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Wyświetlanie 1-10 z 177
Tytuł:
The activity of class I, II, III and IV alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in the sera of bladder cancer patients
Autorzy:
Orywal, Karolina
Jelski, Wojciech
Werel, Tadeusz
Szmitkowski, Maciej
Tematy:
alcohol dehydrogenase isoenzymes
aldehyde dehydrogenase
bladder cancer
Pokaż więcej
Wydawca:
Polskie Towarzystwo Biochemiczne
Powiązania:
https://bibliotekanauki.pl/articles/1038688.pdf  Link otwiera się w nowym oknie
Opis:
Objectives. Studies on alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) activity in the sera of patients with malignant neoplasms show that cancer cells in many organs may release ADH isoenzymes into the blood. The aim of this study was to investigate the differences in the activity of ADH isoenzymes and ALDH in the sera of patients with bladder cancer (BCa), and with different grades of the disease. Material and Methods. Blood samples were taken from 39 patients with BCa (15 patients with low-grade and 24 with high-grade BCa) and from 60 healthy subjects. Class III and IV of ADH and total ADH activity were measured using the photometric method, while class I and II ADH and ALDH activity using the fluorometric method with class-specific fluorogenic substrates. Results. The activity of the class I ADH isoenzyme and total ADH was significantly higher in the sera of BCa patients as compared to control group. Analysis of ALDH activity did not show statistically significant differences between the tested groups. Significantly higher total activity of ADH in comparison to control was found in both, low-grade and high-grade BCa group. The activity of ADH class I was also significantly higher in high-grade BCa group when compared to low-grade patients and controls. Conclusion. The increase of total ADH activity in the sera of BCa patients seems to be caused by isoenzymes released from cancerous cells. The higher activity of ADH I probably resulted from metastatic tumors as significant increase was detected only in the sera of high-grade bladder cancer patients.
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Substrate and Inhibitor Spectra of Ethylbenzene Dehydrogenase: Perspectives on Application Potential and Catalytic Mechanism
Autorzy:
Dudzik, Agnieszka
Heidera, Johann
Knack, Daniel
Salwinski, Aleksander
Szaleniec, Maciej
Hagel, Corina
Wydawca:
American Society for Microbiology
Cytata wydawnicza:
D. Knack, C. Hagel, M. Szaleniec, A. Dudzik, A. Salwinski, J. Heider, "Substrate and inhibitor spectrum of ethylbenzene dehydrogenase: perspectives on application potential and catalytic mechanism", Appl. Environ. Microb., 78 (2012) 6475–6482
Opis:
the priority program 1319 of the German Research Foundation (DFG), he excellence program LOEWE/Synmikro from the state of Hessen in Germany, computational grant MNiSW/SGI3700/PAN/121/2006, the Polish National Science Center under grant N N204 269038, Biotransformations for Pharmaceutical and Cosmetics Industry No. POIG.01.03.01-00-158/09-00, funded in part by the European Union within the European Regional Development Fund.
Maciej Szaleniec
Ethylbenzene dehydrogenase (EbDH) catalyzes the initial step in anaerobic degradation of ethylbenzene in denitrifying bacteria, namely, the oxygen-independent hydroxylation of ethylbenzene to (S)-1-phenylethanol. In our study we investigate the kinetic properties of 46 substrate analogs acting as substrates or inhibitors of the enzyme. The apparent kinetic parameters of these compounds give important insights into the function of the enzyme and are consistent with the predicted catalytic mechanism based on a quantum chemical calculation model. In particular, the existence of the proposed substrate-derived radical and carbocation intermediates is substantiated by the formation of alternative dehydrogenated and hydroxylated products from some substrates, which can be regarded as mechanistic models. In addition, these results also show the surprisingly high diversity of EbDH in hydroxylating different kinds of alkylaromatic and heterocyclic compounds to the respective alcohols. This may lead to attractive industrial applications of ethylbenzene dehydrogenase for a new process of producing alcohols via hydroxylation of the corresponding aromatic hydrocarbons rather than the customary procedure of reducing the corresponding ketones.
Dostawca treści:
Repozytorium Centrum Otwartej Nauki
Artykuł
Tytuł:
THE ACTIVITY OF SUCCINIC DEHYDROGENASE IN GLIAL TUMORS
Autorzy:
Mossakowski, Mirosław Jan (1929–2001)
Wydawca:
Lawrence Ks.
Powiązania:
Journal of Neuropathology and Experimental Neurology
Opis:
Succinic dehydrogenase activity of astrocytic tumors of varying degrees of anaplasia was assessed by means of the tetrazolium reaction and compared with the activity in oligodendrogliomas and in the various elements of normal brain. Succinic dehydrogenase activity was present in all glial tumors examined. It increased with increasing anaplasia of the tumors. The SDA of oligoden¬droglioma, while high, was less than that of glioblastoma multiforme. The SDA in the cells of piloid astrocytoma appeared to be similar to that of normal astrocytes in white matter. SDA in the cells of gemistocytic astro¬cytoma, malignant glioma and glioblastoma multiforme exceeded considerably that in normal glia. Reactive glia also showed greater SDA than normal glia. There appears to be a relationship between the volume of cytoplasm con¬stituting the cel body and the amount of SDA exhibited by the cell.
Dostawca treści:
RCIN - Repozytorium Cyfrowe Instytutów Naukowych
Książka
Tytuł:
The alcohol dehydrogenase isoenzyme (ADH IV) as a candidate tumour marker of esophageal cancer
Autorzy:
Jelski, Wojciech
Laniewska-Dunaj, Magdalena
Niklinski, Jacek
Kozłowski, Miroslaw
Laudanski, Jerzy
Szmitkowski, Maciej
Tematy:
alcohol dehydrogenase isoenzymes
esophageal cancer
Pokaż więcej
Wydawca:
Polskie Towarzystwo Biochemiczne
Powiązania:
https://bibliotekanauki.pl/articles/1039560.pdf  Link otwiera się w nowym oknie
Opis:
Objective: Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) are present in esophageal cancer cells. Moreover the total activity of ADH as well as the activity of class IV ADH isoenzyme is significantly higher in cancer tissue than in healthy mucosa. The activity of these enzymes in cancer cells is reflected in the sera and could thus be helpful for diagnostics of esophageal cancer. The aim of this study was to investigate a potential significance of ADH isoenzymes and ALDH as tumour markers of esophageal cancer. We defined diagnostic sensitivity, specificity, predictive value for positive and negative results, and receiver-operating characteristics (ROC) curve for tested enzymes. Methods: Serum samples were taken for routine biochemical investigation from 180 patients with esophageal cancer before treatment. Total ADH activity was measured by a photometric method with p-nitrosodimethylaniline as a substrate and ALDH activity by a fluorometric method with 6-methoxy-2-naphtaldehyde as a substrate. For the measurement of the activity of class I and II isoenzymes we employed the fluorometric methods, with class-specific fluorogenic substrates. The activity of class III alcohol dehydrogenase was measured by a photometric method with formaldehyde and class IV with m-nitrobenzaldehyde as a substrate. Results: There was a significant increase in the activity of class IV of ADH isoenzyme (7.65 mU/l vs 5.88 mU/l) and total ADH activity (1198 mU/l vs 848 mU/l) in the sera of esophageal cancer patients compared to the control. The diagnostic sensitivity for ADH IV was 72%, the specificity 76%, the positive and negative predictive values were 80% and 72% respectively. The area under the ROC curve for ADH IV was 0.65. Conclusion: The results suggest a potential significance of ADH IV as a marker of esophageal cancer.
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Enzymatic activity of soils exposed to transportation pollutants, located along road no. 957
Autorzy:
Filipek-Mazur, B.
Tabak, M.
Gorczyca, O.
Tematy:
soil
transportation
dehydrogenase
catalase
arylsulfatase
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Wydawca:
Polskie Towarzystwo Inżynierii Ekologicznej
Powiązania:
https://bibliotekanauki.pl/articles/125389.pdf  Link otwiera się w nowym oknie
Opis:
he research was conducted in order to determine the catalase, dehydrogenase, and arylsulfatase activities of soils exposed to transportation pollutants. The research material consisted of soil samples collected from points located along road no. 957 at a section passing through Zawoja (the Malopolska Region), from places at a distance of 5 and 200 m from the road edge. The samples were collected from a 0–10 cm layer, from areas covered with grasses. No considerable diversification in the enzymatic activity of the soils, depending on their distance from the road edge, was found. The mean activity of catalase and dehydrogenases in the soils located 5 m from the road edge was, respectively, 4 and 7% greater than the activity of the soils located 200 m from the road edge. The mean arylsulfatase activity in the soils located 5 m from the road edge was 3% lower than in the soils located at a distance of 200 m. A positive correlation was found between the catalase and arylsulfatase activities, and the dehy-drogenase activity in the soils.
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Isolation and characterization of novel human short-chain dehydrogenase/reductase SCDR10B which is highly expressed in the brain and acts as hydroxysteroid dehydrogenase*
Autorzy:
Huang, Chaoqun
Wan, Bo
Gao, Bo
Hexige, Saiyin
Yu, Long
Tematy:
expression pattern
clone
brain
hydroxysteroid dehydrogenase
Pokaż więcej
Wydawca:
Polskie Towarzystwo Biochemiczne
Powiązania:
https://bibliotekanauki.pl/articles/1040586.pdf  Link otwiera się w nowym oknie
Opis:
Hydroxysteroid dehydrogenase belongs to the subfamily of short-chain dehydrogenases/reductases (SDR), and 11-β-hydroxysteroid dehydrogenase catalyzes the interconversion of inactive glucocorticoids (cortisone in human, dehydrocorticosterone in rodents) and active glucocorticoids (cortisol in human, corticosterone in rodents). We report here the cloning and characterization of a novel human SDR gene SCDR10B which encodes a protein with similarity to 11β-hydroxysteroid dehydrogenase 1. SCDR10B was isolated from a human brain cDNA library, and was mapped to chromosome 19p13.3 by browsing the UCSC genomic database. It contains an ORF with a length of 858 bp, encoding a protein with a transmembrane helix and SDR domain. Its molecular mass and isoelectric point are predicted to be 30.8 kDa and 10.3 kDa, respectively. SCDR10B protein is highly conserved in mammals and fish. Phylogenetic tree analysis indicated that SCDR10B stands for a new subgroup in the 11β-hydroxysteroid dehydrogenase family. Northern blot analysis showed that SCDR10B was highly expressed in brain, and a strong expression signal was detected in hippocampal neurons by immunohistochemical analysis. RT-PCR and immunohistochemical analysis showed that SCDR10B was up-regulated in lung-cancer cell lines and human lung cancer. SCDR10B can catalyze the dehydrogenation of cortisol in the presence of NADP+, and therefore it is a hydroxysteroid dehydrogenase.
Dostawca treści:
Biblioteka Nauki
Artykuł
Wyświetlanie 1-10 z 177

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