Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P04179 (MnSOD)
 2,777 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

cDNAs coding for human manganese-containing superoxide dismutase (Mn SOD) have been isolated from a human liver and a dibutyryl cyclic AMP differentiated U937 cDNA library constructed in vector lambda gtll. The nucleotide sequences of the insert cDNAs had an opening reading frame coding for 222 amino acid residues. The first 24 amino acids of the primarily translated polypeptide might constitute the leader peptide for transport of the precursors to the mitochondria. Differentiation of the U937 cells with dibutyryl cyclic AMP resulted in a 70% decrease in Mn SOD mRNA. The amino acid sequences of the mature Mn SODs of human, rat and mouse are highly conserved, while the sequences of the leader peptides of these species are moderately conserved.
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PMID:Isolation and characterization of complementary DNAs encoding human manganese-containing superoxide dismutase. 283 Oct 93

The amount of Mn superoxide dismutase (MnSOD) and the activity of Cu,Zn-superoxide dismutase (CuZnSOD) have been studied in human fibroblasts of five subjects with trisomy 21 and five subjects with normal karyotype, using nuclear magnetic relaxation and polarographic methods. In the trisomic fibroblasts we have found a mean molar amount of MnSOD 25.4% lower than in the control, and an amount of CuZnSOD 54.7% higher. A positive significant correlation between the activities of both enzymes has been observed indicating that the two enzymes dismute the O2- cooperatively. However, the increase of MnSOD per unit of CuZnSOD appears significantly lower in the trisomic fibroblasts, an effect that is not due to a diminished inducibility of MnSOD. These findings suggest that the MnSOD and CuZnSOD genes interact to preserve the normal level of total SOD activity.
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PMID:Coordinate expression of Mn-containing superoxide dismutase and Cu,Zn-containing superoxide dismutase in human fibroblasts with trisomy 21. 293 98

Brain trauma was induced in rats by impact of a steel bar on the head with a force such that damage (as measured by neurological scoring) was reversible in fourteen days. Systemic treatment (intraperitoneal injections) with free bovine copper superoxide dismutase or a liposomal form of the enzyme considerably shortened recovery time to less than half. Tests included cranial nerves--cornean and aural reflexes, and sensorial motricity functions--gripping reflexes, displacement reactions, recovery and flexion reflexes, equilibrium tests and spontaneous mobility. Normalisation of EEG recordings was also greatly accelerated in the case of treated animals. No changes of brain glutathione peroxidase, glutathione transferase or Mn superoxide dismutase in traumatized animals were observed. However a slight decrease in Cu-SOD occurs. Cerebral lipoperoxidation is increased in the traumatized animals compared with controls. This increase is reduced on treatment of the rats with liposomal SOD (or the free enzyme). Very small amounts of the exogenous SOD pass the brain barrier, the permeability of which is increased in traumatized animals. The enzyme is particularly concentrated in the cortex. Despite apparent total neurological recovery at 15 days for untreated traumatized animals, significant differences in EEG recordings, in percentage cerebral water content and in histological examination of brain tissue of these controls compared with treated animals were observed with a net improvement in the latter case. The results obtained with this model suggest that clinical treatment of coma states and brain traumas with liposomal superoxide dismutase may have certain advantages over orthodox treatments.
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PMID:Treatment of brain trauma with liposomal superoxide dismutase. 322 60

Mg2+, Ca2+, Mn2+, Zn2+, and Cu content of neurons from chick embryo cortex cultivated in chemically defined serum free growth medium was determined by energy dispersive X-ray fluorescence and atomic absorption spectroscopy. The intracellular volume of cultured neurons was determined to be 2.73 microliters/mg. Intracellular Mn2+, Fe2+, Zn2+, and Cu2+ in the cultivated neurons were 100-200 times the concentrations in the growth medium: Mg2+ and Ca2+ were 0.9 and 1.7 mM respectively, around 20 fold higher than in growth medium. Mg2+, Fe2+, Cu2+ and Zn2+ concentrations in neurons were in the range of ca. 300-600 microM, approximately 2-3 times the values previously reported in glial cells; Ca2+ and Mn2+ content of the neurons were higher by 5 and 10 fold respectively compared to glial cells. In neurons, the subcellular distribution of Fe2+, Cu2+, and Mn2+ follows the rank order: cytosol greater than microsomes greater than mitochondria; for Zn2+ the distribution differs as following: cytosol greater than mitochondria greater than microsomes. Determination of the superoxide dismutase activities in the cultivated neurons indicated that the Mn2+ linked activity predominates whereas, the Cu-Zn dependent enzyme is dominant in glial cells. Enrichment of the culture medium with Mn2+ to 2.5 microM enhanced the Mn-SOD by approximately 33% but the Cu2+-Zn2+ enzyme activity was not modified. The high Mn2+ content, the capacity to accumulate Mn2+, and the predominancy of the Mn-SOD form observed in neurons is in accord with a fundamental functional role for this metal ion in this type of brain cells.
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PMID:Levels and sub-cellular distribution of physiologically important metal ions in neuronal cells cultured from chick embryo cerebral cortex. 323 9

Methods have been developed for the measurements of catalase and superoxide dismutase (SOD) in single, isolated muscle fibers. These fibers are also classified according to fiber type. Catalase is determined using a fluorescent method for the measurement of hydrogen peroxide consumed. SOD measurements are carried out using a modification of established techniques whereby the inhibition of oxidation of epinephrine by SOD is assayed fluorometrically. Both enzymes may be determined in submicrogram samples of dried muscle. This approach avoids the complication of the inclusion of nonmuscle tissue with varying enzymatic activities which is frequently experienced when using homogenates of muscle, particularly diseased muscle. In addition, these techniques can be used to determine the inherent variation in SOD and catalase activities within individual fibers of the same fiber type. The Km and Vmax for catalase, determined using homogenates of human muscle, were found to be 12 mM and 1.45 mumol/min/mg dry wt, respectively. Catalase of muscle was inhibited 50% by 2 microM sodium azide. Mn-SOD contributes less than one-fifth of the total SOD activity. Therefore the activity is largely due to the Cu-Zn form of SOD. These methods are applicable to a wide variety of tissues.
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PMID:Micromethods in single muscle fibers. 1. Determination of catalase and superoxide dismutase. 323 59

In the absence or in the presence of 10(-4)M EDTA cytosolic and lysosomal CuZnSOD and MnSOD activities were differentiated as enzymatic and nonenzymatic (SOD-like). Both activities were about three times lower in mitochondrial matrix compared to those in cytosol and lysosomes. The cytosolic and lysosomal CuZnSOD showed an equal electrophoretic pattern: three peaks of SOD activity with Rf values of 1 = 0.10 and 0.12; 2 = 0.16 and 0.18; 3 = 0.21 and 0.22, respectively. The low anodic mobility was explained by the high isoelectric points (pI) of the three CuZnSOD isoenzymes (approximately 5.7, approximately 6.5 and approximately 7.5) contained both in cytosol and in lysosomes.
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PMID:Studies on the nature of superoxide dismutase activity in sheep liver subcellular fractions. 324 59

This assay for superoxide dismutase (SOD, EC 1.15.1.1) activity involves inhibition of nitroblue tetrazolium reduction, with xanthine-xanthine oxidase used as a superoxide generator. By using a reaction terminator, we can determine 40 samples within 55 min. One unit of activity of pure bovine liver Cu,ZnSOD and chicken liver MnSOD was expressed by 30 ng and 500 ng of protein, respectively. The mean concentrations of Cu,ZnSOD as measured by this method in blood from normal adults were 242 (SEM 4) mg/L in erythrocytes, 548 (SEM 20) micrograms/L in serum, and 173 (SEM 11) micrograms/L in plasma. The Cu,ZnSOD concentrations in serum and plasma of patients with cancer of the large intestine tended to be less and greater than these values, respectively, but not statistically significantly so.
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PMID:A simple method for clinical assay of superoxide dismutase. 334 99

Various superoxide dismutases from different sources, containing Cu, Mn or Fe at the active centre, have been examined with respect to anti-inflammatory activity in a model using adriamycin-induced edema in rats. Very large differences in efficiency are observed, the most active being E. coli Mn-SOD and bovine Cu-SOD. The Fe-SOD from E. coli is active whereas P. leiognathi Fe-SOD is not. Human Mn-SOD shows no significant activity and homologous rat Cu-SOD is totally inactive. Yeast Cu-SOD shows pro-inflammatory properties. Anti-inflammatory activity is not a function of molecular weight or circulation life-time.
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PMID:Anti-inflammatory activity of superoxide dismutases: inhibition of adriamycin induced edema in rats. 350 38

Comparison of superoxide dismutases from different sources with respect to biological activity in the rat tourniquet poditis model shows that anti-ischemic activity is very variable although all the enzymes have the same specific enzymic activity. Both bovine Cu-SOD and E. coli Mn-SOD have excellent properties whereas yeast Cu-SOD and the homologous rat Cu-SOD show zero activity. The results confirm earlier demonstrations that (1) "All superoxide dismutases are equal but some are more equal than others", (2) at the dose levels used (compatible with possible clinical use) homologous enzyme is inefficient and hence human Cu-SOD may not be effective in humans, (3) liposomal encapsulation of bovine Cu-SOD greatly enhances biological efficacity, provides a slow release mechanism of the enzyme and provides a powerful drug for the treatment of ischemic injury.
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PMID:Comparative anti-inflammatory activity of different superoxide dismutases and liposomal SOD in ischemia. 350 53

The anti-arthritic activities of various superoxide dismutases and of liposomal bovine Cu-SOD have been compared in the adjuvant induced Lewis Inbred Rat model. Various approaches, including plethysmometric measurements, red cell sedimentation rates, while cell counts, levels of IgA and IgG immunoglobulins and scoring by visual, radiographic and scintigraphic techniques all concord in a demonstration of different activities for different SODs. The most efficient are liposomal bovine Cu-SOD and E. coli Mn-SOD, a moderate activity being shown by free bovine Cu-SOD. Poor or zero results are obtained with human Mn-SOD, human Cu-SOD or the homologous rat Cu-SOD.
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PMID:Anti-inflammatory activity of superoxide dismutases: studies on adjuvant induced polyarthritis in rats. 350 1


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