A study on inhibitory effect of ethanolic extract of the Pistacia lentiscus on acetylcholinesterase activity

Document Type: Research Paper

Authors

1 Associate Professor - Department of Biochemistry, School of Medicine, Shahed University, Tehran, Iran

2 Professor of Medical Physiology - Neurophysiology Research Center, Shahed University, Tehran, Iran

Abstract

Background and Objective: Changes of the enzyme acetylcholinesterase are involved in pathogenesis of different nervous disorders including Alzheimer’s disease. This research work was conducted to evaluate the inhibitory effect of Pistacia lentiscus ethanolic extract on acetylcholinesterase activity.
Materials and Methods: Activity of the enzyme acetylcholinesterase (AChE) was measured by Ellman method, using  scale. Then, Lineweaver Burk plot was used to calculate Km, Vmax and Ki. In all phases, the enzyme’s concentration was constant and its activity was measured at six different concentrations of acetylthiocholine (5, 10, 15, 20, 25 and 30 mM) at room temperature (25 °C) and based on the optical absorption at 412 nm wavelength. Experiments were conducted in the presence of various concentrations of physostigmine and also Pistacia lentiscus (2, 4, 6, 8, and 10 ug/ml).
Results: Ki of inhibitors were measured at different concentrations of acetylthiocholine (5, 10, 15, 20, 25 and 30 mM) and also in the presence of various concentrations of physostigmine     and Pistacia lentiscus (2, 4, 6, 8, and 10 ug/ml). IC50 of physostigmine and Pistacia lentiscus were determined as 2.9 and 6.5 μg/ml, respectively.
Conclusion: Since lower levels of Ki and IC50 indicate higher inhibitory effects on the enzyme, therefore, results show that physostigmine is a stronger inhibitor than Pistacia lentiscus
Background and Objective: Changes of the enzyme acetylcholinesterase are involved in pathogenesis of different nervous disorders including Alzheimer’s disease. This research work was conducted to evaluate the inhibitory effect of Pistacia lentiscus ethanolic extract on acetylcholinesterase activity.
Materials and Methods: Activity of the enzyme acetylcholinesterase (AChE) was measured by Ellman method, using  scale. Then, Lineweaver Burk plot was used to calculate Km, Vmax and Ki. In all phases, the enzyme’s concentration was constant and its activity was measured at six different concentrations of acetylthiocholine (5, 10, 15, 20, 25 and 30 mM) at room temperature (25 °C) and based on the optical absorption at 412 nm wavelength. Experiments were conducted in the presence of various concentrations of physostigmine and also Pistacia lentiscus (2, 4, 6, 8, and 10 ug/ml).
Results: Ki of inhibitors were measured at different concentrations of acetylthiocholine (5, 10, 15, 20, 25 and 30 mM) and also in the presence of various concentrations of physostigmine     and Pistacia lentiscus (2, 4, 6, 8, and 10 ug/ml). IC50 of physostigmine and Pistacia lentiscus were determined as 2.9 and 6.5 μg/ml, respectively.
Conclusion: Since lower levels of Ki and IC50 indicate higher inhibitory effects on the enzyme, therefore, results show that physostigmine is a stronger inhibitor than Pistacia lentiscus

Keywords


1. Lopes MA, Hototian SR, Bustamante SE, Azevedo D, Tatsch M, Bazzarella MC. Prevalence of cognitive and functional impairment in a community sample in Ribeirao Preto, Brazil. International Journal of Geriatric Psychiatry 2006; 22(8):770-6
2. Olivera Pueya FJ, Rodriguez Torrente M, Lorente Aznar T, Benabarre Ciria S, Pardo Gracia MA, Ceresuela Lopez A. Screening for factors relating to the development of mental disorders in the geriatric population. Atencion primaria 2006; 38(6):353-7
3. Association As. 2010 Alzheimer's disease facts and figures. Alzheimers Dementia 2010; 6(2): 158-94.
4. Hebert L, Scherr P, Bienias J, Bennett D, Evans D. Alzheimer disease in the US population: prevalence estimates using the 2000 census. Archives of Neurology 2003; 60(8): 1119-22.
5. Zhang HY: Sae causes, same cures, Biochemical and Biophysical Research Communication 2006; 351(3):578-81.
6. Parihar MS, Hemneni T. Alzheimer’s disease pathogenesis and therapeutic interventions. Journal of Clinical Neuroscience 2004; 11(5): 456-67.
7. Tabet N. Acetylcholinesterase inhibitors for Alzheimer’s disease: anti-inflammatories in acetylcholine clothing. Age Ageing 2006; 35 (4):336 - 8.
8. Glode TE. Disease modifying therapy for AD? Journal of Neurochemistry 2006; 99(3): 689-707.
9. Johannsen P. Medical treatment of Alzheimer’s disease. Ugeskrift for Laeger 2006; 168(40):3424-3429.
10. Oveysi Y. Pharmacology of neural system drugs. Medical publication of the year 1991; pp54-66.
11. Karimi E. The Iranian herb culture, Rangin Ghalam PUB, 2006, (3): Page 250.
12. The Sinai H, Law on Medical, Soroush Publications, 1998 p. 15-18.
13. Khorasani 13.qyly of H, seasonings Treasure, Cultural Foundation Publishing, 2005, page 354-60
14. Tabet N, Mantle D, Orrel M. Free Radicals as mediators of toxicity in Alzheimer’s disease: a review and hypothesis. Adverse Drug Reactions and Toxicological Reviews 2000; 19:127-52
15. Dehkordi Ghasemi, a plants pharmacopoeia in Iran, Hakim Research Journal 2003, 6 (3): 63-9.
16. Ellman GL, Courthey KD, Andres V, Featherstone AM. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochemical Pharmacology 1961;(7):88-95.
17. Snaz P, Vincent M.C, Diaz D, Repetto M, Repetto J. Red blood cell and total blood actylcholinesterase and plasma pseudo cholinesterase in human observed variances. Journal of Toxicology. Clinical Toxicology 1991;29(1):81-90