Superoxide Dismutase Activity in Two Different Wild-Type Strains of Drosophila melanogaster

Gerontology ◽  
1981 ◽  
Vol 27 (4) ◽  
pp. 205-208 ◽  
Author(s):  
Harold R. Massie ◽  
Trevor R. Williams ◽  
Valerie R. Aiello
Keyword(s):  
Superoxide Dismutase ◽  
Superoxide Dismutase Activity ◽  
Wild Type ◽  
Type Strains ◽  
Drosophila Melanogaste

scholarly journals characterIstIcs of an antIoxIdant actIvIty of YERSINIA PESTIS wIth dIfferent plasmId spectrum

2016 ◽  
Vol 1 (5) ◽  
pp. 133-137
Author(s):  
Токмакова ◽  
Elena Tokmakova ◽  
Витязева ◽  
Svetlana Vityazeva ◽  
Иванова ◽  
...  
Keyword(s):  
Experimental Data ◽  
Antioxidant Activity ◽  
Superoxide Dismutase ◽  
Yersinia Pestis ◽  
Superoxide Dismutase Activity ◽  
Wild Type ◽  
Complex Study ◽  
Pathogenic Activity ◽  
The Common ◽  
High Peroxide

Experimental data concerning complex study of antioxidant activity of Y. pestis with different plasmid spectrum (wild-type Yersinia pestis subsp. pestis, Yersinia pestis subsp. altaica and their isogenic variants) are represented in the article. Superoxide dismutase activity of the tested Y.pestis strains was from 6.0 to 9.0×109 microbe cells. Signifi-cant differences between the Y.pestis strains with different plasmid composition were not detected by this parameter. Our results, consistent with the data of other authors, tell that superoxide dismutase activity is a thermo-inducible feature and does nоt depend on a plasmid spectrum. High peroxide destroying activity was also detected in all tested Y.pestis strains. The differences between the strains regarding their common peroxide destroying activity were found. This parameter of the plague microbe strains lacking pYP plasmid was at least 3times lower than common peroxide destroying activity in strains with this plasmid in the genome. In our opinion these revealed differences were caused by characteristics of plasmid spectrum. The common peroxide destroying activity’s degree of Y.pestis strains can be associated with the presence of pYP plasmid in the genome. The isogenic variants of Y.pestis strains lacking one of the plasmids had smaller pathogenic activity. This fact points to the need for further study of these strains.

Factors relating to the aerotolerance of Spirillum volutans

1986 ◽  
Vol 32 (7) ◽  
pp. 548-552 ◽  
Author(s):  
Penelope J. Padgett ◽  
Noel R. Krieg
Keyword(s):  
Superoxide Dismutase ◽  
Peroxidase Activity ◽  
Catalase Activity ◽  
Casein Hydrolysate ◽  
Superoxide Dismutase Activity ◽  
Wild Type ◽  
Aerobic Growth ◽  
Air Atmosphere ◽  
Sequential Selection ◽  
One Step

A variant of the microaerophile Spirillum volutans capable of growth under an air atmosphere (21% oxygen) was obtained by sequential selection and stabilization of colonies able to grow on a casein hydrolysate – succinate – potassium metabisulfite medium under an atmosphere of 14, 16, 18, 20, and finally 21% O2. A small amount of bisulfite (0.0025%) was still required, however, for aerobic growth. Both the variant and the wild type lacked catalase activity, and they had the same levels of superoxide dismutase activity. However, the mutant possessed 13 times more donor: hydrogen-peroxide oxidoreductase (peroxidase) activity (0.008 IU) than the wild type (0.0006 IU). An aerotolerant mutant was also isolated in one step by treatment with the mutagenic agent ethyl methane sulfonate, followed by incubation under 21% O2; it was found to possess approximately three times the peroxidase activity of the wild type. This mutant lacked catalase activity and the level of superoxide dismutase activity it contained was comparable with the wild type.

Diazoxide Modulates Cardiac Hypertrophy by Targeting H2O2 Generation and Mitochondrial Superoxide Dismutase Activity

2020 ◽  
Vol 13 (1) ◽  
pp. 76-83
Author(s):  
Aline Maria Brito Lucas ◽  
Joana Varlla de Lacerda Alexandre ◽  
Maria Thalyne Silva Araújo ◽  
Cicera Edna Barbosa David ◽  
Yuana Ivia Ponte Viana ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Cardiac Hypertrophy ◽  
Superoxide Dismutase Activity ◽  
Heart Weight ◽  
Pharmacological Intervention ◽  
Wall Thickening ◽  
H2o2 Production ◽  
Mitochondrial Superoxide ◽  
Mitochondrial Superoxide Dismutase

Background: Cardiac hypertrophy involves marked wall thickening or chamber enlargement. If sustained, this condition will lead to dysfunctional mitochondria and oxidative stress. Mitochondria have ATP-sensitive K+ channels (mitoKATP) in the inner membrane that modulate the redox status of the cell. Objective: We investigated the in vivo effects of mitoKATP opening on oxidative stress in isoproterenol- induced cardiac hypertrophy. Methods: Cardiac hypertrophy was induced in Swiss mice treated intraperitoneally with isoproterenol (ISO - 30 mg/kg/day) for 8 days. From day 4, diazoxide (DZX - 5 mg/kg/day) was used in order to open mitoKATP (a clinically relevant therapy scheme) and 5-hydroxydecanoate (5HD - 5 mg/kg/day) or glibenclamide (GLI - 3 mg/kg/day) were used as mitoKATP blockers. Results: Isoproterenol-treated mice had elevated heart weight/tibia length ratios (HW/TL). Additionally, hypertrophic hearts had elevated levels of carbonylated proteins and Thiobarbituric Acid Reactive Substances (TBARS), markers of protein and lipid oxidation. In contrast, mitoKATP opening with DZX avoided ISO effects on gross hypertrophic markers (HW/TL), carbonylated proteins and TBARS, in a manner reversed by 5HD and GLI. Moreover, DZX improved mitochondrial superoxide dismutase activity. This effect was also blocked by 5HD and GLI. Additionally, ex vivo treatment of isoproterenol- induced hypertrophic cardiac tissue with DZX decreased H2O2 production in a manner sensitive to 5HD, indicating that this drug also acutely avoids oxidative stress. Conclusion: Our results suggest that diazoxide blocks oxidative stress and reverses cardiac hypertrophy. This pharmacological intervention could be a potential therapeutic strategy to prevent oxidative stress associated with cardiac hypertrophy.

scholarly journals Identification ofvib-1, a Locus Involved in Vegetative Incompatibility Mediated byhet-cinNeurospora crassa

Genetics ◽  
2002 ◽  
Vol 162 (1) ◽  
pp. 89-101 ◽  
Author(s):  
Qijun Xiang ◽  
N Louise Glass
Keyword(s):  
Acid Phosphatase ◽  
Recognition System ◽  
Deletion Mutants ◽  
Wild Type ◽  
Vegetative Incompatibility ◽  
Death Rates ◽  
Self Recognition ◽  
Allelic Differences ◽  
Native Gel ◽  
Type Strains

AbstractA non-self-recognition system called vegetative incompatibility is ubiquitous in filamentous fungi and is genetically regulated by het loci. Different fungal individuals are unable to form viable heterokaryons if they differ in allelic specificity at a het locus. To identify components of vegetative incompatibility mediated by allelic differences at the het-c locus of Neurospora crassa, we isolated mutants that suppressed phenotypic aspects of het-c vegetative incompatibility. Three deletion mutants were identified; the deletions overlapped each other in an ORF named vib-1 (vegetative incompatibility blocked). Mutations in vib-1 fully relieved growth inhibition and repression of conidiation conferred by het-c vegetative incompatibility and significantly reduced hyphal compartmentation and death rates. The vib-1 mutants displayed a profuse conidiation pattern, suggesting that VIB-1 is a regulator of conidiation. VIB-1 shares a region of similarity to PHOG, a possible phosphate nonrepressible acid phosphatase in Aspergillus nidulans. Native gel analysis of wild-type strains and vib-1 mutants indicated that vib-1 is not the structural gene for nonrepressible acid phosphatase, but rather may regulate nonrepressible acid phosphatase activity.

scholarly journals HET-E and HET-D Belong to a New Subfamily of WD40 Proteins Involved in Vegetative Incompatibility Specificity in the Fungus Podospora anserina

Genetics ◽  
2002 ◽  
Vol 161 (1) ◽  
pp. 71-81
Author(s):  
Eric Espagne ◽  
Pascale Balhadère ◽  
Marie-Louise Penin ◽  
Christian Barreau ◽  
Béatrice Turcq
Keyword(s):  
Genetic Difference ◽  
Podospora Anserina ◽  
Wild Type ◽  
Incompatible Interaction ◽  
Vegetative Incompatibility ◽  
Repeat Domain ◽  
Upper Face ◽  
E1a Gene ◽  
Type Strains ◽  
Wd40 Repeats

Abstract Vegetative incompatibility, which is very common in filamentous fungi, prevents a viable heterokaryotic cell from being formed by the fusion of filaments from two different wild-type strains. Such incompatibility is always the consequence of at least one genetic difference in specific genes (het genes). In Podospora anserina, alleles of the het-e and het-d loci control heterokaryon viability through genetic interactions with alleles of the unlinked het-c locus. The het-d2Y gene was isolated and shown to have strong similarity with the previously described het-e1A gene. Like the HET-E protein, the HET-D putative protein displayed a GTP-binding domain and seemed to require a minimal number of 11 WD40 repeats to be active in incompatibility. Apart from incompatibility specificity, no other function could be identified by disrupting the het-d gene. Sequence comparison of different het-e alleles suggested that het-e specificity is determined by the sequence of the WD40 repeat domain. In particular, the amino acids present on the upper face of the predicted β-propeller structure defined by this domain may confer the incompatible interaction specificity.

scholarly journals Two New Compounds From the Heartwood of Dalbergia melanoxylon and Their Protective Effect on Hypoxia/Reoxygenation Injury in H9c2

2021 ◽  
Vol 16 (1) ◽  
pp. 1934578X2098777
Author(s):  
Yang Liu ◽  
Ni Zhang ◽  
Jun-wei He ◽  
Lan-ying Chen ◽  
Li Yang ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Lactate Dehydrogenase ◽  
Protective Effect ◽  
Superoxide Dismutase Activity ◽  
Spectral Evidence ◽  
Reoxygenation Injury ◽  
Dalbergia Melanoxylon ◽  
New Compounds ◽  
Hypoxia Reoxygenation

A new neoflavonoid, named as (7 R)-(-)-3′,5-dihydroxy-4′,2,4-trimethoxy-dalbergiquinol (1) and a new phenanthrenedione, named as 3′,7-dihydroxy-3,6- dimethoxy-9-phenyl-1,4-phenanthrenedione (2), together with 4 known compounds, 5- O-methyldalbergiphenol (3), 3′,7-dihydroxy-4′,3,6-trimethoxy-9-phenyl-1,4-phenanthrenedione (4), (+)-obtusafuran (5), and melanoxin (6) were isolated from the heartwood of Dalbergia melanoxylon. Their structures were elucidated on the basis of chemical and spectral evidence, as well as by comparison with literature data. Moreover, compound 1 showed a protective effect on hypoxia/reoxygenation injury in H9c2 at 10.0 μM by decreasing lactate dehydrogenase and malondialdehyde activity and enhancing superoxide dismutase activity.

scholarly journals Isolation of a gene required for programmed initiation of development by Aspergillus nidulans.

1992 ◽  
Vol 12 (9) ◽  
pp. 3827-3833 ◽  
Author(s):  
T H Adams ◽  
W A Hide ◽  
L N Yager ◽  
B N Lee
Keyword(s):  
Life Cycle ◽  
Aspergillus Nidulans ◽  
Optimal Growth ◽  
Growth Conditions ◽  
Nutrient Deprivation ◽  
Deletion Mutants ◽  
Wild Type ◽  
Microbial Development ◽  
Type Strains ◽  
Posttranscriptional Level

In contrast to many other cases in microbial development, Aspergillus nidulans conidiophore production initiates primarily as a programmed part of the life cycle rather than as a response to nutrient deprivation. Mutations in the acoD locus result in "fluffy" colonies that appear to grow faster than the wild type and proliferate as undifferentiated masses of vegetative cells. We show that unlike wild-type strains, acoD deletion mutants are unable to make conidiophores under optimal growth conditions but can be induced to conidiate when growth is nutritionally limited. The requirement for acoD in conidiophore development occurs prior to activation of brlA, a primary regulator of development. The acoD transcript is present both in vegetative hyphae prior to developmental induction and in developing cultures. However, the effects of acoD mutations are detectable only after developmental induction. We propose that acoD activity is primarily controlled at the posttranscriptional level and that it is required to direct developmentally specific changes that bring about growth inhibition and activation of brlA expression to result in conidiophore development.

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