The impact of hydroquinone on acetylcholine esterase and certain human carbonic anhydrase isoenzymes (hCA I, II, IX, and XII)

Scozzafava A., KALIN P., SUPURAN C. T., GÜLÇİN İ., ALWASEL S. H.

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.30, sa.6, ss.941-946, 2015 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 30 Sayı: 6
  • Basım Tarihi: 2015
  • Doi Numarası: 10.3109/14756366.2014.999236
  • Dergi Adı: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.941-946
  • Anahtar Kelimeler: Acetylcholinesterase, carbonic anhydrases, enzyme inhibition, hydroquinone, isoenzymes, TROUT ONCORHYNCHUS-MYKISS, ANTIOXIDANT ACTIVITY, VITRO ANTIOXIDANT, SULFONAMIDE DERIVATIVES, ANTIRADICAL ACTIVITIES, INHIBITORY PROPERTIES, SELECTIVE INHIBITORS, ENZYME-ACTIVITY, CAFFEIC ACID, ISOZYMES I
  • Atatürk Üniversitesi Adresli: Evet

Özet

Carbonic anhydrases (CAs) are widespread and the most studied members of a great family of metalloenzymes in higher vertebrates including humans. CAs were investigated for their inhibition of all of the catalytically active mammalian isozymes of the Zn2+-containing CA, (CA, EC 4.2.1.1). On the other hand, acetylcholinesterase (AChE. EC 3.1.1.7), a serine protease, is responsible for ACh hydrolysis and plays a fundamental role in impulse transmission by terminating the action of the neurotransmitter ACh at the cholinergic synapses and neuromuscular junction. In the present study, the inhibition effect of the hydroquinone (benzene-1,4-diol) on AChE activity was evaluated and effectively inhibited AChE with K-i of 1.22 nM. Also, hydroquinone strongly inhibited some human cytosolic CA isoenzymes (hCA I and II) and tumour-associated transmembrane isoforms (hCA IX, and XII), with K(i)s in the range between micromolar (415.81 mu M) and nanomolar (706.79 nM). The best inhibition was observed in cytosolic CA II.