Erythrocyte acetylcholinesterase in psychiatric disorders and controls

Fritze, J.; Beckmann, H.

doi:10.1016/0006-3223(87)90052-7

Cited by 2 publications

(2 citation statements)

References 29 publications

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“…Acetylcholinesterase has been investigated for association with mental disorders and psychosis since long [36]. AChE is reported to be depressed in depression [37], and some other neurological disorders [38] and is known to interact with many drugs of abuse. It can hydrolyze heroin, a well known substance abuse drug [39], though morphine inhibits AChE [40].…”

Section: Discussionmentioning

confidence: 99%

Cannabis Constituents and Acetylcholinesterase Interaction: Molecular Docking, In Vitro Studies and Association with CNR1 rs806368 and ACHE rs17228602

et al. 2020

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The study documented here was aimed to find the molecular interactions of some of the cannabinoid constituents of cannabis with acetylcholinesterase (AChE). Molecular docking and LogP determination were performed to predict the AChE inhibitory effect and lipophilicity. AChE enzyme activity was measured in the blood of cannabis addicted human subjects. Further, genetic predisposition to cannabis addiction was investigated by association analysis of cannabinoid receptor 1 (CNR1) single nucleotide polymorphism (SNP) rs806368 and ACHE rs17228602 using restriction fragment length polymorphism (RFLP) method. All the understudied cannabis constituents showed promising binding affinities with AChE and are lipophilic in nature. The AChE activity was observed to be indifferent in cannabis addicted and non-addicted healthy controls. There was no significant association with CNR1 SNP rs806368 and ACHE rs17228602. The study concludes that in silico prediction for individual biomolecules of cannabis is different from in vivo physiological action in human subjects when all are present together. However, for a deeper mechanistic insight into these interactions and association, multi-population studies are suggested. Further studies to explore the inhibitory potential of different cannabis constituents for intended AChE inhibitor-based drug are warranted.

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Section: Discussionmentioning

confidence: 99%

Cannabis Constituents and Acetylcholinesterase Interaction: Molecular Docking, In Vitro Studies and Association with CNR1 rs806368 and ACHE rs17228602

et al. 2020

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“…AChE activity deficiency coexist (4,5,6), although in other psychiatric disorders this does not seem to be the case (7). Additionally, the AChE from blood cells, especially erythrocytes, has been chosen as an enzyme model since it has been reported to have many properties similar to those of the purified form obtained from brain tissues (8).…”

mentioning

confidence: 99%

Decrease in platelet, erythrocyte and lymphocyte acetylcholinesterase activities due to the presence of protease inhibitors in the storage buffer

et al. 1997

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The effect of the presence of protease inhibit0rs in the storage buffer on acetylcholinesterase (AChE) activity was studied in crude membrane preparations from sheep platelets before and after solubilization of the membranes with Triton X‐100. Although sensitive to the action of trypsin, the biological activity of AChE remained unchanged for as long as 6 days at 4°C in a protease‐inhibitor‐free medium. At 10‐5 M final concentration PMSF reduced AChE activity to 50% after 24 hours of storage. This reduction was abolished in mixtures in which PMSF was present together with 3 mM EGTA, 5 mM EDTA and 0.i mg/mL trypsin inhibitor. Nevertheless, under these conditions, storage periods longer than 24 hours still drastically reduced AChE activity. A mixture of EDTA, EGTA and trypsin inhibitor also produced a decrease in AChE activity after 24 hours. A more complex cocktail of inhibitors including several commonly used peptides decreased AChE activity only if PMSF or EDTA were present in the mixtures. Similar results were obtained with sheep erythrocytes or lymphocytes, and bovine erythrocytes.

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Erythrocyte acetylcholinesterase in psychiatric disorders and controls

Cited by 2 publications

References 29 publications

Cannabis Constituents and Acetylcholinesterase Interaction: Molecular Docking, In Vitro Studies and Association with CNR1 rs806368 and ACHE rs17228602

Cannabis Constituents and Acetylcholinesterase Interaction: Molecular Docking, In Vitro Studies and Association with CNR1 rs806368 and ACHE rs17228602

Decrease in platelet, erythrocyte and lymphocyte acetylcholinesterase activities due to the presence of protease inhibitors in the storage buffer

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