Carbonic Anhydrase Activity During the Larval-Pupal Transformation of Hyalophora Cecropia Reared on Foliage and Synthetic Diet: Effects of Potassium and Chloride on Midgut, Fat Body and Integumentary Enzymes

1981 ◽  
Vol 91 (1) ◽  
pp. 255-269
Author(s):  
JAMES W. JOHNSTON ◽  
ARTHUR M. JUNGREIS
Keyword(s):  
Carbonic Anhydrase ◽  
Fat Body ◽  
Larval Instar ◽  
Pupal Stage ◽  
Carbonic Anhydrase Activity ◽  
Larval Midgut ◽  
Synthetic Diet ◽  
Heat Stable ◽  
Hyalophora Cecropia ◽  
Diet Type

1. Carbonic anhydrase was measured in tissues of silkmoths, Hyalophora cecropia, reared on either a wheatgerm-based synthetic diet or wild cherry foliage in feeding fifth-instar larvae, throughout the larval舑pupal transformation and in newly ecdysed pupae. 2. Carbonic anhydrase activity was present in fat body, midgut and intgeumentary epithelial cells, but not in haemolymph, cuticle or the integumentary musculature. 3. Approximately 70 % of the total carbonic anhydrase present per animal is localized within the epidermal cells of the integument. 4. The midgut is without measurable carbonic anhydrase activity from the day of apolysis (through the newly ecdysed pupal stage in development) until after the larval-pupal ecdysis. 5. In tissues analysed during the feeding fifth larval instar, 150 toward acetazolamide was between 10舑8 and 10舑7 m. 6. With the exception of larval midgut, regardless of stage, tissue or diet, both potassium and chloride normally inhibit carbonic anhydrase, with the effects of potassium and chloride being additive. 7. In larval midgut, chloride at concentrations of 50 or 150 mm stimulates carbonic anhydrase activity 30 or 100%, respectively. 8. In foliage-reared insects, potassium enhances chloride stimulation of larval midgut carbonic anhydrase, whereas in synthetic-diet-reared insects, potassium antagonizes the stimulatory effects of chloride. 9. Removal of a heat-stable, dialysable factor associated with the larval midgut of foliage-reared insects converts properties of the foliage midgut enzyme to those characteristic of the synthetic diet type, and vice versa.

INHIBITORS OF CARBONIC ANHYDRASE IN THE AMERICAN COCKROACH, PERIPLANETA AMERICANA (L.)

1956 ◽  
Vol 34 (1) ◽  
pp. 68-74 ◽  
Author(s):  
Ann D. Anderson ◽  
Ralph B. March
Keyword(s):  
Carbonic Anhydrase ◽  
Periplaneta Americana ◽  
Fat Body ◽  
Aqueous Media ◽  
Carbonic Anhydrase Activity ◽  
American Cockroach ◽  
Tissue Homogenates ◽  
Organic Insecticides ◽  
Cell Fragments

Carbonic anhydrase activity has been demonstrated in vitro in preparations of the head, fat body, and gut of the American cockroach, Periplaneta americana (L.), and in the adult housefly, Musca domestica L. The insect factor, which is soluble in aqueous media and can be separated from the particulate cell fragments of insect tissue homogenates is heat labile and sensitive to cyanide inactivation. It is strongly inhibited by sulphanilamide, p-aminoethylphenyl-sulphonamide, and p-chlorphenylsulphonamide. No inhibition has been found with N-substituted sulphonamides or with any of the organic insecticides examined, including DDT, lindane, dieldrin, nicotine, rotenone, pyrethrins, and para-oxon. Sensitivity of carbonic anhydrase to sulphonamides having an intact—SO2NH2 group is also characteristic of mammalian preparations. The data indicate that inhibition of insect carbonic anhydrase cannot be an important factor in the mode of action of DDT or other organic insecticides.

The Halloween genes code for cytochrome P450 enzymes mediating synthesis of the insect moulting hormone

2006 ◽  
Vol 34 (6) ◽  
pp. 1256-1260 ◽  
Author(s):  
K.F. Rewitz ◽  
R. Rybczynski ◽  
J.T. Warren ◽  
L.I. Gilbert
Keyword(s):  
Cytochrome P450 ◽  
Fat Body ◽  
Larval Instar ◽  
Primary Source ◽  
Pupal Stage ◽  
Prothoracic Gland ◽  
Cytochrome P450 Enzymes ◽  
Biosynthetic Activity ◽  
Prothoracic Glands

The developmental events occurring during moulting and metamorphosis of insects are controlled by precisely timed changes in levels of ecdysteroids, the moulting hormones. The final four sequential hydroxylations of steroid precursors into the active ecdysteroid of insects, 20E (20-hydroxyecdysone), are mediated by four cytochrome P450 (P450) enzymes, encoded by genes in the Halloween family. Orthologues of the Drosophila Halloween genes phantom (phm; CYP306A1), disembodied (dib; CYP302A1), shadow (sad; CYP315A1) and shade (shd; CYP314A1) were obtained from the endocrinological model insect, the tobacco hornworm Manduca sexta. Expression of these genes was studied and compared with changes in the ecdysteroid titre that controls transition from the larval to pupal stage. phm, dib and sad, which encode P450s that mediate the final hydroxylations in the biosynthesis of ecdysone, were selectively expressed in the prothoracic gland, the primary source of ecdysone during larval and pupal development. Changes in their expression correlate with the haemolymph ecdysteroid titre during the fifth (final) larval instar. Shd, the 20-hydroxylase, which converts ecdysone into the more active 20E, is expressed in tissues peripheral to the prothoracic glands during the fifth instar. Transcript levels of shd in the fat body and midgut closely parallel the enzyme activity measured in vitro. The results indicate that these Halloween genes are transcriptionally regulated to support the high biosynthetic activity that produces the cyclic ecdysteroid pulses triggering moulting.

1123: Renal Oxalate Transport Depends on Local Carbonic Anhydrase Activity in the Proximal Tubule

2004 ◽  
Vol 171 (4S) ◽  
pp. 296-296
Author(s):  
Michael Straub ◽  
Joséphine Befolo-Elo ◽  
Richard E Hautmann ◽  
Edgar Braendle
Keyword(s):  
Carbonic Anhydrase ◽  
Proximal Tubule ◽  
Carbonic Anhydrase Activity ◽  
Oxalate Transport

scholarly journals Purification and characterization of fat body lipase from the greater wax moth, Galleria mellonella (Lepidoptera: Pyralidae)

2019 ◽  
Vol 81 (1) ◽  
Author(s):  
Rahma R. Z. Mahdy ◽  
Shaimaa A. Mo’men ◽  
Marah M. Abd El-Bar ◽  
Emad M. S. Barakat
Keyword(s):  
Metal Ions ◽  
Kinetic Parameters ◽  
Biochemical Characterization ◽  
Galleria Mellonella ◽  
Fat Body ◽  
Specific Activity ◽  
Larval Instar ◽  
Gel Filtration ◽  
Molecular Weights

Abstract Background Insect lipid mobilization and transport are currently under research, especially lipases and lipophorin because of their roles in the production of energy and lipid transport at a flying activity. The present study has been conducted to purify intracellular fat body lipase for the first time, from the last larval instar of Galleria mellonella. Results Purification methods by combination of ammonium sulfate [(NH4)2SO4] precipitation and gel filtration using Sephadex G-100 demonstrated that the amount of protein and the specific activity of fat body lipase were 0.008633 ± 0.000551 mg/ml and 1.5754 ± 0.1042 μmol/min/mg protein, respectively, with a 98.9 fold purity and recovery of 50.81%. Hence, the sephadex G-100 step was more effective in the purification process. SDS-PAGE and zymogram revealed that fat body lipase showed two monomers with molecular weights of 178.8 and 62.6 kDa. Furthermore, biochemical characterization of fat body lipase was carried out through testing its activities against several factors, such as different temperatures, pH ranges, metal ions, and inhibitors ending by determination of their kinetic parameters with the use of p-nitrophenyl butyrate (PNPB) as a substrate. The highest activities of enzyme were determined at the temperature ranges of 35–37 °C and 37–40 °C and pH ranges of 7–9 and 7–10. The partially purified enzyme showed significant stimulation by Ca2+, K+, and Na+ metal ions indicating that fat body lipase is metalloproteinase. Lipase activity was strongly inhibited by some inhibitors; phenylmethylsulfonyl fluoride (PMSF), ethylene-diaminetetractic acid (EDTA), and ethylene glycoltetraacetic acid (EGTA) providing evidence of the presence of serine residue and activation of enzymes by metal ions. Kinetic parameters were 0.316 Umg− 1 Vmax and 301.95 mM Km. Conclusion Considering the purification of fat body lipase from larvae and the usage of some inhibitors especially ion chelating agents, it is suggested to develop a successful control of Galleria mellonella in near future by using lipase inhibitors.

scholarly journals Pathogenicity and Side Effect of Indigenous Beauveria bassiana on Coccinella undecimpunctata and Hippodamia variegata (Coleoptera: Coccinellidae)

Insects ◽  
2021 ◽  
Vol 12 (1) ◽  
pp. 42
Author(s):  
Samy Sayed ◽  
Sayed-Ashraf Elarrnaouty ◽  
Saad AlOtaibi ◽  
Mohamed Salah
Keyword(s):  
Beauveria Bassiana ◽  
Indirect Effect ◽  
Developmental Stages ◽  
Larval Instar ◽  
Pupal Stage ◽  
Tween 80 ◽  
Contact Method ◽  
Coccinella Undecimpunctata ◽  
Hippodamia Variegata ◽  
Application Methods

This study aimed to estimate the virulence of an indigenous Beauveria bassiana on all developmental stages of two indigenous coccinellids; Coccinella undecimpunctata and Hippodamia variegata through three application methods; direct spray, contact method, and feeding on aphids treated with the fungus (ingestion). Also, indirect effect on all developmental stages resulted from 1st larval instar treated with these application methods. All treatments were done with a concentration of 1 × 105 which was recommended in previous studies for different aphid species with a control of 0.02% Tween 80 (v/v). The mortality of 1st larval instar of both H. variegata and C. undecimpunctata and pupal stage of C. undecimpunctata were significantly increased with spray method only. Also, contact method achieved significantly higher mortality on 1st larval instar of C. undecimpunctata only. Regard to indirect effect, except of mortality of 1st larval instar of both predators and 2nd larval instar of H. variegata, other developmental instars/stages of both predators were not affected by B. bassiana through the three tested application methods in the mortality, duration, survival, cumulative survival male and female longevity, and fecundity. Therefore, both tested predatory coccinellids could be compatible with this indigenous isolate of B. bassiana where, in general, there are no negative effects of the fungus on both predators.

RENAL CARBONIC ANHYDRASE IN PREMATURE AND MATURE INFANTS

PEDIATRICS ◽  
1951 ◽  
Vol 7 (2) ◽  
pp. 182-185
Author(s):  
RICHARD DAY ◽  
JANE FRANKLIN
Keyword(s):  
Carbonic Anhydrase ◽  
Premature Infants ◽  
Carbonic Anhydrase Activity ◽  
Renal Carbonic Anhydrase

The carbonic anhydrase activity in the kidneys of premature infants was studied because it was thought that if the renal enzyme is as deficient as that in the blood, inefficiency in acidification of urine might result. In contrast with the blood, postmortem specimens of kidneys of premature infants were found to exhibit carbonic anhydrase activity similar to that found in the case of kidneys from older infants and adults.

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