In Vitro and in Vivo Effects of Dantrolene on Carbonic Anhydrase Enzyme Activities

Gülçın, İlhami; Beydemır, Şükrü; Büyükokuroğlu, Mehmet Emin

doi:10.1248/bpb.27.613

Cited by 109 publications

(97 citation statements)

References 21 publications

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“…CA-II is the most widely distributed CA in the eye, kidney, central nervous system (CNS) and inner ear. There are also membrane-bound (CA IV, CA IX, CA XII, CA XIV), mitochondrial (CA V), secretory forms (CA VI) and several acatalytic forms (CA VIII, CA X, CA XI) 9,10 . Other CA isoforms are found in a variety of tissues where they participate in several important biologic processes [11][12][13][14] .…”

Section: Introductionmentioning

confidence: 99%

Carbonic anhydrase inhibitory properties of novel sulfonamide derivatives of aminoindanes and aminotetralins

Akbaba

Akıncıoğlu

Göçer

et al. 2013

Journal of Enzyme Inhibition and Medicinal Chemistry

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110

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Six sulfonamides derived from indanes and tetralines were synthesized. The human carbonic anhydrase isozymes hCA I and hCA II inhibition effects of the synthesized sulfonamides were determined. From these compounds, while N-(5,6-dimethoxy-2,3-dihydro-1H-inden-2-yl) methane sulfonamide showed the most potent inhibitory effect against hCA I (K i ¼ 46 AE 5.4 mM, r 2 ¼ 0.978), N-(1,2,3,4-tetrahydronaphthalene-2-yl)methanesulfonamide was found to have the best inhibitory effect against hCA II (K i ¼ 94 AE 7.6 mM, r 2 ¼ 0.982).

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Section: Introductionmentioning

confidence: 99%

Carbonic anhydrase inhibitory properties of novel sulfonamide derivatives of aminoindanes and aminotetralins

Akbaba

Akıncıoğlu

Göçer

et al. 2013

Journal of Enzyme Inhibition and Medicinal Chemistry

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110

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“…In a recent study, it was demonstrated that dimethoxy-bromophenol derivatives incorporating cyclopropane moieties have shown picomolar inhibition against cytosolic CA I, II and tumor-associated CA IX, and XII 9 . The relationship between anti-oxidant molecules and CA isoenzyme inhibition is well established [56][57][58] . It is well known that bromophenol derivatives had some biological activities including anti-oxidant and radical scavenging 55 , acetylcholine esterase inhibition properties 55,59 .…”

Section: Resultsmentioning

confidence: 99%

The effects of some bromophenols on human carbonic anhydrase isoenzymes

Taslimi

Gülçın

Öztaşkın

et al. 2015

Journal of Enzyme Inhibition and Medicinal Chemistry

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109

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Carbonic anhydrases (CAs, EC 4.2.1.1), which are involved in a variety of physiological and pathological processes, are ubiquitous metalloenzymes mainly catalyzing the reversible hydration of carbon dioxide (CO 2 ) to bicarbonate (HCO À 3 ) and proton (H + ). In this study, a dozen of bromophenol derivatives (1-12) were evaluated as metalloenzyme CA (EC 4.2.1.1) inhibitors against the human carbonic anhydrase isoenzymes I and II (hCA I and II). Cytosolic hCA I and II isoenzymes were effectively inhibited by bromophenol derivatives (1-12) with K is in the low nanomolar range of 1.85 ± 0.58 to 5.04 ± 1.46 nM against hCA I and in the range of 2.01 ± 0.52 to 2.94 ± 1.31 nM against hCA II, respectively.

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“…Carbonic anhydrase isoenzymes (hCA I and II) were purified by Sepharose-4B-L-tyrosine-sulfanilamide affinity chromatography in a single purification step 62 . Sepharose-4B-L-tyrosine-sulfanilamide was prepared according to a reported method 61 .…”

Section: Biochemical Studiesmentioning

confidence: 99%

“…Also, three catalytic forms are also known and called CA-related proteins (CARP) [54][55][56][57][58] . All isoenzymes contain a zinc ion (Zn 2+ ) located at the base of a 15 Å deep funnel-shaped active site cavity, that is, coordinated to the imidazole groups of three His residues and to the substrate H 2 O/hydroxide (ÀOH) that reacts with CO 2 [59][60][61][62][63] . Acetylcholinesterase (AChE, EC.…”

Section: Introductionmentioning

confidence: 99%

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

Yılmaz

Akbaba

Özgeriş

et al. 2016

Journal of Enzyme Inhibition and Medicinal Chemistry

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A series of carbamate derivatives were synthesized and their carbonic anhydrase I and II isoenzymes and acetylcholinesterase enzyme (AChE) inhibitory effects were investigated. All carbamates were synthesized from the corresponding carboxylic acids via the Curtius reactions of the acids with diphenyl phosphoryl azide followed by addition of benzyl alcohol. The carbamates were determined to be very good inhibitors against for AChE and hCA I, and II isoenzymes. AChE inhibition was determined in the range 0.209-0.291 nM. On the other hand, tacrine, which is used in the treatment of Alzheimer's disease possessed lower inhibition effect (K i : 0.398 nM). Also, hCA I and II isoenzymes were effectively inhibited by the carbamates, with inhibition constants (K i ) in the range of 4.49-5.61 nM for hCA I, and 4.94-7.66 nM for hCA II, respectively. Acetazolamide, which was clinically used carbonic anhydrase (CA) inhibitor demonstrated K i values of 281.33 nM for hCA I and 9.07 nM for hCA II. The results clearly showed that AChE and both CA isoenzymes were effectively inhibited by carbamates at the low nanomolar levels.

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In Vitro and in Vivo Effects of Dantrolene on Carbonic Anhydrase Enzyme Activities

Cited by 109 publications

References 21 publications

Carbonic anhydrase inhibitory properties of novel sulfonamide derivatives of aminoindanes and aminotetralins

Carbonic anhydrase inhibitory properties of novel sulfonamide derivatives of aminoindanes and aminotetralins

The effects of some bromophenols on human carbonic anhydrase isoenzymes

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

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