Screening the methanol extracts of some Iranian plants for acetylcholinesterase inhibitory activity
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Auteurs : A. Gholamhoseinian ; M. N. Moradi ; F. Sharifi-FarSource :
- Research in Pharmaceutical Sciences [ 1735-5362 ] ; 2009.
Abstract
Acetylcholinesterase (AChE) is the main enzyme for the breakdown of acetylcholine. Nowadays, usage of the inhibitors of this enzyme is one of the most important types of treatment of mild to moderate neurodegenerative diseases such as Alzheimer’s disease. Herbal medicines can be a new source of inhibitors of this enzyme. In this study we examined around 100 different plants to evaluate their inhibitory properties for AChE enzyme. Plants were scientifically identified and their extracts were prepared by methanol percolation. Acetylcholinesterase activity was measured using a colorimetric method in the presence or absence of the extracts. Eserine was used as a positive control. Methanol extracts of the
Url:
PubMed: 21589805
PubMed Central: 3093628
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Screening the methanol extracts of some Iranian plants for acetylcholinesterase inhibitory activity</title><author><name sortKey="Gholamhoseinian, A" sort="Gholamhoseinian, A" uniqKey="Gholamhoseinian A" first="A." last="Gholamhoseinian">A. Gholamhoseinian</name><affiliation><nlm:aff id="AF0001"><italic>Department of Biochemistry, Medical School and Kerman Physiology Research Center, Kerman University of Medical Sciences, Kerman, I.R.Iran</italic></nlm:aff></affiliation><affiliation><nlm:aff>NONE</nlm:aff></affiliation></author><author><name sortKey="Moradi, M N" sort="Moradi, M N" uniqKey="Moradi M" first="M. N." last="Moradi">M. N. Moradi</name><affiliation><nlm:aff id="AF0001"><italic>Department of Biochemistry, Medical School and Kerman Physiology Research Center, Kerman University of Medical Sciences, Kerman, I.R.Iran</italic></nlm:aff></affiliation></author><author><name sortKey="Sharifi Far, F" sort="Sharifi Far, F" uniqKey="Sharifi Far F" first="F." last="Sharifi-Far">F. Sharifi-Far</name><affiliation><nlm:aff id="AF0002"><italic>Department of Pharmacognosy, School of Pharmacy, Kerman university of Medical Sciences, Kerman, I.R.Iran</italic></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">21589805</idno><idno type="pmc">3093628</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3093628</idno><idno type="RBID">PMC:3093628</idno><date when="2009">2009</date><idno type="wicri:Area/Pmc/Corpus">001276</idno><idno type="wicri:Area/Pmc/Curation">001274</idno><idno type="wicri:Area/Pmc/Checkpoint">000F97</idno><idno type="wicri:Area/Ncbi/Merge">000D35</idno><idno type="wicri:Area/Ncbi/Curation">000D35</idno><idno type="wicri:Area/Ncbi/Checkpoint">000D35</idno><idno type="wicri:doubleKey">1735-5362:2009:Gholamhoseinian A:screening:the:methanol</idno><idno type="wicri:Area/Main/Merge">001D68</idno><idno type="wicri:Area/Main/Curation">001D22</idno><idno type="wicri:Area/Main/Exploration">001D22</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Screening the methanol extracts of some Iranian plants for acetylcholinesterase inhibitory activity</title><author><name sortKey="Gholamhoseinian, A" sort="Gholamhoseinian, A" uniqKey="Gholamhoseinian A" first="A." last="Gholamhoseinian">A. Gholamhoseinian</name><affiliation><nlm:aff id="AF0001"><italic>Department of Biochemistry, Medical School and Kerman Physiology Research Center, Kerman University of Medical Sciences, Kerman, I.R.Iran</italic></nlm:aff></affiliation><affiliation><nlm:aff>NONE</nlm:aff></affiliation></author><author><name sortKey="Moradi, M N" sort="Moradi, M N" uniqKey="Moradi M" first="M. N." last="Moradi">M. N. Moradi</name><affiliation><nlm:aff id="AF0001"><italic>Department of Biochemistry, Medical School and Kerman Physiology Research Center, Kerman University of Medical Sciences, Kerman, I.R.Iran</italic></nlm:aff></affiliation></author><author><name sortKey="Sharifi Far, F" sort="Sharifi Far, F" uniqKey="Sharifi Far F" first="F." last="Sharifi-Far">F. Sharifi-Far</name><affiliation><nlm:aff id="AF0002"><italic>Department of Pharmacognosy, School of Pharmacy, Kerman university of Medical Sciences, Kerman, I.R.Iran</italic></nlm:aff></affiliation></author></analytic><series><title level="j">Research in Pharmaceutical Sciences</title><idno type="ISSN">1735-5362</idno><idno type="eISSN">1735-9414</idno><imprint><date when="2009">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Acetylcholinesterase (AChE) is the main enzyme for the breakdown of acetylcholine. Nowadays, usage of the inhibitors of this enzyme is one of the most important types of treatment of mild to moderate neurodegenerative diseases such as Alzheimer’s disease. Herbal medicines can be a new source of inhibitors of this enzyme. In this study we examined around 100 different plants to evaluate their inhibitory properties for AChE enzyme. Plants were scientifically identified and their extracts were prepared by methanol percolation. Acetylcholinesterase activity was measured using a colorimetric method in the presence or absence of the extracts. Eserine was used as a positive control. Methanol extracts of the <italic>Levisticum officinale, Bergeris integrima</italic> and <italic>Rheum ribes</italic> showed more than 50% AChE inhibitory activity. The inhibition kinetics were studied in the presence of the most effective extracts. <italic>L. officinale</italic> and <italic>B. integrima</italic> inhibited AChE activity in a non-competitive manner, while <italic>R. ribes</italic> competitively inhibitied the enzyme as revealed by double-reciprocal Linweaver-Burk plot analysis. Under controlled condition, K<sub>m</sub> and V<sub>max</sub> values of the enzyme were found to be 9.4 mM and 0.238 mM/min, respectively. However, in the presence of <italic>L. officinale, B. integrima</italic>, and <italic>R. ribes</italic> extracts, V<sub>max</sub> values were 0.192, 0.074 and 0.238 mM/min, respectively. Due to the competitive inhibition of the enzyme by <italic>R. ribes</italic> extract, the K<sub>m</sub> value of 21.2 mM was obtained. The concentration required for 50% enzyme inhibition (IC50 value) was 0.5, 0.9, and 0.95 mg/ml for the <italic>L. officinale, B. integrima</italic> and <italic>R. ribes</italic> extracts, respectively. 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sortKey="Michel, Mc" uniqKey="Michel M">MC Michel</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list></list><tree><noCountry><name sortKey="Gholamhoseinian, A" sort="Gholamhoseinian, A" uniqKey="Gholamhoseinian A" first="A." last="Gholamhoseinian">A. Gholamhoseinian</name><name sortKey="Moradi, M N" sort="Moradi, M N" uniqKey="Moradi M" first="M. N." last="Moradi">M. N. Moradi</name><name sortKey="Sharifi Far, F" sort="Sharifi Far, F" uniqKey="Sharifi Far F" first="F." last="Sharifi-Far">F. Sharifi-Far</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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