title: The impact of hydroquinone on acetylcholine esterase and certain human carbonic anhydrase isoenzymes (hCA I, II, IX, and XII).
abstract: 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 Zn(2+)-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 Ki 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 Kis in the range between micromolar (415.81 μM) and nanomolar (706.79 nM). The best inhibition was observed in cytosolic CA II.
authors.affiliation: a Dipartimento di Chimica Ugo Schiff , Università degli Studi di Firenze , Sesto Fiorentino (Firenze) , Italy .
authors.forename: Andrea
authors.initials: A
authors.lastname: Scozzafava
authors.affiliation: b Chemistry Department, Science Faculty , Ataturk University , Erzurum , Turkey .
authors.forename: Pınar
authors.initials: P
authors.lastname: Kalın
authors.affiliation: a Dipartimento di Chimica Ugo Schiff , Università degli Studi di Firenze , Sesto Fiorentino (Firenze) , Italy .|c Neurofarba Department, Section of Pharmaceutical and Nutriceutical Sciences , Università degli Studi di Firenze , Sesto Fiorentino (Florence) , Italy , and.
authors.forename: Claudiu T
authors.initials: CT
authors.lastname: Supuran
authors.affiliation: b Chemistry Department, Science Faculty , Ataturk University , Erzurum , Turkey .|d Department of Zoology, College of Science , King Saud University , Riyadh-Saudi Arabia.
authors.forename: İlhami
authors.initials: İ
authors.lastname: Gülçin
authors.affiliation: d Department of Zoology, College of Science , King Saud University , Riyadh-Saudi Arabia.
authors.forename: Saleh H
authors.initials: SH
authors.lastname: Alwasel
mesh_terms: D000110:Acetylcholinesterase / Q000378:metabolism*; D000951:Antigens, Neoplasm / Q000378:metabolism; D024401:Carbonic Anhydrase I / Q000037:antagonists & inhibitors / Q000378:metabolism; D024402:Carbonic Anhydrase II / Q000037:antagonists & inhibitors / Q000378:metabolism; D000071231:Carbonic Anhydrase IX; D002257:Carbonic Anhydrase Inhibitors / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D002256:Carbonic Anhydrases / Q000378:metabolism; D002800:Cholinesterase Inhibitors / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D004305:Dose-Response Relationship, Drug; D006801:Humans; D006873:Hydroquinones / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D007527:Isoenzymes / Q000037:antagonists & inhibitors / Q000378:metabolism; D015394:Molecular Structure; D013329:Structure-Activity Relationship
chemical_list: D000951:Antigens, Neoplasm; D002257:Carbonic Anhydrase Inhibitors; D002800:Cholinesterase Inhibitors; D006873:Hydroquinones; D007527:Isoenzymes; D000110:Acetylcholinesterase; D024401:Carbonic Anhydrase I; D024402:Carbonic Anhydrase II; C089226:CA9 protein, human; D000071231:Carbonic Anhydrase IX; D002256:Carbonic Anhydrases; C477378:carbonic anhydrase XII; C031927:hydroquinone
keywords: Acetylcholinesterase; carbonic anhydrases; enzyme inhibition; hydroquinone; isoenzymes