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Journal articles on the topic 'Human carbonic anhydrase'

Author: Grafiati

Published: 6 September 2023

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1

Sly, William S., and Peiyi Y. Hu. "Human Carbonic Anhydrases and Carbonic Anhydrase Deficiencies." Annual Review of Biochemistry 64, no. 1 (June 1995): 375–401. http://dx.doi.org/10.1146/annurev.bi.64.070195.002111.

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2

Tomar, Jyoti Singh, and Jun Shen. "Characterization of Carbonic Anhydrase In Vivo Using Magnetic Resonance Spectroscopy." International Journal of Molecular Sciences 21, no. 7 (April 1, 2020): 2442. http://dx.doi.org/10.3390/ijms21072442.

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Carbonic anhydrase is a ubiquitous metalloenzyme that catalyzes the reversible interconversion of CO2/HCO3−. Equilibrium of these species is maintained by the action of carbonic anhydrase. Recent advances in magnetic resonance spectroscopy have allowed, for the first time, in vivo characterization of carbonic anhydrase in the human brain. In this article, we review the theories and techniques of in vivo 13C magnetization (saturation) transfer magnetic resonance spectroscopy as they are applied to measuring the rate of exchange between CO2 and HCO3− catalyzed by carbonic anhydrase. Inhibitors of carbonic anhydrase have a wide range of therapeutic applications. Role of carbonic anhydrases and their inhibitors in many diseases are also reviewed to illustrate future applications of in vivo carbonic anhydrase assessment by magnetic resonance spectroscopy.

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3

Wani, Tanvi V., and Mrunmayee P. Toraskar. "QSAR STUDIES ON HUMAN CARBONIC ANHYDRASE II INHIBITORS." INDIAN DRUGS 58, no. 11 (December 28, 2021): 18–28. http://dx.doi.org/10.53879/id.58.11.12350.

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Carbonic anhydrase II is one of the forms of human α carbonic anhydrases which are ubiquitous metalloenzymes that catalyze inter-conversion of carbon dioxide and water to bicarbonate and proton, overexpression of which leads to disorders such as glaucoma. 2D and 3D Quantitative Structure Activity Relationship studies were carried out on previously synthesized series of sulfanilamide derivatives by VLife MDS software using stepwise variable, multi-linear regression and k-nearest neighbor molecular field analysis methods. 2D-QSAR model depicts contribution of halogens (such as chlorine and fluorine), methylene and oxygen atoms to inhibition of human carbonic anhydrases II activity. Using k-nearest neighbor molecular field analysis method two 3D-QSAR models (model A and B) were generated from which model A was found to be the best validated model with q2 (0.9494), pred_r2 (0.7367) and q2 _ se (0.2037). It displayed the fact that the inhibitory action of sulfanilamide derivatives against human carbonic anhydrases II is influenced by hydrophobicity and electro positivity.

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4

Dodgson, S. J., R. E. Forster, W. S. Sly, and R. E. Tashian. "Carbonic anhydrase activity of intact carbonic anhydrase II-deficient human erythrocytes." Journal of Applied Physiology 65, no. 4 (October 1, 1988): 1472–80. http://dx.doi.org/10.1152/jappl.1988.65.4.1472.

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Intact erythrocytes from subjects with deficiency of blood carbonic anhydrase (CA) II and from normal subjects were assayed for enzyme activity by use of an 18O exchange technique in a solution containing 25 mM (CO2 + NaHCO3) plus 125 mM NaCl. At 25 degrees C and pH 7.4, the catalyzed reaction velocity was 0.32 +/- 0.04 M/s for the CA II-deficient and 1.60 +/- 0.12 M/s for the normal cells, a ratio of 1:5. Under the same conditions at 37 degrees C the relative difference between the CA II-deficient and normal cells was much less: the velocity for the CA II-deficient cells was 0.84 +/- 0.07 M/s and for the normal cells 1.60 +/- 0.32 M/s, a ratio of 1:1.9. Results were comparable for the hemolysates with the NaHCO3 reduced to 85 mM (the corresponding intracellular concentration): at 25 degrees C CA II-deficient cells had a velocity of 0.36 +/- 0.01 M/s compared with 1.12 +/- 0.04 M/s for the normal cells, a ratio of 1:3.1. At 37 degrees C again the relative difference between hemolysates from CA II normal and deficient cells was much less: the CA II-deficient cells had a reaction velocity of 1.17 +/- 0.22 M/s vs. 2.60 +/- 0.36 M/s for the normal cells, a ratio of 1:2.2. The greater fractional reduction of enzyme velocity of CA II-deficient cells at 25 degrees C compared with 37 degrees C appears to be explained by a greater chloride inhibition of the presumed CA I at the lower temperature.(ABSTRACT TRUNCATED AT 250 WORDS)

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5

Peters, T., F. Papadopoulos, H. P. Kubis, and G. Gros. "Properties of a carbonic anhydrase inhibitor protein in flounder serum." Journal of Experimental Biology 203, no. 19 (October 1, 2000): 3003–9. http://dx.doi.org/10.1242/jeb.203.19.3003.

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The blood serum of the European flounder Platichthys flesus strongly inhibits soluble erythrocytic carbonic anhydrase from the same species. The inhibition is of the uncompetitive type. Hence, the mechanism of the carbonic anhydrase inhibition is different from that of all other known carbonic anhydrase inhibitors. The serum showed no inhibitory effect on carbonic anhydrase from human and bovine red blood cells. By applying the (18)O exchange reaction, it could be demonstrated that the presence of the carbonic anhydrase inhibitor in the extracellular fluid has no effect on carbonic anhydrase in intact red blood cells. Thus, this carbonic anhydrase inhibitor seems to act only within the plasma space of the circulatory system. However, the carbonic anhydrase inhibitor does appear to reduce the bicarbonate permeability of flounder red cells to approximately one-quarter of normal levels as measured by the (18)O exchange reaction. The 28 kDa carbonic anhydrase inhibitor was isolated from the serum by gel filtration. The isolated inhibitor was detected in acrylamide gels as a single band representing a 7 kDa protein. The denaturing conditions used in electrophoresis presumably led to a dissociation of the native protein into subunits.

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6

Fujikawa-Adachi, Kiyomi, Isao Nishimori, Takahiro Taguchi, and Saburo Onishi. "Human Mitochondrial Carbonic Anhydrase VB." Journal of Biological Chemistry 274, no. 30 (July 23, 1999): 21228–33. http://dx.doi.org/10.1074/jbc.274.30.21228.

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7

Barlow, Jonathan H., Nicholas Lowe, Yvonne H. Edwards, and Peter H. W. Butterworth. "Human carbonic anhydrase I cDNA." Nucleic Acids Research 15, no. 5 (1987): 2386. http://dx.doi.org/10.1093/nar/15.5.2386.

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8

D'Ambrosio, Katia, Simone Carradori, Simona M. Monti, Martina Buonanno, Daniela Secci, Daniela Vullo, Claudiu T. Supuran, and Giuseppina De Simone. "Out of the active site binding pocket for carbonic anhydrase inhibitors." Chemical Communications 51, no. 2 (2015): 302–5. http://dx.doi.org/10.1039/c4cc07320g.

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9

Sinha, Reema, Himanshu Singh, Sandeep Kumar Bansal, Rahul Kaushik, and Krishan Kumar Verma. "IN-SILICO DOCKING STUDIES OF CARBONIC ANHYDRASE INHIBITORS IN THE MANAGEMENT OF NEUROPATHIC PAIN." Journal of Applied Pharmaceutical Sciences and Research 5, no. 4 (April 5, 2023): 17–27. http://dx.doi.org/10.31069/japsr.v5i4.03.

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Background: In the present study, the in-silico docking studies of carbonic anhydrase inhibitors with 4RUX i.e. The crystal Structure of Human carbonic Anhydrase II protein was performed in the management of neuropathic pain. Materials and Methods: The crystal structure of protein PDB ID: 4RUX was downloaded from the RCSB PDB database and the ligand molecules of carbonic anhydrase inhibitors were drawn from Marvin Sketch. Docking studies between ligand and protein to predict binding interactions by using AutoDock 4.2 and the receptor-ligand complex interaction viewed by using Biovia Drug Discovery studio. Result: Carbonic anhydrase inhibitors showed binding energy ranging between -5.41 to -8.63. Ganoderic acid A showed better binding energy -8.63 kcal/mol than the standard Acetazolamide -6.22 kcal/mol. Conclusion: The result clearly indicates that among carbonic anhydrase inhibitors, Ganoderic acid A and Morindone show better hydrogen bonding and binding affinity towards carbonic anhydrase II (PDB ID: 4RUX). Thus, conclude that among carbonic anhydrase inhibitors Ganoderic acid A (obtained from Ganoderma lucidium) and Morindone (both obtained from Morinda citrifolia (NONI)} provide the better pharmacological effect.

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10

Abbas Albaayit, Shaymaa Fadhel. "ENZYME INHIBITORY PROPERTIES OF ZERUMBONE." Pakistan Journal of Agricultural Sciences 58, no. 03 (June 1, 2021): 1207–9. http://dx.doi.org/10.21162/pakjas/21.9759.

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Zerumbone (ZER) is a well-known sesquiterpene composite can be set up in the rhizomes of Zingiber zerumbet (Smith), having anti-cancer, anti-inflammatory and anti-hyperglycemic effects. This study aimed to investigate the inhibitory potential of ZER against drug-target enzymes involved in human pathologies, namely, obesity (Pancreatic lipase) and idiopathic intracranial hypertension (carbonic anhydrase). Result: ZER inhibits pancreatic lipase and carbonic anhydrase at percentages of 52.5 and 71.3% with 184.1±5 and 69.3±0.43 μg/mL IC50 values, respectively. Consequently, ZER has an excellent inhibitory action against pancreatic lipase and carbonic anhydrase, making it interesting anti-obesity drug candidate and avert patho-physiological-related carbonic anhydrase

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11

Arslan, Oktay, and Ö. İrfan Küfrevioğlu. "Affinity to some inhibitors of human carbonic anhydrase‐i and bovine carbonic anhydrase." Journal of Environmental Science and Health . Part A: Environmental Science and Engineering and Toxicology 31, no. 8 (September 1996): 2017–22. http://dx.doi.org/10.1080/10934529609376471.

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12

Runtsch, Leander Simon, David Michael Barber, Peter Mayer, Michael Groll, Dirk Trauner, and Johannes Broichhagen. "Azobenzene-based inhibitors of human carbonic anhydrase II." Beilstein Journal of Organic Chemistry 11 (July 7, 2015): 1129–35. http://dx.doi.org/10.3762/bjoc.11.127.

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Aryl sulfonamides are a widely used drug class for the inhibition of carbonic anhydrases. In the context of our program of photochromic pharmacophores we were interested in the exploration of azobenzene-containing sulfonamides to block the catalytic activity of human carbonic anhydrase II (hCAII). Herein, we report the synthesis and in vitro evaluation of a small library of nine photochromic sulfonamides towards hCAII. All molecules are azobenzene-4-sulfonamides, which are substituted by different functional groups in the 4´-position and were characterized by X-ray crystallography. We aimed to investigate the influence of electron-donating or electron-withdrawing substituents on the inhibitory constant K i. With the aid of an hCAII crystal structure bound to one of the synthesized azobenzenes, we found that the electronic structure does not strongly affect inhibition. Taken together, all compounds are strong blockers of hCAII with K i = 25–65 nM that are potentially photochromic and thus combine studies from chemical synthesis, crystallography and enzyme kinetics.

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13

Dixit, Sarvesh Datta, and Shalini Singh. "in silico Modeling of Curcumin Based Sulfonamides Inhibitors of the Human trans-Membrane Carbonic Anhydrase Isozyme, hCA IX by CoMSIA." Asian Journal of Organic & Medicinal Chemistry 6, no. 4 (December 31, 2021): 306–9. http://dx.doi.org/10.14233/ajomc.2021.ajomc-p354.

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Carbonic anhydrases, hCAs IX and XII are applied as the markers of progression of the disease in many oxygen deficient tumours and their specially manoeuvred inhibition is directly related to containing the growth of both primary tumours and tumour growth of secondary nature. Ligand-based quantitative structure-activity relationship (QSAR) studies were carried out on curcumin related, sulphonamide derivatives as inhibitors of human trans-membrane carbonic anhydrase isozyme, hCA IX by comparative molecular field similarity analysis (CoMSIA) implemented through the SYBYL package. The capacity of the model to predict coveted compound was evaluated using test set of three compounds. The best model created was found to be of choice as it showed a r2 value of 0.811 and a cross validated coefficient q2 value of 0.617 in tripos CoMSIA hydrophobic region. Results of the present study indicated that hydrophobic region factors play an important role in carbonic anhydrase hCA IX inhibition for compounds.

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14

Amiss, J. C., S. J. Gurman, and W. R. Chegwidden. "EXAFS Studies of Human Carbonic Anhydrase." Le Journal de Physique IV 7, no. C2 (April 1997): C2–617—C2–618. http://dx.doi.org/10.1051/jp4/1997115.

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15

Takacova, Martina, Monika Barathova, Miriam Zatovicova, Tereza Golias, Ivana Kajanova, Lenka Jelenska, Olga Sedlakova, Eliska Svastova, Juraj Kopacek, and Silvia Pastorekova. "Carbonic Anhydrase IX—Mouse versus Human." International Journal of Molecular Sciences 21, no. 1 (December 30, 2019): 246. http://dx.doi.org/10.3390/ijms21010246.

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In contrast to human carbonic anhydrase IX (hCA IX) that has been extensively studied with respect to its molecular and functional properties as well as regulation and expression, the mouse ortholog has been investigated primarily in relation to tissue distribution and characterization of CA IX-deficient mice. Thus, no data describing transcriptional regulation and functional properties of the mouse CA IX (mCA IX) have been published so far, despite its evident potential as a biomarker/target in pre-clinical animal models of tumor hypoxia. Here, we investigated for the first time, the transcriptional regulation of the Car9 gene with a detailed description of its promoter. Moreover, we performed a functional analysis of the mCA IX protein focused on pH regulation, cell–cell adhesion, and migration. Finally, we revealed an absence of a soluble extracellular form of mCA IX and provided the first experimental evidence of mCA IX presence in exosomes. In conclusion, though the protein characteristics of hCA IX and mCA IX are highly similar, and the transcription of both genes is predominantly governed by hypoxia, some attributes of transcriptional regulation are specific for either human or mouse and as such, could result in different tissue expression and data interpretation.

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16

Bhakta, Abhijit, Maitreyi Bandyopadhyay, Sayantan Dasgupta, Santanu Sen, Arun Kumar, and Utpal Kumar Biswas. "Effect of NaHS on carbonic anhydrase activity of human erythrocyte." Asian Journal of Medical Sciences 7, no. 3 (January 6, 2016): 23–27. http://dx.doi.org/10.3126/ajms.v7i3.14047.

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Background: In contrast to its role as poison, hydrogen sulfide (H2S) is recently considered as a gaso-transmitter which mediates important physiologic functions in humans. Evidence is accumulating to demonstrate that inhibitors of H2S production or therapeutic H2S donor compounds exert significant effects in various experimental models. Carbonic anhydrases (CA) are a group of zinc-containing metalloenzymes that catalyse the reversible hydration of carbon dioxide. CAs activity in erythrocytes (CAI and CAII) has recently been observed to be associated with various pathological conditions especially in diabetes mellitus, hypertension and lipid disorders. Alteration of this enzyme activity has been reported by the effect of advanced glycation end products methylglyoxal and reduced glutathione. Aims and Objectives: As H2S, being a mediator of many physiological functions and synthesized in vivo, may affect functions of many intracellular proteins like carbonic anhydrase, the objective of this study is to find out if there is any change in the carbonic anhydrase activity under the effect of H2S- donor NaHS in dose dependant manner using RBC model in vitro.Materials and Methods: Blood sample was collected from forty (40) numbers of healthy volunteers of 18-40 years of in heparin containing vials and packed cells were prepared immediately by centrifugation The packed erythrocytes were washed three times with normal saline and diluted (1:10) with the normal saline. One ml each of diluted packed cells was taken in eight test tubes. Serial dilutions of NaHS (1to 250 µMol/L) was added to all the test tubes except for the first test tube where only normal saline was added and incubated at room temperature for one hour. Haemolysates was prepared from the erythrocytes with equal volume of distilled water in each tube and the CA activity was determined in the haemolysates using standardized method.Results: There is significant increase of CA activity in dose dependent manner under the effect of NaHS and also compared to the activity of hemolysate prepared without NaHS. Conclusions:Our study for the first time demonstrated that the Carbonic Anhydrase activity of erythrocytes is significantly increases by the effect of NaHS and this study reveals some important biological role of H2S and carbonic anhydrase.Asian Journal of Medical Sciences Vol. 7(3) 2016 23-27

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17

Sasso, Emanuele, Monica Vitale, Francesca Monteleone, Francesca Ludovica Boffo, Margherita Santoriello, Daniela Sarnataro, Corrado Garbi, et al. "Binding of Carbonic Anhydrase IX to 45S rDNA Genes Is Prevented by Exportin-1 in Hypoxic Cells." BioMed Research International 2015 (2015): 1–10. http://dx.doi.org/10.1155/2015/674920.

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Carbonic anhydrase IX (CA IX) is a surrogate marker of hypoxia, involved in survival and pH regulation in hypoxic cells. We have recently characterized its interactome, describing a set of proteins interacting with CA IX, mainly in hypoxic cells, including several members of the nucleocytoplasmic shuttling apparatuses. Accordingly, we described complex subcellular localization for this enzyme in human cells, as well as the redistribution of a carbonic anhydrase IX pool to nucleoli during hypoxia. Starting from this evidence, we analyzed the possible contribution of carbonic anhydrase IX to transcription of the 45S rDNA genes, a process occurring in nucleoli. We highlighted the binding of carbonic anhydrase IX to nucleolar chromatin, which is regulated by oxygen levels. In fact, CA IX was found on 45S rDNA gene promoters in normoxic cells and less represented on these sites, in hypoxic cells and in cells subjected to acetazolamide-induced acidosis. Both conditions were associated with increased representation of carbonic anhydrase IX/exportin-1 complexes in nucleoli. 45S rRNA transcript levels were accordingly downrepresented. Inhibition of nuclear export by leptomycin B suggests a model in which exportin-1 acts as a decoy, in hypoxic cells, preventing carbonic anhydrase IX association with 45S rDNA gene promoters.

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18

Jakubowski, Maciej, Ewa Szahidewicz-Krupska, and Adrian Doroszko. "The Human Carbonic Anhydrase II in Platelets: An Underestimated Field of Its Activity." BioMed Research International 2018 (June 28, 2018): 1–10. http://dx.doi.org/10.1155/2018/4548353.

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Carbonic anhydrases constitute a group of enzymes that catalyse reversible hydration of carbon dioxide leading to the formation of bicarbonate and proton. The platelet carbonic anhydrase II (CAII) was described for the first time in the '80s of the last century. Nevertheless, its direct role in platelet physiology and pathology still remains poorly understood. The modulation of platelet CAII action as a therapeutic approach holds promise as a novel strategy to reduce the impact of cardiovascular diseases. This short review paper summarises the current knowledge regarding the role of human CAII in regulating platelet function. The potential future directions considering this enzyme as a potential drug target and important pathophysiological chain in platelet-related disorders are described.

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19

Zhu, X. L., and W. S. Sly. "Carbonic anhydrase IV from human lung. Purification, characterization, and comparison with membrane carbonic anhydrase from human kidney." Journal of Biological Chemistry 265, no. 15 (May 1990): 8795–801. http://dx.doi.org/10.1016/s0021-9258(19)38958-6.

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20

Huang, Xiaojing, Daniel Winter, Dominic J. Glover, Claudiu T. Supuran, and William A. Donald. "Effects of Phosphorylation on the Activity, Inhibition and Stability of Carbonic Anhydrases." International Journal of Molecular Sciences 24, no. 11 (May 25, 2023): 9275. http://dx.doi.org/10.3390/ijms24119275.

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Carbonic anhydrases (CAs) are a metalloenzyme family that have important roles in cellular processes including pH homeostasis and have been implicated in multiple pathological conditions. Small molecule inhibitors have been developed to target carbonic anhydrases, but the effects of post-translational modifications (PTMs) on the activity and inhibition profiles of these enzymes remain unclear. Here, we investigate the effects of phosphorylation, the most prevalent carbonic anhydrase PTM, on the activities and drug-binding affinities of human CAI and CAII, two heavily modified active isozymes. Using serine to glutamic acid (S > E) mutations to mimic the effect of phosphorylation, we demonstrate that phosphomimics at a single site can significantly increase or decrease the catalytic efficiencies of CAs, depending on both the position of the modification and the CA isoform. We also show that the S > E mutation at Ser50 of hCAII decreases the binding affinities of hCAII with well-characterized sulphonamide inhibitors including by over 800-fold for acetazolamide. Our findings suggest that CA phosphorylation may serve as a regulatory mechanism for enzymatic activity, and affect the binding affinity and specificity of small, drug and drug-like molecules. This work should motivate future studies examining the PTM-modification forms of CAs and their distributions, which should provide insights into CA physiopathological functions and facilitate the development of ‘modform-specific’ carbonic anhydrase inhibitors.

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21

Alvarez, Laetitia, Marjorie Fanjul, Nicholas Carter, and Etienne Hollande. "Carbonic Anhydrase II Associated with Plasma Membrane in a Human Pancreatic Duct Cell Line (CAPAN-1)." Journal of Histochemistry & Cytochemistry 49, no. 8 (August 2001): 1045–53. http://dx.doi.org/10.1177/002215540104900812.

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The subcellular distribution of carbonic anhydrase II, either throughout the cytosol or in the cytoplasm close to the apical plasma membrane or vesicular compartments, suggests that this enzyme may have different roles in the regulation of pH in intra- or extracellular compartments. To throw more light on the role of pancreatic carbonic anhydrase II, we examined its expression and subcellular distribution in Capan-1 cells. Immunocytochemical analysis by light, confocal, and electron microscopy, as well as immunoblotting of cell homogenates or purified plasma membranes, was performed. A carbonic anhydrase II of 29 kD associated by weak bonds to the inner leaflet of apical plasma membranes of polarized cells was detected. This enzyme was co-localized with markers of Golgi compartments. Moreover, the defect of its targeting to apical plasma membranes in cells treated with brefeldin A was indicative of its transport by the Golgi apparatus. We show here that a carbonic anhydrase II is associated with the inner leaflet of apical plasma membranes and with the cytosolic side of the endomembranes of human cancerous pancreatic duct cells (Capan-1). These observations point to a role for this enzyme in the regulation of intra- and extracellular pH. (J Histochem Cytochem 49:1045–1053, 2001)

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22

Riley, D. A., D. H. Lang, and J. Kenneth Chong. "Carbonic anhydrase activity of human peripheral nerves." Plastic and Reconstructive Surgery 76, no. 2 (August 1985): 338. http://dx.doi.org/10.1097/00006534-198508000-00088.

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23

Nishimori, I., and S. Onishi. "Carbonic anhydrase isozymes in the human pancreas." Digestive and Liver Disease 33, no. 1 (February 2001): 68–74. http://dx.doi.org/10.1016/s1590-8658(01)80138-9.

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24

Väänänen, H. K., M. Paloniemi, and J. Vuori. "Purification and localization of human carbonic anhydrase." Histochemistry 83, no. 3-4 (July 1985): 231–35. http://dx.doi.org/10.1007/bf00953989.

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25

Gupta, Preeti, and Shashank Deep. "Salt mediated unusual switching in the aggregation kinetic profile of human carbonic anhydrase." RSC Advances 5, no. 116 (2015): 95717–26. http://dx.doi.org/10.1039/c5ra17794d.

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26

Cavaliere, Franco, Simonetta Masieri, Stefania Nori, Sergio I. Magalini, and Salvatore R. Allegra. "Carbonic Anhydrase in Human Nasal Epithelium: Localization and Effect of the Inhibition by Dichlorphenamide." American Journal of Rhinology 10, no. 2 (March 1996): 113–18. http://dx.doi.org/10.2500/105065896781795003.

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Carbonic anhydrase has not hitherto been reported in nasal mucosa. In the first part of this study, five specimens of human nasal mucosa from the inferior turbinate were obtained from five healthy subjects and tested for this enzyme with a histochemical reaction. Carbonic anhydrase was identified in the columnar ciliated respiratory epithelium, but was absent in the adjacent stratified squamous epithelium. The effect of the inhibition of this enzyme on the pH values and Na, K, and Cl activity in nasal secretion was subsequently investigated. Fifteen patients, affected by endocranial hypertension and to whom dichlorphenamide—an inhibitor of carbonic anhydrase—was administered, were studied. The pH value, determined with a surface electrode before giving the drug and 30, 60, and 90 minutes later, significantly increased and reached a peak at 60 minutes. Na, K, and Cl concentration was assessed by indirect potentiometry in the nasal secretion and in the plasma both before giving dichlorphenamide and 60 minutes later. Although no change was observed in the plasma, in the nasal secretion Na and Cl concentration increased and K concentration decreased. As a consequence, the gradients of Na and K between plasma and secretion decreased, and that of Cl increased. We assume analogous changes in the rate of transport through the mucosa to occur. These results thus suggest that carbonic anhydrase is involved in control of the pH of nasal secretions as well as in the electrolyte transport through the epithelium.

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27

Ali, Majid, Murat Bozdag, Umar Farooq, Andrea Angeli, Fabrizio Carta, Paola Berto, Giuseppe Zanotti, and Claudiu T. Supuran. "Benzylaminoethyureido-Tailed Benzenesulfonamides: Design, Synthesis, Kinetic and X-ray Investigations on Human Carbonic Anhydrases." International Journal of Molecular Sciences 21, no. 7 (April 7, 2020): 2560. http://dx.doi.org/10.3390/ijms21072560.

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A drug design strategy of carbonic anhydrase inhibitors (CAIs) belonging to sulfonamides incorporating ureidoethylaminobenzyl tails is presented. A variety of substitution patterns on the ring and the tails, located on para- or meta- positions with respect to the sulfonamide warheads were incorporated in the new compounds. Inhibition of human carbonic anhydrases (hCA) isoforms I, II, IX and XII, involving various pathologies, was assessed with the new compounds. Selective inhibitory profile towards hCA II was observed, the most active compounds being low nM inhibitors (KIs of 2.8–9.2 nM, respectively). Extensive X-ray crystallographic analysis of several sulfonamides in an adduct with hCA I allowed an in-depth understanding of their binding mode and to lay a detailed structure-activity relationship.

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28

Boer, W. H., H. A. Koomans, and E. J. Dorhout Mees. "Acute effects of thiazides, with and without carbonic anhydrase inhibiting activity, on lithium and free water clearance in man." Clinical Science 76, no. 5 (May 1, 1989): 539–45. http://dx.doi.org/10.1042/cs0760539.

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1. The acute effects of chlorothiazide and bendroflumethiazide on renal Li+ clearance (CLi) were studied in Na+-restricted healthy humans during maximum water diuresis. 2. Chlorothiazide, which has marked carbonic anhydrase inhibiting activity, increased CLi by about 25%. The concomitant rise in uric acid clearance, maximum urine flow and bicarbonate excretion suggests that this drug suppressed proximal reabsorption through carbonic anhydrase inhibition, which would also explain the observed fall in glomerular filtration rate (increased glomerulotubular feedback activity). 3. Bendroflumethiazide, which lacks carbonic anhydrase inhibiting activity, did not affect CLi or any of the other above-mentioned variables. 4. It is concluded from the lack of an effect of bendroflumethiazide on CLi that Li+ is not reabsorbed in thiazide-sensitive segments of the human distal nephron. The rise in CLi after chlorothiazide is most likely due to suppressed Li+ reabsorption in the proximal tubules resulting from carbonic anhydrase inhibition. 5. The results of this study are compatible with the concept that CLi is an index of Na+ and water delivery from the proximal tubules in humans.

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29

Glöckner, Steffen, Andreas Heine, and Gerhard Klebe. "A Proof-of-Concept Fragment Screening of a Hit-Validated 96-Compounds Library against Human Carbonic Anhydrase II." Biomolecules 10, no. 4 (March 29, 2020): 518. http://dx.doi.org/10.3390/biom10040518.

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Fragment screening is a powerful tool to identify and characterize binding pockets in proteins. We herein present the results of a proof-of-concept screening campaign of a versatile 96-entry fragment library from our laboratory against the drug target and model protein human carbonic anhydrase II. The screening revealed a novel chemotype for carbonic anhydrase inhibition, as well as less common non-covalent interaction types and unexpected covalent linkages. Lastly, different runs of the PanDDA tool reveal a practical hint for its application.

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30

Nocentini, Alessio, Doretta Cuffaro, Lidia Ciccone, Elisabetta Orlandini, Susanna Nencetti, Elisa Nuti, Armando Rossello, and Claudiu T. Supuran. "Activation of carbonic anhydrases from human brain by amino alcohol oxime ethers: towards human carbonic anhydrase VII selective activators." Journal of Enzyme Inhibition and Medicinal Chemistry 36, no. 1 (October 25, 2020): 48–57. http://dx.doi.org/10.1080/14756366.2020.1838501.

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Hussein, Buthaina, Laurance M. S. Bourghli, Muhammed Alzweiri, Yusuf Al-Hiari, Mohammad Abu Sini, Soraya Alnabulsi, and Batool Al-Ghwairi. "Synthesis and Biological Evaluation of Carbonic Anhydrase III and IX Inhibitors using Gas Chromatography with Modified pH Sensitive Pellets." Jordan Journal of Pharmaceutical Sciences 16, no. 2 (July 24, 2023): 426–39. http://dx.doi.org/10.35516/jjps.v16i2.1470.

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Fifteen compounds were synthesized and tested as potential carbonic anhydrase III (CAIII) and carbonic anhydrase IX (CAIX) inhibitors, six of which are novel. Amides (a1-4), hydroxamic acids (b1-2), and imines (c1-9) derivatives were evaluated for their inhibitory activity against CAII and CAIX using gas chromatography with modified pH-sensitive pellets. The derivatives showed inhibition percentages between 12-56% for CAIII and 44-59% for CAIX, compared to 49% and 63% for captopril (the positive control), respectively. Imines showed the best inhibition of CAIII, while all derivatives showed comparable activity against CAIX. It is hypothesized that the nitrogen atom in imine, amide, or hydroxamic acid moieties in the vicinity of an ionizable group is in coordination with the zinc ion in the active site. Furthermore, the candidates were tested for their antimicrobial and antifungal activity. Generally, they showed low to zero activity against some gram-positive and negative bacteria. This supports the theory of their ability to bind to human carbonic anhydrase but not to bacterial one. These compounds could serve as useful scaffolds to develop more potent and selective carbonic anhydrase inhibitors as anti-obesity and anticancer candidates.

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Supuran, Claudiu T. "Emerging role of carbonic anhydrase inhibitors." Clinical Science 135, no. 10 (May 2021): 1233–49. http://dx.doi.org/10.1042/cs20210040.

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Abstract Inhibition of carbonic anhydrase (CA, EC 4.2.1.1) was clinically exploited for decades, as most modern diuretics were obtained considering as lead molecule acetazolamide, the prototypical CA inhibitor (CAI). The discovery and characterization of multiple human CA (hCA) isoforms, 15 of which being known today, led to new applications of their inhibitors. They include widely clinically used antiglaucoma, antiepileptic and antiobesity agents, antitumor drugs in clinical development, as well as drugs for the management of acute mountain sickness and idiopathic intracranial hypertension (IIH). Emerging roles of several CA isoforms in areas not generally connected to these enzymes were recently documented, such as in neuropathic pain, cerebral ischemia, rheumatoid arthritis, oxidative stress and Alzheimer’s disease. Proof-of-concept studies thus emerged by using isoform-selective inhibitors, which may lead to new clinical applications in such areas. Relevant preclinical models are available for these pathologies due to the availability of isoform-selective CAIs for all human isoforms, belonging to novel classes of compounds, such as coumarins, sulfocoumarins, dithiocarbamates, benzoxaboroles, apart the classical sulfonamide inhibitors. The inhibition of CAs from pathogenic bacteria, fungi, protozoans or nematodes started recently to be considered for obtaining anti-infectives with a new mechanism of action.

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Murakami, H., and W. S. Sly. "Purification and characterization of human salivary carbonic anhydrase." Journal of Biological Chemistry 262, no. 3 (January 1987): 1382–88. http://dx.doi.org/10.1016/s0021-9258(19)75797-4.

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Merz, Kenneth M. "Carbon dioxide binding to human carbonic anhydrase II." Journal of the American Chemical Society 113, no. 2 (January 1991): 406–11. http://dx.doi.org/10.1021/ja00002a004.

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Baird,, Teaster T., Abdul Waheed, Torayuki Okuyama, William S. Sly, and Carol A. Fierke. "Catalysis and Inhibition of Human Carbonic Anhydrase IV†." Biochemistry 36, no. 9 (March 1997): 2669–78. http://dx.doi.org/10.1021/bi962663s.

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Song, He, David L. Wilson, Erik R. Farquhar, Edwin A. Lewis, and Joseph P. Emerson. "Revisiting Zinc Coordination in Human Carbonic Anhydrase II." Inorganic Chemistry 51, no. 20 (October 3, 2012): 11098–105. http://dx.doi.org/10.1021/ic301645j.

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KUMPULAINEN, TIMO. "CARBONIC ANHYDRASE ISOENZYME C IN THE HUMAN RETINA." Acta Ophthalmologica 58, no. 3 (May 27, 2009): 397–405. http://dx.doi.org/10.1111/j.1755-3768.1980.tb05739.x.

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Roy, Bidhan C., Abir L. Banerjee, Michael Swanson, Xiao G. Jia, Manas K. Haldar, Sanku Mallik, and D. K. Srivastava. "Two-Prong Inhibitors for Human Carbonic Anhydrase II." Journal of the American Chemical Society 126, no. 41 (October 2004): 13206–7. http://dx.doi.org/10.1021/ja047271k.

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Roth, D. E., P. J. Venta, R. E. Tashian, and W. S. Sly. "Molecular basis of human carbonic anhydrase II deficiency." Proceedings of the National Academy of Sciences 89, no. 5 (March 1, 1992): 1804–8. http://dx.doi.org/10.1073/pnas.89.5.1804.

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Campbell, Andrew R., Dennis L. Andress, and Erik R. Swenson. "Identification and characterization of human neutrophil carbonic anhydrase." Journal of Leukocyte Biology 55, no. 3 (March 1994): 343–48. http://dx.doi.org/10.1002/jlb.55.3.343.

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Wingo, Thomas, Chingkuang Tu, Philip J. Laipis, and David N. Silverman. "The Catalytic Properties of Human Carbonic Anhydrase IX." Biochemical and Biophysical Research Communications 288, no. 3 (November 2001): 666–69. http://dx.doi.org/10.1006/bbrc.2001.5824.

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Abbas, Saghir, Sumera Zaib, Shafiq Ur Rahman, Saqib Ali, Shahid Hameed, Muhammad N. Tahir, Khurram S. Munawar, Farzana Shaheen, Syed M. Abbas, and Jamshed Iqbal. "Carbonic Anhydrase Inhibitory Potential of 1,2,4-triazole-3-thione Derivatives of Flurbiprofen, Ibuprofen and 4-tert-butylbenzoic Hydrazide: Design, Synthesis, Characterization, Biochemical Evaluation, Molecular Docking and Dynamic Simulation Studies." Medicinal Chemistry 15, no. 3 (April 12, 2019): 298–310. http://dx.doi.org/10.2174/1573406414666181012165156.

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Background:The over-expression of the carbonic anhydrases results in some specific carcinomas including pancreatic, gastric and brain tumor. Tumors are distinguished under hypoxic conditions and various investigations are being carried out to target the known hypoxic areas of the tumors to increase the sensitivity towards standard therapeutic treatment.Objective:Herein, we have designed and synthesized some biologically important esters, hydrazides, thiocarbamates, 1,2,4-triazole-3-thiones and Schiff bases. The purpose of the research was to evaluate the derivative against carbonic anhydrase and to assess the toxicity of the same compounds.Method:The structures of all the compounds were characterized by FT-IR, mass spectrometry, elemental analysis, 1H and 13C NMR spectroscopy. The synthetic derivatives were screened for their inhibitory potential against carbonic anhydrase II by in vitro assay. Double reciprocal plots for inhibition kinetics of the potent compounds were constructed and mode of inhibition was determined. Furthermore, to check the cytotoxicity, these derivatives were tested against human breast adenocarcinoma by MTT method.Results:X-ray diffraction analysis of the compounds 10, 14 and 15 showed that they did not have any π-π or C-H…&π interactions. The experimental results were validated by molecular docking and dynamic simulations of the potent compounds in the active pocket of enzyme. Important binding interactions of potent compounds with the key residues in the active site of the carbonic anhydrase enzyme were revealed. Drug likeness profile of the derivatives was evaluated to determine the physicochemical properties.Conclusion:The proposed synthetic approach provides a suitable platform for the generation of a new library of compounds which could potentially be employed in the future testing and optimization of inhibitor potencies.

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Draghici, Bogdan, Daniela Vullo, Suleyman Akocak, Ellen A. Walker, Claudiu T. Supuran, and Marc A. Ilies. "Ethylene bis-imidazoles are highly potent and selective activators for isozymes VA and VII of carbonic anhydrase, with a potential nootropic effect." Chem. Commun. 50, no. 45 (2014): 5980–83. http://dx.doi.org/10.1039/c4cc02346c.

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Zhao, Jingming, Anna Kajetanowicz, and Thomas R. Ward. "Carbonic anhydrase II as host protein for the creation of a biocompatible artificial metathesase." Organic & Biomolecular Chemistry 13, no. 20 (2015): 5652–55. http://dx.doi.org/10.1039/c5ob00428d.

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Cabaleiro-Lago, Celia, and Martin Lundqvist. "The Effect of Nanoparticles on the Structure and Enzymatic Activity of Human Carbonic Anhydrase I and II." Molecules 25, no. 19 (September 25, 2020): 4405. http://dx.doi.org/10.3390/molecules25194405.

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Human carbonic anhydrases (hCAs) belong to a well characterized group of metalloenzymes that catalyze the conversion of carbonic dioxide into bicarbonate. There are currently 15 known human isoforms of carbonic anhydrase with different functions and distribution in the body. This links to the relevance of hCA variants to several diseases such as glaucoma, epilepsy, mountain sickness, ulcers, osteoporosis, obesity and cancer. This review will focus on two of the human isoforms, hCA I and hCA II. Both are cytosolic enzymes with similar topology and 60% sequence homology but different catalytic efficiency and stability. Proteins in general adsorb on surfaces and this is also the case for hCA I and hCA II. The adsorption process can lead to alteration of the original function of the protein. However, if the function is preserved interesting biotechnological applications can be developed. This review will cover the knowledge about the interaction between hCAs and nanomaterials. We will highlight how the interaction may lead to conformational changes that render the enzyme inactive. Moreover, the importance of different factors on the final effect on hCAs, such as protein stability, protein hydrophobic or charged patches and chemistry of the nanoparticle surface will be discussed.

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Angeli, Andrea, Marta Ferraroni, Alessio Nocentini, Silvia Selleri, Paola Gratteri, Claudiu T. Supuran, and Fabrizio Carta. "Polypharmacology of epacadostat: a potent and selective inhibitor of the tumor associated carbonic anhydrases IX and XII." Chemical Communications 55, no. 40 (2019): 5720–23. http://dx.doi.org/10.1039/c8cc09568j.

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Shamsutdinov, N. Sh. "The role of myoepithelial cells in the morphogenesis of pleomorphic adenomas of the salivary glands and their identification." Kazan medical journal 72, no. 2 (February 15, 1991): 133–36. http://dx.doi.org/10.17816/kazmj106591.

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The morphogenesis of 15 pleomorphic adenomas was studied. Identification of myoepithelial cells was carried out by immunohistochemical method using polyclonal antibodies to myosin, human carbonic anhydrase III, monoclonal antibodies to proteins of intermediate filaments of cytokeratin polypeptides No. 8 (clone H 1), No. 17 (clone E 3) and No. 18 (clone C 12). Myoepithelial, epithelial and other cells are involved in the morphogenesis of the studied tumors. It is recommended to use antibodies to myosin, carbonic anhydrase III, keratins No. 8, 17, 18 in the diagnosis of pleomorphic adenomas of the salivary glands.

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Höhne, Claudia, Philipp A. Pickerodt, Roland C. Francis, Willehad Boemke, and Erik R. Swenson. "Pulmonary vasodilation by acetazolamide during hypoxia is unrelated to carbonic anhydrase inhibition." American Journal of Physiology-Lung Cellular and Molecular Physiology 292, no. 1 (January 2007): L178—L184. http://dx.doi.org/10.1152/ajplung.00205.2006.

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Acute hypoxic pulmonary vasoconstriction can be inhibited by high doses of the carbonic anhydrase inhibitor acetazolamide. This study aimed to determine whether acetazolamide is effective at dosing relevant to human use at high altitude and to investigate whether its efficacy against hypoxic pulmonary vasoconstriction is dependent on carbonic anhydrase inhibition by testing other potent heterocyclic sulfonamide carbonic anhydrase inhibitors. Six conscious dogs were studied in five protocols: 1) controls, 2) low-dose intravenous acetazolamide (2 mg·kg−1·h−1), 3) oral acetazolamide (5 mg/kg), 4) benzolamide, a membrane-impermeant inhibitor, and 5) ethoxzolamide, a membrane-permeant inhibitor. In all protocols, unanesthetized dogs breathed spontaneously during the first hour (normoxia) and then breathed 9–10% O2 for the next 2 h. Arterial oxygen tension ranged between 35 and 39 mmHg during hypoxia in all protocols. In controls, mean pulmonary artery pressure increased by 8 mmHg and pulmonary vascular resistance by 200 dyn·s·cm−5 ( P <0.05). With intravenous acetazolamide, mean pulmonary artery pressure and pulmonary vascular resistance remained unchanged during hypoxia. With oral acetazolamide, mean pulmonary artery pressure increased by 5 mmHg ( P < 0.05), but pulmonary vascular resistance did not change during hypoxia. With benzolamide and ethoxzolamide, mean pulmonary artery pressure increased by 6–7 mmHg and pulmonary vascular resistance by 150–200 dyn·s·cm−5 during hypoxia ( P < 0.05). Low-dose acetazolamide is effective against acute hypoxic pulmonary vasoconstriction in vivo. The lack of effect with two other potent carbonic anhydrase inhibitors suggests that carbonic anhydrase is not involved in the mediation of hypoxic pulmonary vasoconstriction and that acetazolamide acts on a different receptor or channel.

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Alterio, V., M. Tanc, J. Ivanova, R. Zalubovskis, I. Vozny, S. M. Monti, A. Di Fiore, G. De Simone, and C. T. Supuran. "X-ray crystallographic and kinetic investigations of 6-sulfamoyl-saccharin as a carbonic anhydrase inhibitor." Organic & Biomolecular Chemistry 13, no. 13 (2015): 4064–69. http://dx.doi.org/10.1039/c4ob02648a.

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Teruya, Kanae, Kathryn F. Tonissen, and Sally-Ann Poulsen. "Recent developments of small molecule chemical probes for fluorescence-based detection of human carbonic anhydrase II and IX." MedChemComm 7, no. 11 (2016): 2045–62. http://dx.doi.org/10.1039/c6md00296j.

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The increasingly sophisticated array of approaches for the specific labeling and fluorescence-based detection of carbonic anhydrase enzymes using small molecule affinity-based chemical probes is reviewed.

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