scholarly journals Anti-hyperglycemic activity of encapsulated Java tea-based drink on malondialdehyde formation

2019 ◽  
Vol 9 (4) ◽  
pp. 88-95 ◽  
Keyword(s):  
Malondialdehyde Formation

scholarly journals Salinity Stress Affects Photosynthesis, Malondialdehyde Formation, and Proline Content in Portulaca oleracea L.

Plants ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 845
Author(s):  
Helena Hnilickova ◽  
Kamil Kraus ◽  
Pavla Vachova ◽  
Frantisek Hnilicka
Keyword(s):  
Salt Stress ◽  
Water Potential ◽  
Co2 Concentration ◽  
Co2 Assimilation ◽  
Proline Content ◽  
Portulaca Oleracea ◽  
Control Group ◽  
Malondialdehyde Formation ◽  
Salinity Levels ◽  
Mda Content

In this investigation, the effect of salt stress on Portulaca oleracea L. was monitored at salinity levels of 100 and 300 mM NaCl. At a concentration of 100 mM NaCl there was a decrease in stomatal conductance (gs) simultaneously with an increase in CO2 assimilation (A) at the beginning of salt exposure (day 3). However, the leaf water potential (ψw), the substomatal concentration of CO2 (Ci), the maximum quantum yield of photosystem II (Fv/Fm), and the proline and malondialdehyde (MDA) content remained unchanged. Exposure to 300 mM NaCl caused a decrease in gs from day 3 and a decrease in water potential, CO2 assimilation, and Fv/Fm from day 9. There was a large increase in proline content and a significantly higher MDA concentration on days 6 and 9 of salt stress compared to the control group. After 22 days of exposure to 300 mM NaCl, there was a transition from the C4 cycle to crassulacean acid metabolism (CAM), manifested by a rapid increase in substomatal CO2 concentration and negative CO2 assimilation values. These results document the tolerance of P. oleracea to a lower level of salt stress and the possibility of its use in saline localities.

scholarly journals Pecan pericarp extract protects against carbon tetrachloride-induced liver injury through oxidative mechanism in rats

2020 ◽  
Vol 9 (5) ◽  
pp. 652-660
Author(s):  
Hallegue Dorsaf ◽  
Moujahed Sabrine ◽  
Ben Lamine Houda ◽  
Ben Rhouma Khémais ◽  
Sakly Mohsen ◽  
...  
Keyword(s):  
Carbon Tetrachloride ◽  
Structural Integrity ◽  
Histopathological Examination ◽  
Hepatoprotective Activity ◽  
Hepatic Tissue ◽  
Inflammatory Infiltration ◽  
Liver Histopathology ◽  
Malondialdehyde Formation ◽  
Hepatic Lipid Peroxidation ◽  
Group 2

Abstract The purpose of this study was to quantify the proanthocyanidin content of pecan (Carya illinoinensis) pericarp extract (PPE) and to assess its useful impacts against carbon tetrachloride (CCl4)-induced hepatotoxicity. Rats were randomly divided into four groups: Group 1: received intraperitoneal injection of saline solution, Group 2: was injected with PPE (25 mg/kg body weight) for 10 consecutive days, Group 3: received CCl4 (0.5 ml/kg, subcutaneous injection), Group 4: was coadministred with PPE + CCl4. The CCl4 was administered every 3 days during 10 days. Results revealed the presence of a high amount of total proanthocyanidins in the PPE (81.01 ± 0.21 mg TAE.g−1DW). CCl4 injection induced significant reductions in hepatic antioxidants but increased hepatic lipid peroxidation (LPO) as well as serum injury biomarkers. However, cotreatment with PPE significantly (P < 0.05) inverted CCl4-induced increase in plasma alanine aminotransferase, aspartate aminotransferase, alkaline phosphatase, and lactate dehydrogenase activities, respectively to 74%, 77%, 60%, and 82% compared with CCl4 group. No significant toxic effects were observed following treatment with plant extract alone. PPE cotreatment also decreased significant (P < 0.05) the hepatic malondialdehyde formation (21%) and enhanced the liver catalase activity (107%) in CCl4-intoxicated rats. The histopathological examination showed inflammatory infiltration and degenerative changes in the hepatic tissue following CCl4 injection. The hepatoprotective activity of PPE against CCl4 exposure was supported by the maintenance of structural integrity of liver histopathology. In conclusion, the current study illustrated that PPE pretreatment significantly improved all examined parameters, restored the hepatic architecture and successfully alleviates oxidative damage induced by CCl4 intoxication.

Influence of Platelet Activation on Erythrocyte Deformability

1983 ◽  
Vol 49 (02) ◽  
pp. 084-086 ◽  
Author(s):  
W Palinski ◽  
A Torsellini ◽  
L Doni
Keyword(s):  
Arachidonic Acid ◽  
Acetylsalicylic Acid ◽  
Platelet Activation ◽  
Platelet Rich Plasma ◽  
Plasma Viscosity ◽  
Erythrocyte Deformability ◽  
Direct Influence ◽  
Antagonistic Action ◽  
Malondialdehyde Formation ◽  
Autologous Platelet

SummaryErythrocyte deformability was demonstrated to be influenced by platelet activation. Deformability of erythrocytes suspended in autologous platelet poor plasma (PPP), obtained from platelet rich plasma (PRP), was significantly reduced when PRP had previously been incubated with a platelet activating substance (arachidonic acid, adrenaline or ADP). The possibility of a direct influence of the activating substance on erythrocyte deformability was examined and malondialdehyde formation was determined as an indicator of platelet activation. Erythrocyte deformability was not impaired when endoperoxide formation in platelets was blocked by an inhibitor of cyclooxigenase (acetylsalicylic acid). Plasma viscosity was not influenced by platelet activation as demonstrated by filtration and viscosimetry. Recent studies showed that prostacyclin (PGI2) increases erythrocyte deformability (1). The antagonistic action between prostacyclin released by vessel walls and products of platelet metabolism being well known, we discuss possible mechanisms of this effect and pathophysiological relevance of our results.

scholarly journals Some effects of vitamin E and selenium deprivation on tissue enzyme levels and indices of tissue peroxidation in rainbow trout (Salmo gairdneri)

1985 ◽  
Vol 53 (1) ◽  
pp. 149-157 ◽  
Author(s):  
J. G. Bell ◽  
C. B. Cowey ◽  
J. W. Adron ◽  
Aileen M. Shanks
Keyword(s):  
Rainbow Trout ◽  
Vitamin E ◽  
Peroxidase Activity ◽  
Cumene Hydroperoxide ◽  
Dietary Vitamin ◽  
Salmo Gairdneri ◽  
Deficient Diet ◽  
Exudative Diathesis ◽  
Malondialdehyde Formation

1. Duplicate groups of rainbow trout (Salrno gairdnert) (mean weight 11 g) were given for 40 weeks one of four partially purified diets that were either adequate or low in selenium or vitamin E or both.2. Weight gains of trout given the dually deficient diet were significantly lower than those of trout given a complete diet or a diet deficient in Se. No mortalities occurred and the only pathology seen was exudative diathesis in the dually deficient trout.3. There was significant interaction between the two nutrients both with respect to packed cell volume and to malondialdehyde formation in the in vitro NADPH-dependent microsomal lipid peroxidation system.4. Tissue levels of vitamin E and Se decreased to very low levels in trout given diets lacking these nutrients. For plasma there was a significant effect of dietary vitamin E on Se concentration.5. Glutathione (GSH) peroxidase (EC 1. 1 1. 1.9) activity in liver and plasma was significantly lower in trout receiving low dietary Se but was independent of vitamin E intake. The ratios of hepatic GSH peroxidase activity measured with cumene hydroperoxide and hydrogen peroxide were the same for all treatments. This confirms the absence of a Se-independent GSH peroxidase activity in trout liver.6. Se deficiency did not lead to any compensatory increase in hepatic GSH transferase (EC 2. 5. 1. 18) activity; values were essentially the same in all treatments.7. Plasma pyruvate kinase (EC 2. 7. 1.40) activity increased significantly in the trout deficient in both nutrients. This was thought to be due to leakage of the enzyme from the muscle and may be indicative of incipient (subclinical) muscle damage.

scholarly journals F1F0-ATPase, early target of the radical initiator 2,2′-azobis-(2-amidinopropane) dihydrochloride in rat liver mitochondria in vitro

1996 ◽  
Vol 320 (2) ◽  
pp. 571-576 ◽  
Author(s):  
Frédéric BEAUSEIGNEUR ◽  
Marc GOUBERN ◽  
Marie-France CHAPEY ◽  
Joseph GRESTI ◽  
Catherine VERGELY ◽  
...  
Keyword(s):  
Permeability Transition ◽  
Liver Mitochondria ◽  
Proton Channel ◽  
Rat Liver Mitochondria ◽  
Antioxidant Defences ◽  
Radical Initiator ◽  
Malondialdehyde Formation ◽  
Respiratory Chain Activity ◽  
F1fo Atpase

This study was designed to determine which enzyme activities were first impaired in mitochondria exposed to 2,2′-azobis-(2-amidinopropane) dihydrochloride (AAPH), a known radical initiator. EPR spin-trapping revealed generation of reactive oxygen species although malondialdehyde formation remained very low. With increasing AAPH concentrations, State-3 respiration was progressively depressed with unaltered ADP/O ratios. A top-down approach demonstrated that alterations were located at the phosphorylation level. As shown by inhibitor titrations, ATP/ADP translocase activity was unaffected in the range of AAPH concentrations used. In contrast, AAPH appeared to exert a deleterious effect at the level of F1FO-ATPase, comparable with dicyclohexylcarbodi-imide, which alters FO proton channel. A comparison of ATP hydrolase activity in uncoupled and broken mitochondria reinforced this finding. In spite of its pro-oxidant properties, AAPH was shown to act as a dose-dependent inhibitor of cyclosporin-sensitive permeability transition initiated by Ca2+, probably as a consequence of its effect on F1FO-ATPase. Resveratrol, a potent antiperoxidant, completely failed to prevent the decrease in State-3 respiration caused by AAPH. The data suggest that AAPH, when used under mild conditions, acted as a radical initiator and was capable of damaging F1FO-ATPase, thereby slowing respiratory chain activity and reducing mitochondrial antioxidant defences.

Cyclosporin a increased malondialdehyde formation in EBV-infected human B cells is inhibited by Vitamin E

2006 ◽  
Vol 130 (2) ◽  
pp. 322
Author(s):  
C. Chen ◽  
T.D. Johnston ◽  
H. Jeon ◽  
M. Ibrahim ◽  
D. Ranjan
Keyword(s):  
Vitamin E ◽  
B Cells ◽  
Cyclosporin A ◽  
Human B Cells ◽  
Malondialdehyde Formation
Sign in / Sign up

Export Citation Format

Share Document