The effect of caffeic acid phenethyl ester (CAPE) on metabolic enzymes including acetylcholinesterase,butyrylcholinesterase, glutathione S-transferase,lactoperoxidase, and carbonic anhydrase isoenzymes I,II, IX,and XII |
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| Authors: | ?lhami Gülçin Andrea Scozzafava Claudiu T Supuran Hulya Ak?nc?o?lu Zeynep Koksal Fikret Turkan |
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| Institution: | 1. Department of Chemistry, Faculty of Science, Ataturk University, Erzurum, Turkey,;2. Department of Zoology, College of Science, King Saud University, Riyadh, Saudi Arabia, igulcin@atauni.edu.tr;4. Dipartimento Di Chimica Ugo Schiff, Università Degli Studi Di Firenze, Firenze, Italy,;5. Dipartimento Di Chimica Ugo Schiff, Università Degli Studi Di Firenze, Firenze, Italy,;6. Department of Neurofarba, Section of Pharmaceutical and Nutriceutical Sciences, Università Degli Studi Di Firenze, Florence, Italy,;7. Central Researching Laboratory, Agri Ibrahim Cecen University, Agri, Turkey, and;8. Department of Chemistry, Faculty of Science, Ataturk University, Erzurum, Turkey,;9. Health Services Vocational School, Igd?r University, Igd?r, Turkey |
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| Abstract: | Caffeic acid phenethyl ester (CAPE) is an active component of honeybee propolis extracts. Carbonic anhydrases (CAs, EC 4.2.1.1) are widespread and intensively studied metalloenzymes present in higher vertebrates including humans as many diverse isoforms. Acetylcholinesterase (AChE) is responsible for acetyl choline (ACh) hydrolysis and plays a fundamental role in nerve impulse transmission by terminating the action of the ACh neurotransmitter at cholinergic synapses and neuromuscular junctions. Butyrylcholinesterase (BChE) is another enzyme abundantly present in the liver and released into blood in a soluble form. Lactoperoxidase (LPO) is an enzyme involved in fighting pathogenic microorganisms whereas glutathione S-transferases (GSTs) are dimeric proteins present both in prokaryotic and eukaryotic organisms and involved in cellular detoxification mechanisms. In the present study, the inhibition effect of CAPE on human carbonic anhydrase (hCA) isoforms I, II, IX, and XII, AChE, BChE, LPO, and GST was evaluated. CAPE inhibited these enzymes with Kis in the range between micromolar to picomolar. The best inhibitory effect was observed against AChE and BChE. |
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| Keywords: | Acetylcholinesterase butyrylcholinesterase caffeic acid phenethyl ester carbonic anhydrase glutathione S-transferase lactoperoxidase |
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