Superoxide dismutase activity and reduced glutathione content in cataractous lens of patients with glucose-6-phosphate dehydrogenase deficiency

1987 ◽  
Vol 8 (3) ◽  
pp. 191-195 ◽  
Author(s):  
A. Vanella ◽  
G. Gorgone ◽  
N. Cavallaro ◽  
C. Castorina ◽  
A. Campisi ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Dehydrogenase Deficiency ◽  
Reduced Glutathione ◽  
Superoxide Dismutase Activity ◽  
Cataractous Lens ◽  
Glucose 6 Phosphate Dehydrogenase

scholarly journals Equine Glucose-6-phosphate Dehydrogenase Deficiency

1994 ◽  
Vol 31 (5) ◽  
pp. 518-527 ◽  
Author(s):  
S. L. Stockham ◽  
J. W. Harvey ◽  
D. A. Kinden
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
G6pd Deficiency ◽  
Dehydrogenase Deficiency ◽  
Reduced Glutathione ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Electron Microscopic ◽  
Transmission Electron ◽  
Transmission Electron Microscopic ◽  
Reduced Nicotinamide Adenine Dinucleotide ◽  
Glucose 6 Phosphate Dehydrogenase

Glucose-6-phosphate dehydrogenase (G6PD) deficiency is a well-characterized X-linked inherited disorder in humans but has not been reported in horses. We describe a persistent hemolytic anemia and hyperbilirubinemia due to a severe G6PD deficiency in an American Saddlebred colt. Other abnormalities in the colt's erythrocytes as compared with those of healthy horses ( n = 22–35) included increased activities of hexokinase and pyruvate kinase, decreased concentrations of reduced glutathione and reduced nicotinamide adenine dinucleotide phosphate (NADP), and increased concentration of oxidized NADP. Morphologic abnormalities included eccentrocytosis, pyknocytosis, anisocytosis, macrocytosis, and increased number of Howell-Jolly bodies. Scanning and transmission electron microscopic examinations revealed that eccentrocytes had contracted to spherical regions and thin collapsed regions. Eccentrocytes were more electron dense than were normal erythrocytes when examined by transmission electron microscopy. When exposed to acetylphenylhydrazine, erythrocytes from the G6PD-deficient colt produced more and smaller Heinz bodies than did erythrocytes from normal horses. Abnormalities in the colt's dam included presence of eccentrocytes and pyknocytes; her average erythrocyte G6PD activity was slightly below the range of reference values.

scholarly journals Effect of catalase inactivation on levels of inorganic peroxides, superoxide dismutase, glutathione, oxygen consumption and life span in adult houseflies (Musca domestica)

1983 ◽  
Vol 216 (2) ◽  
pp. 503-506 ◽  
Author(s):  
R G Allen ◽  
K J Farmer ◽  
R S Sohal
Keyword(s):  
Superoxide Dismutase ◽  
Oxygen Consumption ◽  
Life Span ◽  
Musca Domestica ◽  
Catalase Activity ◽  
Reduced Glutathione ◽  
Superoxide Dismutase Activity ◽  
Adaptive Responses ◽  
Total Inhibition ◽  
Rate Of Oxygen Consumption

The effects of total inhibition of catalase, induced by 3-amino-1,2,4-triazole, on the adult housefly (Musca domestica) were examined. The lack of catalase activity had no effect on the longevity of the houseflies. Inorganic-peroxide concentration was elevated at younger ages, but declined in older flies. The rate of oxygen consumption by the flies was greatly decreased and the levels of oxidized as well as reduced glutathione were augmented. Superoxide dismutase activity showed a slight increase. This study suggests that loss of catalase activity does not affect survival of houseflies due to adaptive responses.

Superoxide Dismutase Activity and Reduced Glutathione Content in Erythrocytes of Uremic Patients on Chronic Dialysis

1983 ◽  
Vol 70 (5) ◽  
pp. 312-315 ◽  
Author(s):  
A. Vanella ◽  
E. Geremia ◽  
R. Pinturo ◽  
P. Tiriolo ◽  
G. Liuzzo ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Reduced Glutathione ◽  
Superoxide Dismutase Activity ◽  
Chronic Dialysis ◽  
Uremic Patients

scholarly journals Melatonin and garlic cytoprotective-ameliorative effects on dibutyl phthalate intoxication on sperm DNA and testicular biomakers of rabbits

2020 ◽  
Vol 18 (3) ◽  
pp. 158-166
Author(s):  
M Shinkut ◽  
T Aluwong ◽  
P.I. Rekwot ◽  
A.I. Nwannenna ◽  
F.U. Samuel
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Dibutyl Phthalate ◽  
Reduced Glutathione ◽  
Superoxide Dismutase Activity ◽  
Dna Integrity ◽  
Sperm Dna Fragmentation ◽  
Activity Increase ◽  
Sperm Dna ◽  
Group B

The study investigated the cytoprotective and ameliorative effects of melatonin and Allium sativum (garlic) on dibutyl phthalate (DBP)-induced oxidative stress, its impact on sperm DNA integrity and testicular oxidative stress biomarkers. Forty two rabbit bucks were randomly divided into 7 groups of 6 bucks each labeled as A, B, C, D, E, F and G: The treatment were as follows: A (served as negative control, received olive oil for 16 weeks); B (served as positive control, exposed to DBP for 16 weeks, no treatment); C (given melatonin for 8 weeks, thereafter DBP for 8 weeks); D (administered garlic for 8 weeks, thereafter DBP for 8 weeks); E (exposed to DBP for 8 weeks, thereafter melatonin for 8 week); F (exposed to DBP for 8 weeks, thereafter garlic for 8 weeks); and G (exposed to DBP for 8 weeks, thereafter melatonin + garlic for 8 weeks). Ejaculated semen was collected on the last day (112th) using artificialv vagina for rabbit and pooled for each group was used for sperm DNA fragmentation index (SDFI) determination, rabbits were sacrificed and the testes harvested for determination of superoxide dismutase activity, reduced glutathione and malondialdehyde concentration. Results showed a significant increase (P = 0.0018) in the mean SDFI in group B (78.20 ± 4.72), compared to other groups. A significant increase (P ≤ 0.0001) in superoxide dismutase activity, increase reduced glutathione concentration and decrease malondialdehyde concentrations in the treatment groups compared to the DBP exposed group without treatment (group B) were observed. Melatonin and garlic demonstrated cytoprotective and ameliorative effects against DBP-induced oxidative stress in rabbit bucks. Keywords: Dibutyl phthalate, Garlic, Melatonin, Sperm DNA, Testicular biomarkers

scholarly journals Sulfhemoglobinemia and Acute Hemolytic Anemia with Heinz Bodies Following Contact with a Fungicide— Zinc Ethylene Bisdithiocarbamate—in a Subject with Glucose-6-Phosphate Dehydrogenase Deficiency and Hypocatalasemia

Blood ◽  
1963 ◽  
Vol 21 (4) ◽  
pp. 484-494 ◽  
Author(s):  
JACK PINKHAS ◽  
MEIR DJALDETTI ◽  
HENRY JOSHUA ◽  
CHAIM RESNICK ◽  
ANDRÉ DE VRIES
Keyword(s):  
Red Blood Cells ◽  
Hemolytic Anemia ◽  
Blood Cells ◽  
Dehydrogenase Deficiency ◽  
Reduced Glutathione ◽  
Body Formation ◽  
Low Glucose ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Enzymatic Defect

Abstract Sulfhemoglobinemia associated with Heinz body formation and acute hemolytic anemia following contact with a fungicide, zinc ethylene bisdithiocarbamate, is described in a Persian Jew whose red blood cells had low glucose-6-phosphate dehydrogenase activity with low and unstable reduced glutathione and low catalase activity. The fungicide, similarly to acetylphenylhydrazine, was capable of decreasing in vitro the reduced glutathione of the patient’s red blood cells, as well as of those of other subjects with the same enzymatic defect. The sulfhemoglobinemia and the hemolytic anemia are considered to have been produced independently by the fungicide, the glucose-6-phosphate dehydrogenase deficiency having played a role only in the latter. The possibility that the hypocatalasemia was a factor in rendering the patient’s red blood cells sensitive to the hemolysis- and sulfhemoglobin-producing action of the fungicide is discussed. The importance of zinc ethylene bisdithiocarbamate as a sulfhemoglobin-producing and hemolytic agent is stressed, in view of the widespread use of this fungicide.

SUPEROXIDE DISMUTASE ACTIVITY AND REDUCED GLUTATHIONE LEVELS IN Cu-OVERLOAD LIVER FROM SHEEP

1997 ◽  
Vol 17 (1) ◽  
pp. 115-123 ◽  
Author(s):  
Aldo S Sansinanea ◽  
Silvia I Cerone ◽  
Sergio A Streitenberger ◽  
Cecilia García ◽  
Nestor Auza
Keyword(s):  
Superoxide Dismutase ◽  
Reduced Glutathione ◽  
Superoxide Dismutase Activity
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