期刊
JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
卷 31, 期 6, 页码 1095-1101出版社
TAYLOR & FRANCIS LTD
DOI: 10.3109/14756366.2015.1094470
关键词
Acetylcholinesterase; butyrylcholinesterase; caffeic acid phenethyl ester; carbonic anhydrase; glutathione S-transferase; lactoperoxidase
资金
- EU project of the 7th FP, Metoxia
- EU project of the 7th FP, Dynano
- Research Chairs Program at King Saud University
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 K(i)s in the range between micromolar to picomolar. The best inhibitory effect was observed against AChE and BChE.
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