Role of Oxygen Radicals in Peroxidation of Docosahexaenoic Acid by Rat Brain Homogenate in vitro

1987 ◽  
pp. 103-108 ◽  
Author(s):  
T. Shingu ◽  
N. Salem
Keyword(s):  
Docosahexaenoic Acid ◽  
Rat Brain ◽  
Oxygen Radicals ◽  
Brain Homogenate

In vitro anticholinesterase, antimonoamine oxidase and antioxidant properties of alkaloid extracts from kola nuts (Cola acuminata and Cola nitida)

2018 ◽  
Vol 16 (1) ◽  
Author(s):  
Ganiyu Oboh ◽  
Ayokunle O. Ademosun ◽  
Opeyemi B. Ogunsuyi ◽  
Esther T. Oyedola ◽  
Tosin A. Olasehinde ◽  
...  
Keyword(s):  
Side Effects ◽  
Neurodegenerative Diseases ◽  
Rat Brain ◽  
Brain Homogenate ◽  
Oh Radicals ◽  
Mao Inhibitors ◽  
Alkaloid Extracts ◽  
Cola Nitida ◽  
Cola Acuminata

Abstract Background The development of cholinesterase (ChE) and monoamine oxidase (MAO) inhibitors for management of neurodegenerative diseases such as Alzheimer’s disease (AD) has come with their undesirable side effects. Hence, research for potent but natural ChE and MAO inhibitors with little or no side effects is essential. This study investigated the potentials of alkaloid extracts from two Cola species as nutraceuticals for prevention and management of AD. Methods Alkaloid extracts were obtained from two Cola species (Cola nitida [KN] and Cola acuminata [KA]) by solvent extraction method. The extracts were characterized for their alkaloid contents using gas chromatography (GC). The effects of the extracts on ChE and MAO activities were investigated in vitro. Also, the extracts’ ability to inhibit Fe2+-induced lipid peroxidation in rat brain homogenate, scavenge DPPH and OH radicals, as well as chelate Fe2+ were determined. Results GC characterization revealed the presence of augustamine and undulatine as the predominant alkaloids in the extracts. There was no significant (P > 0.05) difference in the inhibitory effects of the extracts on ChE activities. However, KA extract exhibited significantly higher (P < 0.05) MAO inhibitory effect than KN. Also, KA extract inhibited Fe2+- induced malondialdehyde (MDA) production in rat brain homogenate more significantly than KN, while there was no significant difference in DPPH and OH radicals scavenging, as well as Fe2+-chelating abilities of the extracts. Conclusions Our findings revealed that KN and KA alkaloid extracts exhibited significant effect in vitro on biological pathways that may contribute to neuroprotection for the management of neurodegenerative diseases.

An in vitro study of the role of docosahexaenoic acid in human tau protein aggregation

2016 ◽  
Vol 35 (14) ◽  
pp. 3176-3181
Author(s):  
Elham Sadat Mostafavi ◽  
Mohammad Ali Nasiri Khalili ◽  
Sirus Khodadadi ◽  
Gholam Hossein Riazi
Keyword(s):  
Docosahexaenoic Acid ◽  
Protein Aggregation ◽  
Tau Protein ◽  
In Vitro Study ◽  
Vitro Study

scholarly journals Antioxidative Activity of Ferrocenes Bearing 2,6-Di-Tert-Butylphenol Moieties

2010 ◽  
Vol 2010 ◽  
pp. 1-6 ◽  
Author(s):  
E. R. Milaeva ◽  
S. I. Filimonova ◽  
N. N. Meleshonkova ◽  
L. G. Dubova ◽  
E. F. Shevtsova ◽  
...  
Keyword(s):  
Lipid Peroxidation ◽  
Rat Brain ◽  
Antioxidative Activity ◽  
Neuroprotective Effect ◽  
In Vitro Study ◽  
Brain Homogenate ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Calcium Dependent

The antioxidative activity of ferrocenes bearing either 2,6-di-tert-butylphenol or phenyl groups has been compared using DPPH (1,1-diphenyl-2-picrylhydrazyl) test and in the study of the in vitro impact on lipid peroxidation in rat brain homogenate and on some characteristics of rat liver mitochondria. The results of DPPH test at20∘C show that the activity depends strongly upon the presence of phenolic group but is improved by the influence of ferrocenyl fragment. The activity of N-(3,5-di-tert-butyl-4-hydroxyphenyl)iminomethylferrocene (1), for instance, was 88.4%, which was higher than the activity of a known antioxidant 2,6-di-tert-butyl-4-methylphenol (BHT) (48.5%), whereas the activity of N-phenyl-iminomethylferrocene2was almost negligible−2.9%. The data obtained demonstrate that the compounds with 2,6-di-tert-butylphenol moiety are significantly more active than the corresponding phenyl analogues in the in vitro study of lipid peroxidation in rat brain homogenate. Ferrocene1performs a promising behavior as an antioxidant and inhibits the calcium-dependent swelling of mitochondria. These results allow us to propose the potential cytoprotective (neuroprotective) effect of ditopic compounds containing antioxidant 2,6-di-tert-butylphenol group and redox active ferrocene fragment.

Respiratory Activity of Isolated Rat Brain Mitochondria following in vitro Exposure to Oxygen Radicals

1983 ◽  
Vol 3 (2) ◽  
pp. 207-214 ◽  
Author(s):  
Lars Hillered ◽  
Lars Ernster
Keyword(s):  
Xanthine Oxidase ◽  
Rat Brain ◽  
Oxygen Radicals ◽  
Respiratory Activity ◽  
Brain Mitochondria ◽  
Iron Chelate ◽  
Rat Brain Mitochondria ◽  
In Vitro Exposure ◽  
Isolated Rat

Respiratory activity of isolated rat brain mitochondria was measured following in vitro exposure to oxygen radicals. The radicals were generated by hypoxanthine and xanthine oxidase in the presence of a suitable iron chelate and caused a severe inhibition of respiration stimulated by phosphate plus ADP (with malate + glutamate as substrate). The damage could be prevented by catalase or high concentrations of mannitol, but not by superoxide dismutase. A similar effect was observed when hypoxanthine and xanthine oxidase were replaced by glucose and glucose oxidase or by hydrogen peroxide. Most of the findings indicate that the hydroxyl radical is the damaging agent. It is concluded that brain mitochondria exposed to oxygen radicals in vitro show an inhibition of respiratory activity similar to that reported by other investigators as occurring in mitochondria in vivo following transient cerebral ischemia. Therefore, oxygen radicals may contribute to this type of cell damage.

Dual Isoflurane-induced Preconditioning Improves Neuroprotection in Rat Brain In Vitro and the Role of Extracellular Signal-regulated Protein Kinase

2011 ◽  
Vol 26 (1) ◽  
pp. 36-42 ◽  
Author(s):  
Sheng Wang ◽  
Su-xiang Guo ◽  
Zhi-gang Dai ◽  
Xi-wei Dong ◽  
Yang Liu ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Rat Brain ◽  
Extracellular Signal

Bispyridinium Oximes As Antidotal Treatment of Cyclosarin Poisoning—In Vitro and In Vivo Testing

2005 ◽  
Vol 24 (6) ◽  
pp. 399-402 ◽  
Author(s):  
Lucie Bartosova ◽  
Kamil Kuca ◽  
Daniel Jun ◽  
Gabriela Kunesova
Keyword(s):  
Rat Brain ◽  
Organophosphorus Compounds ◽  
Brain Homogenate ◽  
Chemical Structures ◽  
Hi 6 ◽  
In Vivo Testing ◽  
Acetylcholinesterase Enzyme ◽  
Enzyme Source

The mechanism of intoxication with organophosphorus compounds, including highly toxic nerve agents and less toxic pesticides, is based on the formation of irreversibly inhibited acetylcholinesterase, which causes cumulation of neuromediator acetylcholine in synaptic clefts and subsequent overstimulation of cholinergic receptors, that is followed by a generalized cholinergic crisis. Nerve agent poisoning is conventionally treated using a combination of a cholinolytic (atropine mostly) to counteract the accumulation of acetylcholine and acetylcholinesterase reactivators (pralidoxime or obidoxime) to reactivate inhibited acetylcholinesterase. In this study of cyclosarin poisoning treatment, oximes of different chemical structures (obidoxime, HI-6, BI-6, and HS-6) were tested in vitro on rat brain acetylcholinesterase (enzyme source: rat brain homogenate), and afterwards, they were tested in vivo in equimolar doses, in mice and rats. The HI-6 oxime appeared to be the most effective oxime in vitro and in vivo.

Spectrophotometry of b-type cytochromes in rat brain in vivo and in vitro

1989 ◽  
Vol 256 (4) ◽  
pp. C840-C848 ◽  
Author(s):  
C. A. Piantadosi
Keyword(s):  
Low Temperature ◽  
Rat Brain ◽  
Spectral Characteristics ◽  
Brain Homogenate ◽  
Brain Mitochondria ◽  
Oxidation Reduction ◽  
Intact Brain

Terminal oxidase inhibitors such as cyanide (CN) and carbon monoxide (CO) produce different absorption changes in the intact brain, suggesting different mitochondrial responses to the inhibitors. In the present study, the nature of the cytochromes involved in CO and CN responses in vivo was investigated by low-temperature spectroscopy of rat brain, frozen in situ, and of preparations of brain homogenate and isolated mitochondria. Comparison of the spectra from different preparations at the high resolution afforded by low-temperature spectroscopy indicated that absorption responses to CO in vivo originated from mitochondrial b cytochromes. Further detailed spectral analysis of mitochondrial preparations revealed three CN-insensitive b cytochromes in nonsynaptic brain mitochondria; one cytochrome could be reduced by succinate in the presence of CN, the second could be reduced by succinate plus ATP, and the third could be reduced only by anaerobiosis. The spectral characteristics of the mitochondrial b cytochromes, when compared with spectra from CO-exposed brain tissue frozen in situ, strongly implicated the energy-dependent cytochrome b in the oxidation-reduction (redox) responses caused by CO in vivo.

IN VITRO SCREEN OF INHIBITORS OF RAT BRAIN TYROSINE HYDROXYLASE

1967 ◽  
Vol 45 (1) ◽  
pp. 115-131 ◽  
Author(s):  
E. G. McGeer ◽  
P. L. McGeer
Keyword(s):  
Tyrosine Hydroxylase ◽  
Rat Brain ◽  
Inhibitory Activity ◽  
Brain Homogenate ◽  
Inhibitory Effect ◽  
Side Chain ◽  
Complexing Agents ◽  
Hydroxy Groups ◽  
Brain Tyrosine Hydroxylase

Over 600 compounds were tested at 10−4 M concentration as inhibitors of tyrosine hydroxylase activity in crude rat-brain homogenate. Most of the compounds had little or no inhibitory effect and those with strong inhibitory properties were, except for a very few oxidizing and complexing agents, all close structural analogues of tyrosine or of its catechol metabolites. Data obtained in this screen are generally in accord with previous data reported in the literature. For high inhibitory activity in the tyrosine series, side-chain substitution is critical. N-Substitution is particularly undesirable. For high inhibitory activity in the catechol series, the ring hydroxy groups should be 3,4 in relation to a C—C—N side chain. Further ring substitution is undesirable, but some side-chain substitution is permissible.

Sign in / Sign up

Export Citation Format

Share Document