Survival role of superoxide dismutase 1 on human granulosa luteinized cells in vitroSurvival role of superoxide dismutase 1 on human granulosa luteinized cells in vitro

2011 ◽  
Vol 45 (04) ◽  
pp. 175-181
Author(s):  
J. Dineva ◽  
I. Vangelov ◽  
R. Abrashev ◽  
K. Todorova ◽  
D. Gulenova ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Superoxide Dismutase 1

Potential Role of the Porcine Superoxide Dismutase 1 (SOD1) Gene in Pig Reproduction

2013 ◽  
Vol 24 (1) ◽  
pp. 1-9 ◽  
Author(s):  
D. Bjerre ◽  
L. B. Madsen ◽  
T. Mark ◽  
S. Cirera ◽  
K. Larsen ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Potential Role ◽  
Superoxide Dismutase 1 ◽  
Sod1 Gene

scholarly journals The Role of 2% Rebamipide Eye Drops Related to Conjunctival Differentiation in Superoxide Dismutase-1 (Sod1) Knockout Mice

2018 ◽  
Vol 59 (3) ◽  
pp. 1675 ◽  
Author(s):  
Takashi Kojima ◽  
Cem Simsek ◽  
Ayako Igarashi ◽  
Kazue Aoki ◽  
Kazunari Higa ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Knockout Mice ◽  
Eye Drops ◽  
Superoxide Dismutase 1

scholarly journals Oxidation of the Tryptophan 32 Residue of Human Superoxide Dismutase 1 Caused by Its Bicarbonate-dependent Peroxidase Activity Triggers the Non-amyloid Aggregation of the Enzyme

2014 ◽  
Vol 289 (44) ◽  
pp. 30690-30701 ◽  
Author(s):  
Fernando R. Coelho ◽  
Asif Iqbal ◽  
Edlaine Linares ◽  
Daniel F. Silva ◽  
Filipe S. Lima ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Peroxidase Activity ◽  
Oxidation Products ◽  
Superoxide Dismutase 1 ◽  
Amyloid Aggregation ◽  
Post Translational Modifications ◽  
Covalent Dimer ◽  
Als Patients ◽  
Lateral Sclerosis

The role of oxidative post-translational modifications of human superoxide dismutase 1 (hSOD1) in the amyotrophic lateral sclerosis (ALS) pathology is an attractive hypothesis to explore based on several lines of evidence. Among them, the remarkable stability of hSOD1WT and several of its ALS-associated mutants suggests that hSOD1 oxidation may precede its conversion to the unfolded and aggregated forms found in ALS patients. The bicarbonate-dependent peroxidase activity of hSOD1 causes oxidation of its own solvent-exposed Trp32 residue. The resulting products are apparently different from those produced in the absence of bicarbonate and are most likely specific for simian SOD1s, which contain the Trp32 residue. The aims of this work were to examine whether the bicarbonate-dependent peroxidase activity of hSOD1 (hSOD1WT and hSOD1G93A mutant) triggers aggregation of the enzyme and to comprehend the role of the Trp32 residue in the process. The results showed that Trp32 residues of both enzymes are oxidized to a similar extent to hSOD1-derived tryptophanyl radicals. These radicals decayed to hSOD1-N-formylkynurenine and hSOD1-kynurenine or to a hSOD1 covalent dimer cross-linked by a ditryptophan bond, causing hSOD1 unfolding, oligomerization, and non-amyloid aggregation. The latter process was inhibited by tempol, which recombines with the hSOD1-derived tryptophanyl radical, and did not occur in the absence of bicarbonate or with enzymes that lack the Trp32 residue (bovine SOD1 and hSOD1W32F mutant). The results support a role for the oxidation products of the hSOD1-Trp32 residue, particularly the covalent dimer, in triggering the non-amyloid aggregation of hSOD1.

scholarly journals Cleavage of folates during ethanol metabolism. Role of acetaldehyde/xanthine oxidase-generated superoxide

1989 ◽  
Vol 257 (1) ◽  
pp. 277-280 ◽  
Author(s):  
S Shaw ◽  
E Jayatilleke ◽  
V Herbert ◽  
N Colman
Keyword(s):  
Superoxide Dismutase ◽  
Xanthine Oxidase ◽  
Folinic Acid ◽  
Folate Deficiency ◽  
Ethanol Metabolism

Although folate deficiency and increased requirements for folate are observed in most alcoholics, the possibility that acetaldehyde generated from ethanol metabolism may increase folate catabolism has not been previously demonstrated. Folate cleavage was studied in vitro during the metabolism of acetaldehyde by xanthine oxidase, measured as the production of p-aminobenzoylglutamate from folate using h.p.l.c. Acetaldehyde/xanthine oxidase generated superoxide, which cleaved folates (5-methyltetrahydrofolate greater than folinic acid greater than folate) and was inhibited by superoxide dismutase. Cleavage was increased by addition of ferritin and inhibited by desferrioxamine (a tight chelator of iron), suggesting the importance of catalytic iron. Superoxide generated from the metabolism of ethanol to acetaldehyde in the presence of xanthine oxidase in vivo may contribute to the severity of folate deficiency in the alcoholic.

An Intersubunit Disulfide Bond Prevents in Vitro Aggregation of a Superoxide Dismutase-1 Mutant Linked to Familial Amytrophic Lateral Sclerosis†

Biochemistry ◽  
2004 ◽  
Vol 43 (17) ◽  
pp. 4899-4905 ◽  
Author(s):  
Soumya S. Ray ◽  
Richard J. Nowak ◽  
Konstantin Strokovich ◽  
Robert H. Brown ◽  
Thomas Walz ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Disulfide Bond ◽  
Superoxide Dismutase 1 ◽  
Lateral Sclerosis

scholarly journals Role of the (Mn)superoxide dismutase of Enterococcus faecalis in the in vitro interaction with microglia

Microbiology ◽  
2011 ◽  
Vol 157 (6) ◽  
pp. 1816-1822 ◽  
Author(s):  
Samuele Peppoloni ◽  
Brunella Posteraro ◽  
Bruna Colombari ◽  
Lidia Manca ◽  
Axel Hartke ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Enterococcus Faecalis ◽  
Stress Responses ◽  
Peritoneal Macrophages ◽  
Infection Process ◽  
Microglial Cells ◽  
Infection Model

Enterococcus faecalis is a significant human pathogen worldwide and is responsible for severe nosocomial and community-acquired infections. Although enterococcal meningitis is rare, mortality is considerable, reaching 21 %. Nevertheless, the pathogenetic mechanisms of this infection remain poorly understood, even though the ability of E. faecalis to avoid or survive phagocytic attack in vivo may be very important during the infection process. We previously showed that the manganese-cofactored superoxide dismutase (MnSOD) SodA of E. faecalis was implicated in oxidative stress responses and, interestingly, in the survival within mouse peritoneal macrophages using an in vivo–in vitro infection model. In the present study, we investigated the role of MnSOD in the interaction of E. faecalis with microglia, the brain-resident macrophages. By using an in vitro infection model, murine microglial cells were challenged in parallel with the wild-type strain JH2-2 and its isogenic sodA deletion mutant. While both strains were phagocytosed by microglia efficiently and to a similar extent, the ΔsodA mutant was found to be significantly more susceptible to microglial killing than JH2-2, as assessed by the antimicrobial protection assay. In addition, a significantly higher percentage of acidic ΔsodA-containing phagosomes was found and these also underwent enhanced maturation as determined by the expression of endolysosomal markers. In conclusion, these results show that the MnSOD of E. faecalis contributes to survival of the bacterium in microglial cells by influencing their antimicrobial activity, and this could even be important for intracellular killing in neutrophils and thus for E. faecalis pathogenesis.

scholarly journals Role of Superoxide in Catalase-Peroxidase-Mediated Isoniazid Action against Mycobacteria

1998 ◽  
Vol 42 (3) ◽  
pp. 709-711 ◽  
Author(s):  
Jian-Ying Wang ◽  
Richard M. Burger ◽  
Karl Drlica
Keyword(s):  
Superoxide Dismutase ◽  
Mycobacterium Smegmatis ◽  
Enzyme Complex ◽  
Bacteriostatic Activity ◽  
Catalase Peroxidase ◽  
Superoxide Dismutase Gene

ABSTRACT Isoniazid (INH) activation in vitro is associated with reduction of the mycobacterial ferric KatG catalase-peroxidase by hydrazine and reaction with O2 to form an oxyferrous enzyme complex. Since this complex could also form directly via reaction of ferric KatG with superoxide, intracellular activation might be responsive to superoxide concentration. When Mycobacterium smegmatiscarrying the M. bovis katG gene was treated with nontoxic levels of plumbagin, a generator of superoxide, the bacteriostatic activity of INH increased unless a plasmid-borne superoxide dismutase gene was also present. Thus, endogenous superoxide probably contributes to intracellular activation of INH.

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