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

Abstract

Health Services Vocational School, Igdır University, Igdır, Turkey AbstractCaffeic 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.

Synthesis of N-alkyl (aril)-tetra pyrimidine thiones and investigation of their human carbonic anhydrase I and II inhibitory effects

“…Cytosolic hCA I is expressed in the body and can be found in high concentrations in the blood and gastrointestinal tract 89 . The slow cytosolic isoform hCA I was effectively inhibited by newly synthesised N-alkyl (aril)-tetra pyrimidine thiones (1-5) with K i values ranging of 218.5 ± 23.9-312.6 ± 61.1 p.m. (Table 1).…”

Rosmarinic acid inhibits some metabolic enzymes including glutathioneS-transferase, lactoperoxidase, acetylcholinesterase, butyrylcholinesterase and carbonic anhydrase isoenzymes

“…Both CA isozymes (CA IX and XII) were prepared in recombinant form as reported earlier 17 . The inhibitory effect of rosmarinic acid on AChE/BChE activities were measured according to spectrophotometric method of Ellman et al 18 as described previously 12 . Acetylthiocholine iodide (AChI) or butyrylthiocholine iodide (BChI) was used as substrates of the reaction.…”

“…AChE is known to be abundant in the muscle, brain and erythrocyte membrane, whereas BChE has a higher activity in liver, intestine, heart, kidney and lung. AChE and BChE share 65% amino acid sequence homology and have similar molecular forms and active sites despite being products of different genes on the human chromosomes 12 .…”

“…They are essential and found in all kingdoms of life. GSTs catalyse the conjugation of GSH by a sulfhydryl group (-SH) to electrophilic centres on a wide variety of substrates in order to make the compounds more water soluble 12 . For example, the detoxification of 1,2-epoxyethylbenzene can be given.…”

Synthesis and inhibitory properties of some carbamates on carbonic anhydrase and acetylcholine esterase

“…Subsequently, the reaction was initiated by the addition of 50 mL of AChI (10 mM). The hydrolysis of these AChI was monitored spectrophotometrically by the formation of yellow 5-thio-2-nitrobenzoate anion as the result of the reaction of DTNB with thiocholine, released by the enzymatic hydrolysis of AChI, at a wavelength of 412 nm 67,95 . For determination of the effect of carbamates (10-16) on AChE, different carbamates (10-16) concentrations were added into the reaction solution.…”