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)

Our laboratories previously isolated a putative extracellular or membrane-associated Cu/Zn superoxide dismutase (Cu/Zn-SOD) gene, designated a signal peptide-containing (SP) Cu/Zn-SOD, from Schistosoma mansoni. SOD activity was thus investigated throughout the life cycle of S. mansoni and found in all stages: eggs, miracidia, cercariae, schistosomula, lung-stage worms, and adult worms. The adult worms had the highest SOD activity (53 +/- 9 nitrite units), which was five times higher than that of eggs or miracidia and twice as high as that of 3-h-old mechanically transformed schistosomula. Cu/Zn-SOD constituted over 95% of the total SOD activity found in S. mansoni, compared with that of Mn-SOD. Most of Cu/Zn-SOD specific activity was associated with a detergent-extractable fraction of the parasite. Isoelectric focusing gel electrophoresis analysis revealed that there were four major pI variants of Cu/Zn-SOD present in the adult worms. Only two of these Cu/Zn-SOD pI variants were present in the 3-h-old mechanically transformed schistosomula. Fast protein liquid chromatography gel filtration fractionation of adult parasite extract was carried out to correlate the SP Cu/Zn-SOD with the SOD activity by using anti-SP Cu/Zn-SOD monoclonal antibodies, which separated the immunoreactive gene product and the SOD activity into different fractions. Quantitative tissue fractionation also revealed a discordant distribution of the gene product compared with that of Cu/Zn-SOD activity. These results indicated the existence of another Cu/Zn-SOD(s) in the parasite. Purification of the Cu/Zn-SOD activity from the adult worms showed that it represented the two lower-pI variants found in both adult worms and 3-h-old schistosomula. Peptide sequence analysis of the purified Cu/Zn-SOD confirmed that there is a second form of Cu/Zn-SOD in the parasite.
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PMID:Identification and purification of a second form of Cu/Zn superoxide dismutase from Schistosoma mansoni. 150 Jan 73

Genetic strains of the snail Biomphalaria glabrata vary in their resistance to the parasite Schistosoma mansoni. Phagocytic cells (hemocytes) circulating in the hemolymph of B. glabrata play an essential role in the snail's innate immune response. Hemocytes of resistant B. glabrata kill S. mansoni in vitro via a mechanism which involves a respiratory burst. Reactive oxygen species (ROS), which are products of the respiratory burst, can act as mediators of both oxidative damage and of immune-related intracellular signaling pathways. One specific ROS, hydrogen peroxide (H2O2), has been shown to be involved in hemocyte-mediated sporocyst killing. We tested the hypothesis that Cu/Zn superoxide dismutase (SOD), a cytosolic enzyme that catalyzes the conversion of superoxide anion to H2O2, is somehow different between resistant and susceptible snail strains. We report a hemocyte transcript with all the features of a typical cytosolic Cu/Zn SOD (GenBank accession numbers AY505496 and AY505497). The amount of Cu/Zn SOD mRNA in hemocytes from resistant snails was double that of hemocytes from susceptible snails, and this correlated directly with an increased Cu/Zn SOD enzymatic activity in resistant hemocytes. Additional experiments determined that in vitro interaction/encapsulation of sporocysts did not influence Cu/Zn SOD mRNA levels in hemocytes from either snail strain. Thus, resistance in this host-parasite system does not appear to depend on a transcriptional response of hemocyte Cu/Zn SOD, but may be due, at least in part, to a constitutively elevated enzymatic level of Cu/Zn SOD.
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PMID:Constitutive differences in Cu/Zn superoxide dismutase mRNA levels and activity in hemocytes of Biomphalaria glabrata (Mollusca) that are either susceptible or resistant to Schistosoma mansoni (Trematoda). 1538 2