Ascorbate interacts with sodium selenite to increase glutathione peroxidase activity in selenium-deficient chick duodena cultured in vitro

1989 ◽  
Vol 20 (1-2) ◽  
pp. 87-94 ◽  
Author(s):  
Mary S. Cupp ◽  
Gerald F. Combs ◽  
Robert A. Corradino
Keyword(s):  
Glutathione Peroxidase ◽  
Peroxidase Activity ◽  
Sodium Selenite ◽  
Glutathione Peroxidase Activity

Increased glutathione peroxidase activity in human blood mononuclear cells upon in vitro incubation with n-3 fatty acids

1994 ◽  
Vol 47 (8) ◽  
pp. 1315-1323 ◽  
Author(s):  
Catherine Joulain ◽  
Annie F. Prigent ◽  
Georges Némoz ◽  
Michel Lagarde
Keyword(s):  
Fatty Acids ◽  
Glutathione Peroxidase ◽  
Human Blood ◽  
Peroxidase Activity ◽  
Mononuclear Cells ◽  
Glutathione Peroxidase Activity ◽  
In Vitro Incubation ◽  
Blood Mononuclear Cells

Vitamin E protection of obesity-enhanced vascular calcification in uremic rats

2014 ◽  
Vol 306 (4) ◽  
pp. F422-F429 ◽  
Author(s):  
A. Peralta-Ramírez ◽  
A. Montes de Oca ◽  
A. I. Raya ◽  
C. Pineda ◽  
I. López ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Vitamin E ◽  
Glutathione Peroxidase ◽  
Peroxidase Activity ◽  
Calcium Concentration ◽  
Soft Tissues ◽  
Zucker Rats ◽  
Glutathione Peroxidase Activity ◽  
Obese Rats

This study aimed to determine the extent of extraskeletal calcification in uremic Zucker rats, by comparing obese and lean phenotypes, and to evaluate the influence of vitamin E (VitE) on the development of calcifications in both uremic rats and human vascular smooth muscle cells (HVSMCs) cultured in vitro. Zucker rats of lean and obese phenotypes with normal renal function [control (C); C-lean and C-obese groups] and with uremia [5/6 nephrectomy (Nx); Nx-lean and Nx-obese groups] and uremic rats treated with VitE (Nx-lean + VitE and Nx-obese + VitE groups) were studied. Uremic groups were subjected to Nx, fed a 0.9% phosphorus diet, and treated with calcitriol (80 ng/kg ip). The aortic calcium concentration was significantly higher ( P < 0.05) in Nx-obese rats (10.0 ± 2.1 mg/g tissue) than in Nx-lean rats (3.6 ± 1.3 mg/g tissue). A decrease in plasma glutathione peroxidase activity was observed in Nx-obese rats compared with Nx-lean rats (217.2 ± 18.2 vs. 382.3 ± 15.5 nmol·min−1·ml−1, P < 0.05). Treatment with VitE restored glutathione peroxidase activity and reduced the aortic calcium concentration to 4.6 ± 1.3 mg/g tissue. The differences in mineral deposition between Nx-lean, Nx-obese, Nx-lean + VitE, and Nx-obese + VitE rats were also evidenced in other soft tissues. In HVSMCs incubated with high phosphate, VitE also prevented oxidative stress and reduced calcium content, bone alkaline phosphatase, and gene expression of core-binding factor-α1. In conclusion, uremic obese rats develop more severe calcifications than uremic lean rats and VitE reduces oxidative stress and vascular calcifications in both rats and cultures of HVSMCs.

In Vivo and in Vitro Variations of Human Erythrocyte Glutathione Peroxidase Activity as Result of Cells Ageing, Selenium Availability and Peroxide Activation

1978 ◽  
Vol 39 (3) ◽  
pp. 399-408 ◽  
Author(s):  
G. Perona ◽  
G. C. Guidi ◽  
A. Piga ◽  
R. Cellerino ◽  
R. Menna ◽  
...  
Keyword(s):  
Glutathione Peroxidase ◽  
Peroxidase Activity ◽  
Human Erythrocyte ◽  
Glutathione Peroxidase Activity ◽  
Peroxide Activation

Glutathione Peroxidase And Malondialdehyde Production In The Arachidonic Acid Metabolism Of Human Platelets

1981 ◽  
Author(s):  
G C Guidi ◽  
R Schiavon ◽  
G L Avventi ◽  
G Perona
Keyword(s):  
Arachidonic Acid ◽  
Glutathione Peroxidase ◽  
Peroxidase Activity ◽  
Acid Metabolism ◽  
Inverse Correlation ◽  
Human Platelets ◽  
Arachidonic Acid Metabolism ◽  
Glutathione Peroxidase Activity ◽  
Physiological Variations

A series of functional parameters, including the aggregability triggered by various agents, the in vitro malondialdehyde production and the glutathio ne peroxidase activity, has been investigated in platelets from normal blood donors.Glutathione peroxidase activity assays showed a significant inverse correlation with malondialdehyde induced by arachidonic acid but not with aggregation data and malondialdehyde induced by thrombin. Moreover, arachidonic acid generates in human platelets lysates large amounts of hydrogen acceptor substrate(s) for the glutathione peroxidase with peculiar kinetic features. These are related to ma londialdehyde production and to partial inhibition by acetyl-salicilic acid and are likely connected with prostaglandin metabolism.Our data suggest that physiological variations in glutathione peroxidase activity are important in human platelet arachidonic acid metabolism, because they modulate the biosynthesis of key end-products, as thromboxane A2, whose malondialdehyde is an inde.

scholarly journals Two immunologically distinct Yc-type subunits are present in rat lung glutathione S-transferases

1984 ◽  
Vol 224 (1) ◽  
pp. 335-338 ◽  
Author(s):  
S V Singh ◽  
Y C Awasthi
Keyword(s):  
Glutathione Peroxidase ◽  
Rat Liver ◽  
Peroxidase Activity ◽  
Gel Electrophoresis ◽  
Rat Lung ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase ◽  
Two Dimensional Gel Electrophoresis ◽  
Glutathione S Transferases

Two types of 25 000-Mr subunits are present in rat lung glutathione S-transferase I (pI 8.8). These subunits, designated Yc and Yc', are immunologically and functionally distinct from each other. The homodimers YcYc (pI 10.4) and Yc'Yc' (pI 7.6) obtained by hybridization in vitro of the two subunits of glutathione S-transferase I (pI 8.8) were isolated and characterized. Results of these studies indicate that only the Yc subunits express glutathione peroxidase activity and cross-react with the antibodies raised against glutathione S-transferase B (YaYc) or rat liver. The Yc' subunits do not express glutathione peroxidase activity and do not cross-react with the antibodies raised against glutathione S-transferase B of rat liver. The amino acid compositions of these two subunits are also different. These two subunits can also be separated by the two-dimensional gel electrophoresis of glutathione S-transferase I (pI 8.8) of rat lung.

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