Molecular evolution of the carbonic anhydrase genes: Calculation of divergence time for mouse carbonic anhydrase I and II

1986 ◽  
Vol 23 (4) ◽  
pp. 294-299 ◽  
Author(s):  
Peter J. Fraser ◽  
Peter J. Curtis
Keyword(s):  
Molecular Evolution ◽  
Carbonic Anhydrase ◽  
Divergence Time ◽  
Carbonic Anhydrase I

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.

scholarly journals New Histamine-Related Five-Membered N-Heterocycle Derivatives as Carbonic Anhydrase I Activators

Molecules ◽  
2022 ◽  
Vol 27 (2) ◽  
pp. 545
Author(s):  
Niccolò Chiaramonte ◽  
Alessio Gabellini ◽  
Andrea Angeli ◽  
Gianluca Bartolucci ◽  
Laura Braconi ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Imidazole Ring ◽  
Aliphatic Chain ◽  
Amino Group ◽  
Carbonic Anhydrase I ◽  
Terminal Amino ◽  
Human Carbonic Anhydrase ◽  
New Compounds ◽  
Related Compounds ◽  
Micromolar Range

A series of histamine (HST)-related compounds were synthesized and tested for their activating properties on five physiologically relevant human Carbonic Anhydrase (hCA) isoforms (I, II, Va, VII and XIII). The imidazole ring of HST was replaced with different 5-membered heterocycles and the length of the aliphatic chain was varied. For the most interesting compounds some modifications on the terminal amino group were also performed. The most sensitive isoform to activation was hCA I (KA values in the low micromolar range), but surprisingly none of the new compounds displayed activity on hCA II. Some derivatives (1, 3a and 22) displayed an interesting selectivity for activating hCA I over hCA II, Va, VII and XIII.

scholarly journals Multiple transgressions and slow evolution shape the phylogeographic pattern of the blind cave-dwelling shrimp Typhlocaris

PeerJ ◽  
2018 ◽  
Vol 6 ◽  
pp. e5268 ◽  
Author(s):  
Tamar Guy-Haim ◽  
Noa Simon-Blecher ◽  
Amos Frumkin ◽  
Israel Naaman ◽  
Yair Achituv
Keyword(s):  
Molecular Evolution ◽  
Mediterranean Sea ◽  
Divergence Time ◽  
Evolutionary Rates ◽  
Radiometric Dating ◽  
Small Range ◽  
Biogeographic Patterns ◽  
Blind Cave ◽  
The Mediterranean ◽  
Slow Evolution

Background Aquatic subterranean species often exhibit disjunct distributions, with high level of endemism and small range, shaped by vicariance, limited dispersal, and evolutionary rates. We studied the disjunct biogeographic patterns of an endangered blind cave shrimp, Typhlocaris, and identified the geological and evolutionary processes that have shaped its divergence pattern. Methods We collected Typlocaris specimens of three species (T. galilea, T. ayyaloni, and T. salentina), originating from subterranean groundwater caves by the Mediterranean Sea, and used three mitochondrial genes (12S, 16S, cytochrome oxygnese subunit 1 (COI)) and four nuclear genes (18S, 28S, internal transcribed spacer, Histon 3) to infer their phylogenetic relationships. Using the radiometric dating of a geological formation (Bira) as a calibration node, we estimated the divergence times of the Typhlocaris species and the molecular evolution rates. Results The multi-locus ML/Bayesian trees of the concatenated seven gene sequences showed that T. salentina (Italy) and T. ayyaloni (Israel) are sister species, both sister to T. galilea (Israel). The divergence time of T. ayyaloni and T. salentina from T. galilea was 7.0 Ma based on Bira calibration. The divergence time of T. ayyaloni from T. salentina was 5.7 (4.4–6.9) Ma according to COI, and 5.8 (3.5–7.2) Ma according to 16S. The computed interspecific evolutionary rates were 0.0077 substitutions/Myr for COI, and 0.0046 substitutions/Myr for 16S. Discussion Two consecutive vicariant events have shaped the phylogeographic patterns of Typhlocaris species. First, T. galilea was tectonically isolated from its siblings in the Mediterranean Sea by the arching uplift of the central mountain range of Israel ca. seven Ma. Secondly, T. ayyaloni and T. salentina were stranded and separated by a marine transgression ca. six Ma, occurring just before the Messinian Salinity Crisis. Our estimated molecular evolution rates were in one order of magnitude lower than the rates of closely related crustaceans, as well as of other stygobiont species. We suggest that this slow evolution reflects the ecological conditions prevailing in the highly isolated subterranean water bodies inhabited by Typhlocaris.

scholarly journals Synthesis of Novel Selenides Bearing Benzenesulfonamide Moieties as Carbonic Anhydrase I, II, IV, VII, and IX Inhibitors

2017 ◽  
Vol 8 (12) ◽  
pp. 1213-1217 ◽  
Author(s):  
Andrea Angeli ◽  
Damiano Tanini ◽  
Antonella Capperucci ◽  
Claudiu T. Supuran
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase I
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