High ammonia levels decrease brain acetylcholinesterase activity both in vivo and in vitro

1994 ◽  
Vol 22 (3) ◽  
pp. 177-184 ◽  
Author(s):  
Elena Kosenko ◽  
Yuri Kaminsky ◽  
Maria-Dolores Miñana ◽  
Santiago Grisolia ◽  
Vicente Felipo
Keyword(s):  
Acetylcholinesterase Activity ◽  
High Ammonia ◽  
Brain Acetylcholinesterase

Alanine Reverses the Inhibitory Effect of Phenylalanine on Acetylcholinesterase Activity

2002 ◽  
Vol 57 (5-6) ◽  
pp. 506-511 ◽  
Author(s):  
Stylianos Tsakiris ◽  
Kleopatra H. Schulpis
Keyword(s):  
Ache Activity ◽  
Acetylcholinesterase Activity ◽  
Competitive Inhibitor ◽  
Inhibitory Effect ◽  
Electrophorus Electricus ◽  
Enzyme Stimulation ◽  
Brain Acetylcholinesterase ◽  
Competitive Activation

The aim of this work was to evaluate, in vitro, the effect of ʟ-alanine (Ala) on suckling rat brain acetylcholinesterase (AChE) and on eel Electrophorus electricus pure AChE inhibited by ʟ-phenylalanine (Phe) as well as to investigate whether Phe or Ala is a competitive inhibitor or an effector of the enzyme. AChE activity was determined in brain homogenates and in the pure enzyme after 1 h preincubation with 1.2 mm of Phe or Ala as well as with Phe plus Ala. The activity of the pure AChE was also determined using as a substrate different amounts of acetylthiocholine. Ala reversed completely the inhibited AChE by Phe (18-20% in 500-600 μᴍ substrate, p<0.01). Lineweaver-Burk plots showed that Vmax remained unchanged. However, KM was found increased with Phe (150%, p<0.001), decreased with Ala alone (50%, p<0.001) and unaltered with Phe plus Ala. It is suggested that: a) Phe presents a competitive inhibitory action with the substrate whereas Ala a competitive activation; b) Ala competition with Phe might unbind the latter from AChE molecule inducing the enzyme stimulation; c) Ala might reverse the inhibitory effect of Phe on brain AChE in phenylketonuric patients, if these results are extended into the in vivo reality.

scholarly journals Structure-Antifouling Activity Relationship and Molecular Targets of Bio-Inspired(thio)xanthones

Biomolecules ◽  
2020 ◽  
Vol 10 (8) ◽  
pp. 1126 ◽  
Author(s):  
Joana R. Almeida ◽  
Andreia Palmeira ◽  
Alexandre Campos ◽  
Isabel Cunha ◽  
Micaela Freitas ◽  
...  
Keyword(s):  
Acetylcholinesterase Activity ◽  
Qsar Model ◽  
Artemia Salina ◽  
Activity Relationship ◽  
Predictive Capacity ◽  
Antifouling Activity ◽  
In Silico Studies ◽  
Mussel Adhesive

The development of alternative ecological and effective antifouling technologies is still challenging. Synthesis of nature-inspired compounds has been exploited, given the potential to assure commercial supplies of potential ecofriendly antifouling agents. In this direction, the antifouling activity of a series of nineteen synthetic small molecules, with chemical similarities with natural products, were exploited in this work. Six (4, 5, 7, 10, 15 and 17) of the tested xanthones showed in vivo activity toward the settlement of Mytilus galloprovincialis larvae (EC50: 3.53–28.60 µM) and low toxicity to this macrofouling species (LC50 > 500 µM and LC50/EC50: 17.42–141.64), and two of them (7 and 10) showed no general marine ecotoxicity (<10% of Artemia salina mortality) after 48 h of exposure. Regarding the mechanism of action in mussel larvae, the best performance compounds 4 and 5 might be acting by the inhibition of acetylcholinesterase activity (in vitro and in silico studies), while 7 and 10 showed specific targets (proteomic studies) directly related with the mussel adhesive structure (byssal threads), given by the alterations in the expression of Mytilus collagen proteins (PreCols) and proximal thread proteins (TMPs). A quantitative structure-activity relationship (QSAR) model was built with predictive capacity to enable speeding the design of new potential active compounds.

PET imaging of the in vivo brain acetylcholinesterase activity and nicotine binding in galantamine-treated patients with AD

2008 ◽  
Vol 29 (8) ◽  
pp. 1204-1217 ◽  
Author(s):  
A. Kadir ◽  
T. Darreh-Shori ◽  
O. Almkvist ◽  
A. Wall ◽  
M. Grut ◽  
...  
Keyword(s):  
Pet Imaging ◽  
Acetylcholinesterase Activity ◽  
Brain Acetylcholinesterase

In vivo and in vitro effects of aluminum on the activity of mouse brain acetylcholinesterase

2002 ◽  
Vol 59 (1) ◽  
pp. 41-45 ◽  
Author(s):  
P Zatta ◽  
M Ibn-Lkhayat-Idrissi ◽  
P Zambenedetti ◽  
M Kilyen ◽  
T Kiss
Keyword(s):  
Mouse Brain ◽  
In Vitro Effects ◽  
Brain Acetylcholinesterase

scholarly journals Neuroprotective Effects of the Herbal Formula B401 in Both Cell and Mouse Models of Alzheimer’s Disease

2016 ◽  
Vol 2016 ◽  
pp. 1-17 ◽  
Author(s):  
Chih-Hsiang Hsu ◽  
Sheue-Er Wang ◽  
Ching-Lung Lin ◽  
Chun-Jen Hsiao ◽  
Shuenn-Jyi Sheu ◽  
...  
Keyword(s):  
Cell Model ◽  
Acetylcholinesterase Activity ◽  
Herbal Formula ◽  
Protective Effects ◽  
Neuroprotective Effects ◽  
Neurocognitive Dysfunctions ◽  
Subcutaneous Blood Flow ◽  
Triple Transgenic Mouse

In this study, we have reported the herbal formula B401 that has neuroprotective effects via multifunction, multitarget characteristics. It is possible that the herbal formula B401 may also provide new insights for AD. Here, we studied protective effects in the Tet-On Aβ42-GFP SH-SY5Y cell model and the APP/PS1/Tau triple transgenic mouse model by the herbal formula B401. Inin vitroexperiments, we showed that the herbal formula B401 treatment effectively reduces glutamate-induced excitotoxicity and acetylcholinesterase activity in Tet-On Aβ42-GFP SH-SY5Y cells. Inin vivoexperiments, we found that oral B401 treatment effectively ameliorates neurocognitive dysfunctions of 3× Tg-AD mice via motor and cognitive behavior tests. By using magnetic resonance imaging, moorFLPI instruments, and chemiluminescence methods, we reported that oral B401 treatment effectively alleviates brain atrophy, improves subcutaneous blood flow, and reduces blood ROS in 3× Tg-AD mice. As observed from results of immunohistochemistry staining and western blotting, we found that oral B401 treatment significantly enhances expressions of neuroprotective proteins, while reducing expressions of AD derived proteins such as amyloid beta, phosphorylated Tau, neurofibrillary tangles, and 3-nitrotyrosine in the brain of 3× Tg-AD mice. Thus, the herbal formula B401 may have the potential to be developed into optimum TCM for AD patients.

scholarly journals Changes of Cholinesterase Activity in the Erythrocytes, Plasma, Diaphragm, Liver and Various Parts of the Brain in the Rabbit Following Transfusion of Erythrocytes with Soman Inhibited Acetylcholinesterase

1997 ◽  
Vol 40 (2) ◽  
pp. 37-39
Author(s):  
Jiří Kassa ◽  
Jiří Bajgar ◽  
Josef Fusek
Keyword(s):  
Blood Transfusion ◽  
Cholinesterase Activity ◽  
Acetylcholinesterase Activity ◽  
Significant Inhibition ◽  
Peripheral Compartment ◽  
Peripheral Tissues ◽  
Cholinesterase Activities ◽  
The Brain

1. The changes of cholinesterase activity in rabbit blood, peripheral tissues and the central nervous system following transfusion of erythrocytes with soman inhibited acetylcholinesterase were demonstrated. 2. After incubation with soman for 0.5 or 24 h, erythrocytes without acetylcholinesterase activity were injected to intact rabbits and cholinesterase activity in the erythrocytes, plasma, diaphragm, liver and various parts of the brain were evaluated 24 h following blood-transfusion. 3. When erythrocytes were incubated with soman for 24 h, no changes of cholinesterase activity in the rabbit following blood-transfusion were observed with an exception of erythrocyte acetylcholinesterase. 4. When erythrocytes were incubated with soman for 0.5 h, a significant decrease in cholinesterase activity in the erythrocytes, plasma, diaphragm and liver following blood-transfusion was found. These data show that soman is able to release from erythrocytes and inhibit cholinesterase activities not only in vitro but also in vivo although the significant inhibition of cholinesterase activities by soman was only observed in the peripheral compartment.

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