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Claudiu T Supuran - One of the best experts on this subject based on the ideXlab platform.
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Sulphonamide inhibition profile of Staphylococcus aureus β-Carbonic Anhydrase
'Informa UK Limited', 2020Co-Authors: Linda J. Urbanski, Claudiu T Supuran, Andrea Angeli, Silvia Bua, Marianne Kuuslahti, Vesa. P. Hytönen, Seppo ParkkilaAbstract:This paper presents the production and kinetic and inhibitory characterisation of β-Carbonic Anhydrase from the opportunistic bacterium Staphylococcus aureus (SauBCA). From the eight different Carbonic Anhydrase (CA) families known to date, humans have only the α-form, whereas many clinically relevant pathogens have β- and/or γ-form(s). Based on this discovery, β- and γ-CAs have been introduced as promising new anti-infective targets. The results of this study revealed that recombinant SauBCA possesses significant CO2 hydration activity with a kcat of 1.46 × 105 s−1 and a kcat/KM of 2.56 × 107 s− 1M−1. Its enzymatic function was inhibited by various sulphonamides in the nanomolar − micromolar range, and the Ki of acetazolamide was 628 nM. The best inhibitor was the clinically used sulfamide agent famotidine (Ki of 71 nM). The least efficient inhibitors were zonisamide and dorzolamide. Our work encourages further investigations of SauBCA in an attempt to discover novel drugs against staphylococcal infections
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first evaluation of organotellurium derivatives as Carbonic Anhydrase i ii iv vii and ix inhibitors
Bioorganic Chemistry, 2018Co-Authors: Andrea Angeli, Damiano Tanini, Antonella Capperucci, Claudiu T SupuranAbstract:A series of tellurides was evaluated as Carbonic Anhydrase (CA, EC 4.2.1.1) inhibitors against the human (h) Carbonic Anhydrase isoforms hCA I, II, IV, VII and IX, involved in a variety of diseases, including glaucoma, retinitis pigmentosa, epilepsy, arthritis and tumors. These compounds, which are the first tellurium-containing derivatives acting as inhibitors of Carbonic Anhydrase enzymes, showed effective inhibition against all isoforms investigated and some of them were selective for inhibiting the cytosolic or the membrane-bound CAs. Thus, these Carbonic Anhydrase inhibitors are interesting leads for the development of isoform-selective inhibitors.
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Carbonic Anhydrase from Apis mellifera: purification and inhibition by pesticides
'Informa UK Limited', 2017Co-Authors: Ercan Soydan, Claudiu T Supuran, Murat şenturk, Ahmet Güler, Selim Bıyık, Deniz EkinciAbstract:Carbonic Anhydrase (CA) enzymes have been shown to play an important role in ion transport and in pH regulation in several organisms. Despite this information and the wealth of knowledge regarding the significance of CA enzymes, few studies have been reported about bee CA enzymes and the hazardous effects of chemicals. Using Apis mellifera as a model, this study aimed to determine the risk of pesticides on Apis mellifera Carbonic Anhydrase enzyme (Am CA). CA was initially purified from Apis mellifera spermatheca for the first time in the literature. The enzyme was purified with an overall purification of ∼35-fold with a molecular weight of ∼32 kDa. The enzyme was then exposed to pesticides, including tebuconazole, propoxur, carbaryl, carbofuran, simazine and atrazine. The six pesticides dose-dependently inhibited in vitro AmCA activity at low micromolar concentrations. IC50 values for the pesticides were 0.0030, 0.0321, 0.0031, 0.0087, 0.0273 and 0.0165 μM, respectively. The AmCA inhibition mechanism of these compounds is unknown at this moment
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advances in structure based drug discovery of Carbonic Anhydrase inhibitors
Expert Opinion on Drug Discovery, 2017Co-Authors: Claudiu T SupuranAbstract:Introduction: The enzyme Carbonic Anhydrase (CA, EC 4.2.1.1) is found in numerous organisms across the tree of life, with seven distinct classes known to date. CA inhibition can be exploited for th...
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Isatin: a privileged scaffold for the design of Carbonic Anhydrase inhibitors.
Journal of enzyme inhibition and medicinal chemistry, 2016Co-Authors: Claudia Melis, Claudiu T Supuran, Andrea Angeli, Rita Meleddu, Simona Distinto, Giulia Bianco, Clemente Capasso, Filippo Cottiglia, Rossella Angius, Elias MaccioniAbstract:The isatin scaffold is the constitutive fragment of several natural and synthetic bioactive molecules. Albeit several benzene sulphonamide-based Carbonic Anhydrase inhibitors (CAIs) have been reported, only recently isatin benzene sulphonamides have been studied and proposed as CAIs. In this study we have designed, synthesised, and evaluated the biological activity of a series of differently substituted isatin-based benzene sulphonamides which have been designed for the inhibition of Carbonic Anhydrase isoforms. The activity of all the synthesised compounds was evaluated towards human Carbonic Anhydrase I, II, IX, and XII isozymes. Our results indicate that the nature and position of substituents on the isatin ring can modulate both activity and isozyme selectivity.
Bruce L Tufts - One of the best experts on this subject based on the ideXlab platform.
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evidence for membrane bound Carbonic Anhydrase in the air bladder of bowfin amia calva a primitive air breathing fish
The Journal of Experimental Biology, 1998Co-Authors: Matthieu R Gervais, Bruce L TuftsAbstract:The purpose of this study was to examine the subcellular distribution and isoenzyme characteristics of Carbonic Anhydrase from the gills and respiratory air bladder of bowfin Amia calva, a primitive air-breathing fish. Separation of subcellular fractions by differential centrifugation revealed that the vast majority of Carbonic Anhydrase from the gills of bowfin originated from the cytoplasmic fraction. Washing of the gill microsomal pellet also indicated that the Carbonic Anhydrase originally associated with this pellet was largely due to contamination from the cytoplasmic fraction. Experiments with a Carbonic Anhydrase inhibitor, sulphanilamide, and the plasma Carbonic Anhydrase inhibitor from this species confirmed that the bowfin gill probably contains only one Carbonic Anhydrase isoenzyme which had properties resembling those of CA II. In contrast to the situation in the gills, a relatively large percentage (27%) of the total air bladder Carbonic Anhydrase was associated with the microsomal fraction. Washing of the air bladder microsomal pellet removed little of the Carbonic Anhydrase activity, indicating that most of the Carbonic Anhydrase in the microsomal fraction was associated with the membranes. Like the mammalian pulmonary CA IV isoenzyme, microsomal Carbonic Anhydrase from the bowfin air bladder was less sensitive to the bowfin plasma Carbonic Anhydrase inhibitor, sodium dodecylsulphate (SDS) and sulphanilamide than was cytoplasmic Carbonic Anhydrase from the air bladder. Microsomal Carbonic Anhydrase from the bowfin air bladder also resembled CA IV in that it appears to be anchored to the membrane via a phosphatidylinositol-glycan linkage which could be cleaved by phosphatidylinositol-specific phospholipase C. Taken together, these results suggest that a membrane-bound Carbonic Anhydrase isoenzyme resembling mammalian CA IV in terms of inhibition characteristics and membrane attachment is present in the air-breathing organ of one of the most primitive air-breathing vertebrates.
Enelise Marcelle Amado - One of the best experts on this subject based on the ideXlab platform.
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hemolymph and gill Carbonic Anhydrase are more sensitive to aquatic contamination than mantle Carbonic Anhydrase in the mangrove oyster crassostrea rhizophorae
Comparative Biochemistry and Physiology C-toxicology & Pharmacology, 2017Co-Authors: Matheus Barbosa Dos Santos, Ignacio Evaristo Monteiro Neto, Sarah Rachel Candido De Souza Melo, Enelise Marcelle AmadoAbstract:Abstract Carbonic Anhydrase (CA) is a ubiquitous metalloenzyme of great importance in several physiological processes. Due to its physiological importance and sensitivity to various pollutants, CA activity has been used as biomarker of aquatic contamination. Considering that in bivalves the sensitivity of CA to pollutants seems to be tissue-specific, we proposed here to analyze CA activity of hemolymph, gill and mantle of Crassostrea rhizophorae collected in two tropical Brazilian estuaries with different levels of anthropogenic impact, in dry and rainy season. We found increased Carbonic Anhydrase activity in hemolymph, gill and mantle of oysters collected in the Paraiba Estuary (a site of high anthropogenic impact) when compared to oysters from Mamanguape Estuary (inserted in an area of environmental preservation), especially in the rainy season. CA of hemolymph and gill were more sensitive than mantle CA to aquatic contamination. This study enhances the suitability of Carbonic Anhydrase activity for field biomarker applications with bivalves and brings new and relevant information on hemolymph Carbonic Anhydrase activity as biomarker of aquatic contamination.
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hemolymph and gill Carbonic Anhydrase are more sensitive to aquatic contamination than mantle Carbonic Anhydrase in the mangrove oyster crassostrea rhizophorae
Comparative Biochemistry and Physiology C-toxicology & Pharmacology, 2017Co-Authors: Matheus Barbosa Dos Santos, Ignacio Evaristo Monteiro Neto, Sarah Rachel Candido De Souza Melo, Enelise Marcelle AmadoAbstract:Carbonic Anhydrase (CA) is a ubiquitous metalloenzyme of great importance in several physiological processes. Due to its physiological importance and sensitivity to various pollutants, CA activity has been used as biomarker of aquatic contamination. Considering that in bivalves the sensitivity of CA to pollutants seems to be tissue-specific, we proposed here to analyze CA activity of hemolymph, gill and mantle of Crassostrea rhizophorae collected in two tropical Brazilian estuaries with different levels of anthropogenic impact, in dry and rainy season. We found increased Carbonic Anhydrase activity in hemolymph, gill and mantle of oysters collected in the Paraiba Estuary (a site of high anthropogenic impact) when compared to oysters from Mamanguape Estuary (inserted in an area of environmental preservation), especially in the rainy season. CA of hemolymph and gill were more sensitive than mantle CA to aquatic contamination. This study enhances the suitability of Carbonic Anhydrase activity for field biomarker applications with bivalves and brings new and relevant information on hemolymph Carbonic Anhydrase activity as biomarker of aquatic contamination.
Matthieu R Gervais - One of the best experts on this subject based on the ideXlab platform.
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evidence for membrane bound Carbonic Anhydrase in the air bladder of bowfin amia calva a primitive air breathing fish
The Journal of Experimental Biology, 1998Co-Authors: Matthieu R Gervais, Bruce L TuftsAbstract:The purpose of this study was to examine the subcellular distribution and isoenzyme characteristics of Carbonic Anhydrase from the gills and respiratory air bladder of bowfin Amia calva, a primitive air-breathing fish. Separation of subcellular fractions by differential centrifugation revealed that the vast majority of Carbonic Anhydrase from the gills of bowfin originated from the cytoplasmic fraction. Washing of the gill microsomal pellet also indicated that the Carbonic Anhydrase originally associated with this pellet was largely due to contamination from the cytoplasmic fraction. Experiments with a Carbonic Anhydrase inhibitor, sulphanilamide, and the plasma Carbonic Anhydrase inhibitor from this species confirmed that the bowfin gill probably contains only one Carbonic Anhydrase isoenzyme which had properties resembling those of CA II. In contrast to the situation in the gills, a relatively large percentage (27%) of the total air bladder Carbonic Anhydrase was associated with the microsomal fraction. Washing of the air bladder microsomal pellet removed little of the Carbonic Anhydrase activity, indicating that most of the Carbonic Anhydrase in the microsomal fraction was associated with the membranes. Like the mammalian pulmonary CA IV isoenzyme, microsomal Carbonic Anhydrase from the bowfin air bladder was less sensitive to the bowfin plasma Carbonic Anhydrase inhibitor, sodium dodecylsulphate (SDS) and sulphanilamide than was cytoplasmic Carbonic Anhydrase from the air bladder. Microsomal Carbonic Anhydrase from the bowfin air bladder also resembled CA IV in that it appears to be anchored to the membrane via a phosphatidylinositol-glycan linkage which could be cleaved by phosphatidylinositol-specific phospholipase C. Taken together, these results suggest that a membrane-bound Carbonic Anhydrase isoenzyme resembling mammalian CA IV in terms of inhibition characteristics and membrane attachment is present in the air-breathing organ of one of the most primitive air-breathing vertebrates.
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Evidence for membrane‐bound Carbonic Anhydrase in the air bladder of bowfin (Amia calva), a primitive air‐breathing fish
1998Co-Authors: Matthieu R Gervais, L. TuftsAbstract:The purpose of this study was to examine the subcellular distribution and isoenzyme characteristics of Carbonic Anhydrase from the gills and respiratory air bladder of bowfin Amia calva, a primitive air-breathing fish. Separation of subcellular fractions by differential centrifugation revealed that the vast majority of Carbonic Anhydrase from the gills of bowfin originated from the cytoplasmic fraction. Washing of the gill microsomal pellet also indicated that the Carbonic Anhydrase originally associated with this pellet was largely due to contamination from the cytoplasmic fraction. Experiments with a Carbonic Anhydrase inhibitor, sulphanilamide, and the plasma Carbonic Anhydrase inhibitor from this species confirmed that the bowfin gill probably contains only one Carbonic Anhydrase isoenzyme which had propertie
Matheus Barbosa Dos Santos - One of the best experts on this subject based on the ideXlab platform.
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hemolymph and gill Carbonic Anhydrase are more sensitive to aquatic contamination than mantle Carbonic Anhydrase in the mangrove oyster crassostrea rhizophorae
Comparative Biochemistry and Physiology C-toxicology & Pharmacology, 2017Co-Authors: Matheus Barbosa Dos Santos, Ignacio Evaristo Monteiro Neto, Sarah Rachel Candido De Souza Melo, Enelise Marcelle AmadoAbstract:Abstract Carbonic Anhydrase (CA) is a ubiquitous metalloenzyme of great importance in several physiological processes. Due to its physiological importance and sensitivity to various pollutants, CA activity has been used as biomarker of aquatic contamination. Considering that in bivalves the sensitivity of CA to pollutants seems to be tissue-specific, we proposed here to analyze CA activity of hemolymph, gill and mantle of Crassostrea rhizophorae collected in two tropical Brazilian estuaries with different levels of anthropogenic impact, in dry and rainy season. We found increased Carbonic Anhydrase activity in hemolymph, gill and mantle of oysters collected in the Paraiba Estuary (a site of high anthropogenic impact) when compared to oysters from Mamanguape Estuary (inserted in an area of environmental preservation), especially in the rainy season. CA of hemolymph and gill were more sensitive than mantle CA to aquatic contamination. This study enhances the suitability of Carbonic Anhydrase activity for field biomarker applications with bivalves and brings new and relevant information on hemolymph Carbonic Anhydrase activity as biomarker of aquatic contamination.
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hemolymph and gill Carbonic Anhydrase are more sensitive to aquatic contamination than mantle Carbonic Anhydrase in the mangrove oyster crassostrea rhizophorae
Comparative Biochemistry and Physiology C-toxicology & Pharmacology, 2017Co-Authors: Matheus Barbosa Dos Santos, Ignacio Evaristo Monteiro Neto, Sarah Rachel Candido De Souza Melo, Enelise Marcelle AmadoAbstract:Carbonic Anhydrase (CA) is a ubiquitous metalloenzyme of great importance in several physiological processes. Due to its physiological importance and sensitivity to various pollutants, CA activity has been used as biomarker of aquatic contamination. Considering that in bivalves the sensitivity of CA to pollutants seems to be tissue-specific, we proposed here to analyze CA activity of hemolymph, gill and mantle of Crassostrea rhizophorae collected in two tropical Brazilian estuaries with different levels of anthropogenic impact, in dry and rainy season. We found increased Carbonic Anhydrase activity in hemolymph, gill and mantle of oysters collected in the Paraiba Estuary (a site of high anthropogenic impact) when compared to oysters from Mamanguape Estuary (inserted in an area of environmental preservation), especially in the rainy season. CA of hemolymph and gill were more sensitive than mantle CA to aquatic contamination. This study enhances the suitability of Carbonic Anhydrase activity for field biomarker applications with bivalves and brings new and relevant information on hemolymph Carbonic Anhydrase activity as biomarker of aquatic contamination.