Inhibition properties of some flavonoids on carbonic anhydrase I and II isoenzymes purified from human erythrocytes

2017 ◽  
Vol 31 (9) ◽  
pp. e21930 ◽  
Author(s):  
Zübeyir Huyut ◽  
Şükrü Beydemir ◽  
İlhami Gülçin
Keyword(s):  
Carbonic Anhydrase ◽  
Human Erythrocytes ◽  
Carbonic Anhydrase I

scholarly journals In vitro inhibition of purified human carbonic anhydrase I and II by novel fluorene derivatives

2014 ◽  
Vol 33 (2) ◽  
pp. 199 ◽  
Author(s):  
Hülya Demirhan ◽  
Mustafa Arslan ◽  
Mustafa Oguzhan Kaya ◽  
Yeşim Kaya ◽  
Nahit Gençer ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Human Erythrocytes ◽  
Affinity Column ◽  
Inhibitory Effects ◽  
Thiourea Derivatives ◽  
Carbonic Anhydrase I ◽  
In Vitro Inhibition ◽  
Human Carbonic Anhydrase ◽  
Sepharose 4B

<p>In this study, 9-benzylidene-9<em>H</em>-fluorene-substituted urea (<strong>5a–p</strong>) and thiourea derivatives <strong>(5q–v)</strong> were synthesized and their inhibitory effects on the activity of human carbonic anhydrase (hCA) I and II were evaluated. hCA I and II were purified from human erythrocytes using a Sepharose 4B-L-tyrosine-sulphanilamide affinity column. All the synthesized compounds inhibited the activity of the hCA I and II isoenzymes. Among the synthesized compounds, <strong>5f</strong><strong> </strong>was found to be the most active (IC<sub>50</sub> = 21.4 μM) for inhibition of hCA I and <strong>5s </strong>was the most active (IC<sub>50</sub> = 25.3 μM) for inhibition of<strong> </strong>hCA II.</p><p><strong><br /></strong></p>

scholarly journals Synthesis and Human Carbonic Anhydrase I, II, IX, and XII Inhibition Studies of Sulphonamides Incorporating Mono-, Bi- and Tricyclic Imide Moieties

2021 ◽  
Vol 14 (7) ◽  
pp. 693
Author(s):  
Kalyan K. Sethi ◽  
KM Abha Mishra ◽  
Saurabh M. Verma ◽  
Daniela Vullo ◽  
Fabrizio Carta ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Carbonic Anhydrase ◽  
Docking Studies ◽  
Carbonic Anhydrases ◽  
Molecular Docking Studies ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase ◽  
Inhibition Studies

New derivatives were synthesised by reaction of amino-containing aromatic sulphonamides with mono-, bi-, and tricyclic anhydrides. These sulphonamides were investigated as human carbonic anhydrases (hCAs, EC 4.2.1.1) I, II, IX, and XII inhibitors. hCA I was inhibited with inhibition constants (Kis) ranging from 49 to >10,000 nM. The physiologically dominant hCA II was significantly inhibited by most of the sulphonamide with the Kis ranging between 2.4 and 4515 nM. hCA IX and hCA XII were inhibited by these sulphonamides in the range of 9.7 to 7766 nM and 14 to 316 nM, respectively. The structure–activity relationships (SAR) are rationalised with the help of molecular docking studies.

Crystal analysis of aromatic sulfonamide binding to native and (Zn)2 adduct of human carbonic anhydrase I Michigan 1

2002 ◽  
Vol 339 ◽  
pp. 135-144 ◽  
Author(s):  
Marta Ferraroni ◽  
Fabrizio Briganti ◽  
W.Richard Chegwidden ◽  
Claudiu T. Supuran ◽  
Andrea Scozzafava
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase ◽  
Aromatic Sulfonamide

scholarly journals Synthesis and carbonic anhydrase I, II, IX and XII inhibitory activity of sulfamates incorporating piperazinyl-ureido moieties

2015 ◽  
Vol 23 (17) ◽  
pp. 5619-5625 ◽  
Author(s):  
Cenzo Congiu ◽  
Valentina Onnis ◽  
Alessandro Deplano ◽  
Gianfranco Balboni ◽  
Mariangela Ceruso ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Inhibitory Activity ◽  
Carbonic Anhydrase I

Carbonic anhydrase I and II activation with mono- and dihalogenated histamine derivatives

2011 ◽  
Vol 21 (16) ◽  
pp. 4884-4887 ◽  
Author(s):  
Mohamed-Chiheb Saada ◽  
Daniela Vullo ◽  
Jean-Louis Montero ◽  
Andrea Scozzafava ◽  
Jean-Yves Winum ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase I

A simple enzyme-linked immunoassay of human carbonic anhydrase I for the study of developing erythroid cells

1990 ◽  
Vol 191 (3) ◽  
pp. 169-174 ◽  
Author(s):  
Takahito Kondo ◽  
Kazuhiro Murakami ◽  
Hiroshi Isobe ◽  
Naoyuki Taniguchi ◽  
Yoshikazu Kawakami
Keyword(s):  
Carbonic Anhydrase ◽  
Erythroid Cells ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase

scholarly journals Carbonic Anhydrase I as a New Plasma Biomarker for Prostate Cancer

ISRN Oncology ◽  
2012 ◽  
Vol 2012 ◽  
pp. 1-10 ◽  
Author(s):  
Michiko Takakura ◽  
Akira Yokomizo ◽  
Yoshinori Tanaka ◽  
Michimoto Kobayashi ◽  
Giman Jung ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Carbonic Anhydrase ◽  
Cancer Patients ◽  
Plasma Proteins ◽  
Specific Antigen ◽  
Healthy Controls ◽  
Gray Zone ◽  
Plasma Biomarker ◽  
Carbonic Anhydrase I ◽  
Discrimination Rate

Serum prostate-specific antigen (PSA) levels ranging from 4 to 10 ng/mL is considered a diagnostic gray zone for detecting prostate cancer because biopsies reveal no evidence of cancer in 75% of these subjects. Our goal was to discover a new highly specific biomarker for prostate cancer by analyzing plasma proteins using a proteomic technique. Enriched plasma proteins from 25 prostate cancer patients and 15 healthy controls were analyzed using a label-free quantitative shotgun proteomics platform called 2DICAL (2-dimensional image converted analysis of liquid chromatography and mass spectrometry) and candidate biomarkers were searched. Among the 40,678 identified mass spectrum (MS) peaks, 117 peaks significantly differed between prostate cancer patients and healthy controls. Ten peaks matched carbonic anhydrase I (CAI) by tandem MS. Independent immunological assays revealed that plasma CAI levels in 54 prostate cancer patients were significantly higher than those in 60 healthy controls (, Mann-Whitney test). In the PSA gray-zone group, the discrimination rate of prostate cancer patients increased by considering plasma CAI levels. CAI can potentially serve as a valuable plasma biomarker and the combination of PSA and CAI may have great advantages for diagnosing prostate cancer in patients with gray-zone PSA level.

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