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.

scholarly journals Kolanut consumption, its benefits and side effects

2020 ◽  
Vol 8 (3) ◽  
pp. 356-362
Author(s):  
Adejoke Adebusola Adelusi ◽  
Qudus Adebayo Ogunwolu ◽  
Chinweike Abednego Ugwu ◽  
Modinat Adewunmi Alli ◽  
Kehinde Ademola Adesanya ◽  
...  
Keyword(s):  
Health Status ◽  
Side Effects ◽  
West Africa ◽  
Energy Drinks ◽  
Sweet Taste ◽  
Common Food ◽  
Desk Research ◽  
Cola Nitida ◽  
Cola Acuminata ◽  
Kola Tree

This article assessed kolanut consumption, its benefits and side effects. Kolanut is the fruit of the kola tree, which is indigenous to West Africa. The two main varieties are Cola acuminata and Cola nitida. It is the most common masticatory in Nigeria, and is quite bitter but gives a sweet taste after chewing. A desk research was done using various published literatures on kolanut. It was unveiled that the consumption of kolanut has many benefits as well as side effects. The side effects are dependent on the quantity intake of caffeine, a significant substance present in kolanut. Caffeine is a stimulant like theobromine and kolanin, which are also present in coffee, tea and chocolate. Kolanuts are chewed fresh and are also in the form of extracts, which is common food flavouring found in energy drinks. Right amount of kolanut depends on factors such as age, physiology and health status, and as such, more effort should be channeled into the area of investigating more appropriate quantity of kolanut that should be consumed in relation to people’s status.

scholarly journals Cryo-EM structure of alpha-synuclein fibrils amplified by PMCA from PD and MSA patient brains

2021 ◽  
Author(s):  
Domenic Burger ◽  
Alexis Fenyi ◽  
Luc Bousset ◽  
Henning Stahlberg ◽  
Ronald Melki
Keyword(s):  
Multiple System Atrophy ◽  
Parkinson Disease ◽  
Neurodegenerative Diseases ◽  
Protein Misfolding ◽  
Brain Homogenate ◽  
Alpha Synuclein ◽  
Water Interface ◽  
Control Brain ◽  
Air Water Interface

Synucleinopathies are neurodegenerative diseases related to the aggregation of the protein alpha-synuclein (aSyn). Among these diseases, Parkinson disease (PD) and multiple system atrophy (MSA) are most prevalent. aSyn can readily form different fibrillar polymorphs, if exposed to an air-water interface or by templating with pre-existing fibrils. We here report the structures of three fibrillar polymorphs that were obtained after seeding monomeric aSyn with PD and MSA patients brain homogenates using protein misfolding cyclic amplification (PMCA). Seeding with a control brain homogenate did not produce fibrils, and seeding with other in vitro generated fibrillar polymorphs as a control faithfully produced polymorphs of a different type. The here determined fibril structures from PD and MSA brain tissue represent new folds, which partly resemble that of previously reported in vitro generated fibrils from Y39 phosphorylated aSyn protein. The relevance of these fibrils for synucleinopathies in humans remains to be further investigated.

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.

scholarly journals Inhibition of neural phospholipase D activity by aminoglycoside antibiotics

1991 ◽  
Vol 279 (1) ◽  
pp. 319-321 ◽  
Author(s):  
M Liscovitch ◽  
V Chalifa ◽  
M Danin ◽  
Y Eli
Keyword(s):  
Side Effects ◽  
Rat Brain ◽  
Phospholipase D ◽  
Aminoglycoside Antibiotics ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Brain Membranes ◽  
Rat Brain Membranes ◽  
Isolated Rat

The effects of aminoglycoside antibiotics on phospholipase D (PLD) activity were investigated in permeabilized NG108-15 cells and in isolated rat brain membranes. Neomycin inhibited guanosine 5′-[gamma-thio]triphosphate-stimulated PLD activity in digitonin-permeabilized NG108-15 cells in a concentration-dependent manner (50% inhibition at 100 microM). Neomycin similarly inhibited PLD activity present in rat brain membranes and assayed in vitro with [3H]phosphatidylcholine as substrate (50% inhibition at 65 microM). Other aminoglycosides tested (kanamycin, geneticin and streptomycin) were nearly equipotent inhibitors of rat brain PLD. These results indicate that aminoglycoside antibiotics inhibit phosphatidylcholine-PLD activity with comparable and sometimes greater potency than their well known inhibition of phosphoinositide-phospholipase C. The possibility that PLD inhibition could mediate some of the toxic side effects of aminoglycosides is suggested.

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.

scholarly journals The biosynthesis of brain gangliosides. Ganglioside-glycosylating activity in rat brain neuronal perikarya fraction

1978 ◽  
Vol 174 (3) ◽  
pp. 673-680 ◽  
Author(s):  
H J F Maccioni ◽  
S S Defilpo ◽  
C A Landa ◽  
R Caputto
Keyword(s):  
Rat Brain ◽  
Time Course ◽  
Brain Homogenate ◽  
Acetylneuraminic Acid ◽  
Synaptosomal Fraction ◽  
Old Rats ◽  
Brain Gangliosides

Rat brain homogenate and the synaptosmal and neuronal perikarya fractions from 17-day-old rats were compared for their activities in sialosylating endogenous gangliosides and transferring N-acetylneuraminic acid and galactose to several glycolipids in vitro. The sialosylation of endogenous gangliosides and the activities of sialosyltransferases acting either on lactosylceramide or haematoside as acceptors, as well as galactosyltransferase acting on Tay-Sachs ganglioside as acceptor, were between 3-and 12-fold higher in the neuronal perikarya fraction than in whole homgenate on a protein or ganglioside basis. The activities found in the synaptosomal fraction were negligible. No evidence was found to indicate that the low activities in this fraction were due to the presence of inhibitors of the transfer activities or to inacessibility of the substrates to their respective enzymes. These findings, and the time course of labelling of gangliosides of the neuronal perikarya and synaptosomes from rats that received an injection of N-[3H]acetylmannosamine, indicate that the main cellular site of glycosylation of neuronal gangliosides is in the neuronal perikarya.

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