Shell repair rates and carbonic anhydrase activity during shell repair in Helisoma duryi (Mollusca)

1983 ◽  
Vol 61 (3) ◽  
pp. 597-602 ◽  
Author(s):  
S. C. Kunigelis ◽  
A. S. M. Saleuddin
Keyword(s):  
Carbonic Anhydrase ◽  
Specific Activity ◽  
Regulatory System ◽  
Carbonic Anhydrase Activity ◽  
Mantle Tissue ◽  
Deposition Rates ◽  
Single Plane ◽  
Shell Repair ◽  
Shell Regeneration ◽  
Shell Deposition

Mantle tissue carbonic anhydrase titres were found to vary with shell deposition rates. Following shell injury at the growing edge, linear shell deposition rates and mantle tissue carbonic anhydrase specific activity were found to increase significantly. Increased mantle enzyme activity was detected for a period of 10 days following injury. Replacement of shell in the region of excision was found to occur on a plane slightly lower than that of the surrounding normal shell. This requires the establishment of a new growing edge so a single plane of deposition may be restored. This suggests that the process of shell regeneration does not only include the patching of the actual injury but also allows for the establishment of a new growing edge to correct for the displacement of the plane of shell deposition. These two components of the shell regeneration process have been designated phases I and II, respectively. A third phase allows for the thickening of the mineralized layers of the newly deposited shell. Localization of elevated carbonic anhydrase activity in the portion of the mantle directly underlying the shell injury suggests that a regulatory system is present which enables the animal to detect, define, and localize shell injury repair, expediting the process.

scholarly journals The Carbonic Anhydrase Inhibitor Ethoxzolamide Inhibits the Mycobacterium tuberculosis PhoPR Regulon and Esx-1 Secretion and Attenuates Virulence

2015 ◽  
Vol 59 (8) ◽  
pp. 4436-4445 ◽  
Author(s):  
Benjamin K. Johnson ◽  
Christopher J. Colvin ◽  
David B. Needle ◽  
Felix Mba Medie ◽  
Patricia A. DiGiuseppe Champion ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Carbonic Anhydrase ◽  
Regulatory System ◽  
Carbonic Anhydrase Activity ◽  
Carbonic Anhydrase Inhibitor ◽  
Fluorescent Reporter ◽  
Content Type ◽  
Pathogen Virulence ◽  
Mutant Phenotypes

ABSTRACTMycobacterium tuberculosismust sense and adapt to host environmental cues to establish and maintain an infection. The two-component regulatory system PhoPR plays a central role in sensing and responding to acidic pH within the macrophage and is required forM. tuberculosisintracellular replication and growthin vivo. Therefore, the isolation of compounds that inhibit PhoPR-dependent adaptation may identify new antivirulence therapies to treat tuberculosis. Here, we report that the carbonic anhydrase inhibitor ethoxzolamide inhibits the PhoPR regulon and reduces pathogen virulence. We show that treatment ofM. tuberculosiswith ethoxzolamide recapitulatesphoPRmutant phenotypes, including downregulation of the core PhoPR regulon, altered accumulation of virulence-associated lipids, and inhibition of Esx-1 protein secretion. Quantitative single-cell imaging of a PhoPR-dependent fluorescent reporter strain demonstrates that ethoxzolamide inhibits PhoPR-regulated genes in infected macrophages and mouse lungs. Moreover, ethoxzolamide reducesM. tuberculosisgrowth in both macrophages and infected mice. Ethoxzolamide inhibitsM. tuberculosiscarbonic anhydrase activity, supporting a previously unrecognized link between carbonic anhydrase activity and PhoPR signaling. We propose that ethoxzolamide may be pursued as a new class of antivirulence therapy that functions by modulating expression of the PhoPR regulon and Esx-1-dependent virulence.

Localization of carbonic anhydrase in the cytoplasmic membrane of Neisseria sicca (strain 19)

1981 ◽  
Vol 27 (1) ◽  
pp. 87-92 ◽  
Author(s):  
M. N. MacLeod ◽  
I. W. DeVoe
Keyword(s):  
Carbonic Anhydrase ◽  
Density Gradient ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sucrose Density Gradient ◽  
Carbonic Anhydrase Activity ◽  
Protein Patterns ◽  
Inner Membrane ◽  
Outer Membranes ◽  
Neisseria Sicca

The carbonic anhydrase activity and the growth of Neisseria sicca 19 were inhibited by the sulfonamide acetazolamide (10−5 M). Such inhibition was completely overcome by the addition of exogenous bicarbonate. Some carbonic anhydrase activity associated with the membranous envelope fraction of the cell was released when cells were broken by sonic treatment but not during cell breakage by high-pressure extrusion. After the selective solubilization (4 °C) of the inner membrane of envelopes by treatment with 1% sodium lauroyl sarcosinate, all detectable carbonic anhydrase activity was found in the soluble (inner membrane) fraction. After fractionation of the cell envelope into inner and outer membranes by treatment with ethylenediaminetetraacetate (EDTA) followed by sucrose density gradient centrifugation, the total and specific activity of carbonic anhydrase paralleled that of succinate dehydrogenase, an inner membrane enzyme marker. The Coomassie blue stained protein patterns after polyacrylamide gel electrophoresis of the bands from the sucrose density gradient provided confirmation that the inner and outer membranes had indeed been separated.

Why do hagfish have gill "chloride cells" when they need not regulate plasma NaCl concentration?

1987 ◽  
Vol 65 (8) ◽  
pp. 1956-1965 ◽  
Author(s):  
Jon Mallatt ◽  
David M. Conley ◽  
Richard L. Ridgway
Keyword(s):  
Carbonic Anhydrase ◽  
Ion Transport ◽  
Specific Activity ◽  
Carbonic Anhydrase Activity ◽  
Chloride Cells ◽  
Gillichthys Mirabilis ◽  
The Pacific ◽  
Nacl Concentration ◽  
Tubular System ◽  
Freshwater Teleosts

Two enzymes implicated in branchial ion transport, Na+-K+-ATPase and carbonic anhydrase, were localized in gill ionocytes ("chloride cells") of the Pacific hagfish, Eptatretus stouti, by light microscopic histochemical techniques. In hagfish, ouabain-sensitive Na+-K+-ATPase activity was confined to apical halves of ionocytes, where most of the cytoplasmic tubular system is located. In marine teleosts, Na+-K+-ATPase was noted in chloride cells and erythrocytes. Acetazolamide and potassium cyanate sensitive carbonic anhydrase activity occurred throughout the cytoplasm and nucleus of hagfish ionocytes. Biochemical assay of hagfish gill homogenates for Na+-K+-ATPase yielded a specific activity of 3.1 μmol Pi∙mg protein−1∙h−1 at 37 °C. This resembles values we obtained for freshwater fish (Carassius auratus: 3.3 μmol Pi∙mg protein−1∙h−1; Tilapia shirana: 3.7 μmol Pi∙mg protein−1∙h−1), and is less than values we obtained for marine teleosts (Pomacentrus spp.: 13 μmol Pi∙mg protein−1∙h−1; Gillichthys mirabilis: 6.7 μmol Pi∙mg protein−1∙h−1). Hagfish resemble freshwater teleosts in many other gill features related to ion transport. The presence of carbonic anhydrase in gill ionocytes of hagfish supports the proposal that these cells function in acid–base regulation, i.e., that they exchange H+ for Na+ and [Formula: see text] for Cl−.

Temperature-Related Changes in the Erythrocytic Carbonic Anhydrase (Acetazolamide-Sensitive Esterase) Activity of Goldfish, Carassius Auratus

1979 ◽  
Vol 78 (1) ◽  
pp. 255-264
Author(s):  
ARTHUR H. HOUSTON ◽  
KAREN M. MEAROW
Keyword(s):  
Carbonic Anhydrase ◽  
Carassius Auratus ◽  
Specific Activity ◽  
Thermal Sensitivity ◽  
Carbonic Anhydrase Activity ◽  
Red Cell ◽  
Goldfish Carassius Auratus ◽  
Species Activity ◽  
Plasma Chloride ◽  
Stable Plasma

1. Carbonic anhydrase activity in ‘membrane’ and ‘cytosol’ fractions of goldfish erythrocytes was assayed by the p-nitrophenyl acetate procedure following thermal acclimation. 2. The thermal sensitivity of ‘membrane’-associated activity was apparently unaltered by acclimation. ‘Cytosol’ activity in warm-acclimated specimens was somewhat more thermosensitive than that of animals maintained at low temperature. 3. Significant increases in specific activity, and activity per unit volume of packed cells and blood were observed at higher temperatures when assays were conducted at the temperatures at which the system actually functions in the fish. By contrast, when determinations were carried out at a standard temperature (41 °C) corresponding to the upper incipient lethal for this species, activity was either unaffected, or declined as acclimation temperatures increased. 4. Changes in carbonic anhydrase activity following acclimation are consistent with the hypothesis that this system is implicated in the maintenance of stable plasma chloride levels, and the suggestion that alterations in red cell chloride levels with temperature are, in part at least, attributable to concomitant variations in enzyme activity.

Carbonic anhydrase in mouse skeletal muscle and its influence on contractility

1994 ◽  
Vol 72 (5-6) ◽  
pp. 244-249 ◽  
Author(s):  
Claude H. Côté ◽  
Nicolas Jomphe ◽  
Abdul Odeimat ◽  
Pierre Frémont
Keyword(s):  
Skeletal Muscle ◽  
Carbonic Anhydrase ◽  
Specific Activity ◽  
Physiological Role ◽  
Electrophoretic Analysis ◽  
Carbonic Anhydrase Activity ◽  
Type I ◽  
Carbonic Anhydrase Iii ◽  
Metabolism Enzyme

Carbonic anhydrase III (EC 4.2.1.1) is the most abundant cytosolic protein in type I skeletal muscle fibers. Investigations of its physiological role have mostly been conducted with rat muscles, which sometimes are unsuitable for in vitro studies. The objective of the present study was to characterize the carbonic anhydrase in the mouse soleus muscle to verify if this muscle can be used as a model to further study the enzyme's function. Total carbonic anhydrase specific activity in the mouse soleus was comparable to the value for rat. However, 60% of the total carbonic anhydrase activity in the mouse was of the sulfonamide-sensitive type and, therefore, not related to carbonic anhydrase III. Electrophoretic analysis revealed the presence of a 29-kDa protein in total and cytosolic extracts of the mouse soleus. Immunoblotting with an antibody developed against rat carbonic anhydrase III showed that it was also specific for this 29-kDa peptide, which presumably is the mouse carbonic anhydrase III. Inhibition of the sulfonamide-sensitive activity had no effect on contractile and fatigue characteristics, whereas inhibition of the sulfonamide-resistant carbonic anhydrase III activity led to a significant increase in resistance to fatigue. We conclude that the mouse soleus may represent an excellent model to understand the contribution of different carbonic anhydrase isoforms to muscle physiology.Key words: muscle fatigue, carbonic anhydrase III, sulfonamide, metabolism, enzyme.

TOXICOLOGICAL EFFECTS OF METAL IONS AND SOME PESTICIDES ON CARBONIC ANHYDRASE ACTIVITY PURIFIED FROM BIGHEAD CARP (HYPOPHTHALMICHTHYS NOBILIS) GILL TISSUE

2021 ◽  
Vol 16 (1) ◽  
pp. 59-65
Author(s):  
Muammer KIRICI ◽  
Keyword(s):  
Carbonic Anhydrase ◽  
Metal Ions ◽  
Specific Activity ◽  
Gill Tissue ◽  
Carbonic Anhydrase Activity ◽  
Bighead Carp ◽  
Affinity Column ◽  
Toxicological Effects ◽  
Ic50 Values ◽  
Hypophthalmichthys Nobilis

In this work, the total carbonic anhydrase (CA) enzymes were obtained from bighead carp (Hypophthalmichthys nobilis) gill tissue with a purification fold of 239.62, specific activity of 26128.18 EU mg-1 and a yield of 44.04 % using Sepharose affinity column chromatography. For recording the CA purity, gel electrophoresis was performed in this part. The molecular weight (MW) of total CA enzyme was found 31 kDa. Additionally, the inhibitory effects of diverse pesticide compounds (carbaryl, carbofuran, permethrin, dimethoate, cypermethrin and λ-cyhalothrin) and heavy metals (Cu2+, Fe2+, Pb2+, Co2+) on CA bighead carp gill tissue CA enzyme activities were investigated and also the results calculated, and then plotted. The some pesticide compounds had IC50 amounts in the range of 0.36 - 253.35 μM. Also, the metal ions used had IC50 values ranging from 7.84 to 95.28 mm. As a result of these studies, a stable pH is set as pH: 8.0. CA inhibitors are target molecules in drug design studies.

The influence of saline drinking water on the activity of carbonic anhydrase in the shell gland of laying hens

1989 ◽  
Vol 40 (5) ◽  
pp. 1111 ◽  
Author(s):  
I Yoselewitz ◽  
D Balnave
Keyword(s):  
Drinking Water ◽  
Carbonic Anhydrase ◽  
Laying Hens ◽  
Specific Activity ◽  
Carbonic Anhydrase Activity ◽  
Shell Gland ◽  
Shell Quality ◽  
The Poor ◽  
Egg Shell ◽  
Reduced Activity

Carbonic anhydrase activity was measured in three experiments using mucosal extracts from the shell gland of laying hens given drinking water consisting of town water with or without the addition of sodium chloride (2 g/l). Hens laying eggs with normal or defective shells on both treatments were used. The specific activity of carbonic anhydrase was significantly lower in hens receiving the saline drinking water, but egg shell type had no significant effect on enzyme activity. The results indicate that a reduced activity of carbonic anhydrase in the shell gland contributes to the poor egg shell quality observed in hens receiving saline drinking water.

Milk enzymes—their distribution and activity

1970 ◽  
Vol 37 (2) ◽  
pp. 279-288 ◽  
Author(s):  
B. J. Kitchen ◽  
G. C. Taylor ◽  
I. C. White
Keyword(s):  
Carbonic Anhydrase ◽  
Specific Activity ◽  
Bovine Milk ◽  
Skim Milk ◽  
Total Activity ◽  
Carbonic Anhydrase Activity ◽  
Ammonium Sulphate Precipitation ◽  
Milk Serum ◽  
Fat Fraction ◽  
Mastitic Milk

SummaryThe distribution and activity of alkaline phosphatase (E.C. 3.1.3.1), acid phosphatase (E.C. 3.1.3.2), catalase (E.C. 1.11.1.6), xanthine oxidase (E.C. 1.2.3.2), aldolase (E.C. 4.1.2.7 and 4.1.2.13), ribonuclease (E.C. 2.7.7.16) and carbonic anhydrase (E.C. 4.2.1.1) were studied in the major components of bovine milk. Fractionation was accomplished by centrifugation of milk, skim-milk and buttermilk, and ammonium sulphate precipitation of skim-milk serum. The range of activities found for the enzymes studied are tabulated together with the activities of some of the enzymes in mastitic milk, and the significance of the results obtained is discussed. No carbonic anhydrase activity was detected in any of the samples tested. The other enzymes studied were found to have a greater proportion of their total activity located in the skim-milk fraction. However, all of these enzymes except ribonuclease had a higher specific activity in the fat fraction.

Carbonic anhydrase activity of intact erythrocytes from seven mammals

1983 ◽  
Vol 55 (4) ◽  
pp. 1292-1298 ◽  
Author(s):  
S. J. Dodgson ◽  
R. E. Forster
Keyword(s):  
Enzyme Activity ◽  
Carbonic Anhydrase ◽  
Bos Taurus ◽  
Specific Activity ◽  
Homo Sapiens ◽  
Mammalian Species ◽  
Hemoglobin Concentration ◽  
Carbonic Anhydrase Activity ◽  
Mean Cell Volume ◽  
Intracellular Enzyme

Carbonic anhydrase activity of intact erythrocytes from seven mammalian species was determined at 25 degrees C, pH 7.4, by mass spectrometry using the 18O-exchange technique. The seven species were Cavia porcellus, Mustela putorius furo, Felis domesticus, Canis familiaris, Homo sapiens, Equus caballus, and Bos taurus. Carbonic anhydrase activities determined as a function of hemoglobin concentration (std kcat) for intact erythrocytes at pH 7.4 were not significantly different from those determined for lysed erythrocytes at pH 7.20 for each species. The carbonic anhydrase activity of intact erythrocytes was not changed by a concentration of acetazolamide that inhibited it 85% in lysate (10(-7) M) in the 5-10 min needed for the assay. However, ethoxzolamide, another carbonic anhydrase inhibitor, produced the same fractional inhibition of enzyme activity in erythrocyte suspensions as in lysate in 1-2 min. Thus the inhibition constant, Ki, was approximately the same in both intact and lysed cells from each species, and it was possible to measure the apparent molar enzyme concentration inside the erythrocytes from the concentration of bound inhibitor. Intracellular enzyme concentrations were greater in those species with larger cells, but the specific activity of the carbonic anhydrase per molecule was less so that the overall enzyme activity, std kcat, was not related to mean cell volume. The effective permeability of the cells to the self-exchange of bicarbonate ion, P(HCO3-), averaged 2 X 10(-4) cm x s-1 and did not vary among the species.

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