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

GÜLÇİN İ., Scozzafava A., SUPURAN C. T., Akincioglu H., Koksal Z., Turkan F., ...Daha Fazla

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.31, sa.6, ss.1095-1101, 2016 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 31 Sayı: 6
  • Basım Tarihi: 2016
  • Doi Numarası: 10.3109/14756366.2015.1094470
  • Dergi Adı: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.1095-1101
  • Anahtar Kelimeler: Acetylcholinesterase, butyrylcholinesterase, caffeic acid phenethyl ester, carbonic anhydrase, glutathione S-transferase, lactoperoxidase, TROUT ONCORHYNCHUS-MYKISS, STRUCTURE-ACTIVITY INSIGHT, CHIONANTHUS-VIRGINICUS L., ANTIOXIDANT ACTIVITY, VITRO ANTIOXIDANT, NITRIC-OXIDE, THERAPEUTIC APPLICATIONS, BOVINE LACTOPEROXIDASE, SELECTIVE INHIBITORS, SULFONAMIDE DERIVATIVES
  • Atatürk Üniversitesi Adresli: Evet

Özet

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.