenes growing on glycerol [11].

Biological context of CAT

• Lipid peroxidation was also strongly inhibited by singlet oxygen scavengers, e.g. dimethylfuran and diphenylfuran, and by catalase [12].
• Hydroxyl radicals, superoxide and H2O2 were also not involved, since the relative number of single strand breaks and of sites of base loss (AP sites) was much lower than in the case of DNA damage induced by hydroxyl radicals and since the presence of SOD or catalase had no effect on the extent of the damage [13].
• Thus, extremely high catalase activity and suppression of LPCR are apparently the main mechanisms of the unusually high H202R of RSV-SR transformants, while its suppression by activated ras oncogenes may also take place in some transformants, free of v-src activity [14].
• Glycosylation of catalase inhibitor necessary for activity [15].
• cDNA sequence and deduced amino acid sequence of bovine oviductal fluid catalase [16].

Anatomical context of CAT

• The stimulation of partially purified guanylate cyclase by NO . catalase was similar to that obtained with NO . hemoglobin and with NO . cytochrome P-420 prepared by reaction of hepatic microsomes of phenobarbital-treated rats with NO [17].
• Lipid peroxidation in the submitochondrial particles was not inhibited by the addition of catalase, superoxide dismutase, hydroxyl radical scavengers, or ethylenediaminetetraacetic acid, but was inhibited by the addition of KCN, antimycin-A, NADH, ubiquinol, deferoxamine mesylate, ascorbic acid, and alpha-tocopherol [18].
• Endothelial cells produce H2O2 at an intracellular site in the vicinity of peroxisomes and at a second site near the cell surface that is inaccessible to intracellular catalase or glutathione peroxidase [10].
• Both chromaffin granule lysis and malondialdehyde production were inhibited by the free radical trapping agent butylated hydroxytoluene but not by catalase and/or superoxide dismutase [19].
• A new carnitine palmitoyltransferase (CPT) was purified to homogeneity from bovine liver mitochondria which were 96% free of peroxisomal contamination, as judged by catalase and glutamate dehydrogenase activities [20].

Associations of CAT with chemical compounds

• Transforming growth factor-betas block cytokine induction of catalase and xanthine oxidase mRNA levels in cultured rat cardiac cells [21].
• The function of the bound NADPH, which is tightly bound in bovine liver catalase, has been unknown [22].
• A novel NADPH:(bound) NADP+ reductase and NADH:(bound) NADP+ transhydrogenase function in bovine liver catalase [22].
• Incubation of cells with catalase or treatment of the albumin fraction with isoniazid abolished the stimulation of glucose uptake by polyamines but did not alter the stimulatory effects of insulin or vitamin K5 [23].
• The presence of NO . catalase correlated well with the ability of test solutions to activate purified guanylate cyclase [17].

Regulatory relationships of CAT

• Cytotoxicity caused by bovine serum amine oxidase (5.7 x 10(-3) U/mL) and spermine (340 microM) was completely inhibited by catalase only during short incubation times after which time cytotoxicity occurred [24].

Other interactions of CAT

• Bovine liver catalase, bovine pancreatic insulin, and bovine pancreatic ribonuclease A when individually cospray-dried with lactose showed no extensive initial crystallinity by powder X-ray diffraction, but proteins cospray-dried with mannitol generally showed evidence of mannitol component crystallinity [25].
• However, cyanogen bromide treatment of 2 of the inactive proteins, bovine catalase and concanavalin A from jack bean, yielded peptide fragments which served as substrates for glycosylation [26].
• 2. Through this cyclic reaction of myoglobin between metMb(III) and ferryl-Mb(IV), we proposed that H2O2, one of the potent oxidants in vivo, can be decomposed continuously in cardiac and skeletal muscle tissues in the absence of catalase and peroxidase [27].
• TNF-alpha, IL-1 beta, and antioxidants (superoxide dismutase; catalase; and dimethyl sulfoxide) all induced RBC adhesion to BPAEC [28].

Analytical, diagnostic and therapeutic context of CAT

• There was no significant attenuation in EC injury following incubation with reperfusion effluent stored for 24 h, supplementation with antioxidants (superoxide dismutase + catalase), or inhibition of xanthine oxidase with allopurinol or tungstate [29].
• SDS/PAGE analysis confirmed that alpha-crystallin had formed a soluble complex with catalase after a period of thermal stress [30].
• Two different fractions were present in crystalline bovine liver catalase, and could be resolved using dye-ligand affinity chromatography with Red-A Matrex gel containing Procion HE 3B [3].
• Negatively charged ultrafine silica particles (average diameter 20 nm) were used as support materials for adsorption immobilization of porcine trypsin, horseradish peroxidase, and bovine catalase under various conditions, and the changes in the enzyme activities and the circular dichroism (CD) spectra of these enzymes upon adsorption were measured [31].
• Using a chemical protein modification approach, UV-vis and fluorescence spectroscopies and circular dichroism spectropolarimetry, this study investigates the parameters involved in anti-aggregation mechanism of bovine liver catalase [32].

References